CAZypedia - User contributions [en-ca]

Carbohydrate Binding Module Family 44

2026-02-09T08:48:05Z

Marie-Katherin Zuehlke:

{{CuratorApproved}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM44.html
|}
</div>


== Ligand specificities ==
CBM44, from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum''), targets β-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage β-1,3/β-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a [[Carbohydrate-binding_modules#Types|type B]] CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 104 M-1), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 104 M-1). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.

== Structural Features ==
Like many CBMs, CBM44 exhibits a typical β-sandwich fold: two antiparallel β-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding (Figure 1), as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>.

[[File:pkd-cbm44.png|thumb|200px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([{{PDBlink}}2c26 PDB 2c26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]

== Functionalities ==
Carbohydrate binding and targeting were described as functions of CBM44. While carbohydrate binding was confirmed by AGE and ITC, the [[Carbohydrate-binding modules|targeting effect]] was analyzed by the ability of CBM44 to maintain enzyme activity of [[GH44]] (Cel44A) exposed to a substrate mixture <cite>Najmudin2006</cite>. The ensemble of a [[GH44]] and a CBM44 was found in the multimodular cellulase CtCel9D-Cel44A from ''Acetivibrio thermocellus'' and ligand spectra of both modules are consistent <cite>Najmudin2006</cite>. In the targeting experiment, the fused [[GH44]]-CBM44 construct was compared to the truncated [[GH44]]. In separate xyloglucan or carboxymethylcellulose incubations, the activity of GH44-CBM44 was comparable to that of [[GH44]] alone. In a next step, substrate mixtures were used. These mixtures also contained laminarin and pustulan, which were not degraded. While [[GH44]] activity was decreased, activity was restored by [[GH44]]-CBM44. Thus, given the complex carbohydrates present in plant cell walls, CBM44 may guide the enzyme to its target sugars. Such effects have also been achieved in synthetic CBM44-enzyme chimeras, e.g. [[GH12]] or [[GH28]] <cite>#Furtado2015 #Carli2022</cite>.

== Family Firsts ==
;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase ''Ct''Cel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding β-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.
;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([{{PDBlink}}2c26 PDB 2c26]) <cite>Najmudin2006</cite>.

== References ==
<biblio>
#Najmudin2006 pmid=16314409
#Sugiyama2000 Sugiyama H, Hisamichi K, Usui T, Sakai K, Ishiyama J (2000). ''A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution.'' J Mol Struct. 2000;'''556'''(1-3):173-7. [https://doi.org/10.1016/S0022-2860(00)00630-X DOI: 10.1016/S0022-2860(00)00630-X].
#Furtado2015 pmid=25605422
#Carli2022 Carli S, Meleiro LP, Salgado JCS, Ward RJ (2022). ''Synthetic carbohydrate-binding module-endogalacturonase chimeras increase catalytic efficiency and saccharification of lignocellulose residues''. Biomass Conv Bioref. 2022. [https://doi.org/10.1007/s13399-022-02716-6 DOI: 10.1007/s13399-022-02716-6].
#Ahsan1996 pmid=8824619
#Arai2003 pmid=12511497
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM044]]

Carbohydrate Binding Module Family 102

2024-11-07T10:23:18Z

Marie-Katherin Zuehlke:

{{CuratorApproved}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM102.html
|}
</div>


== Ligand specificities ==
The dissected C-terminal CBM102IV of a surface glycan-binding protein (SGBP; containing four CBM102s I-IV, Figure 1a) of ''Christiangramia forsetii'' KT0803T binds laminarin (from ''Laminaria digitata'') and laminarin-derived oligosaccharides as determined by affinity gel electrophoresis and/or isothermal titration calorimetry <cite>Zuehlke2024</cite>. CBM102IV has a higher affinity to laminarin (Ka ~1.04 x 105 M-1) than to laminariheptaose (Ka ~1.87 x 104 M-1) and laminaripentaose (Ka ~1.39 x 104 M-1). Laminaribiose did not bind the CBM102IV. In addition, the dissected C-terminal CBM102IV has a higher affinity to laminarin than two CBM102 tandem constructs of the SGBP (Ka ~2.76 x 104 M-1 or ~3.63 x 104 M-1) and the full length SGBP (Ka ~3.09 x 104 M-1) <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM102 displays a β-sandwich fold established by two antiparallel β-sheets forming a convex and a concave face. The 3D X-ray crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP showed that, together with two expansive loops, the concave face provides a narrow cleft to accommodate laminaritriose <cite>Zuehlke2024</cite> (Figure 1b). CBM102 thus represents a [[Carbohydrate-binding_modules|type B CBM]]. Three residues located in the concave face mediate polar interactions with laminaritriose (Lys825, Glu827 and Glu837), while one aromatic residue of each loop (Tyr790, Phe861) is involved in CH-π interaction with the ligand (Figure 1c). However, the ''C. forsetii'' protein contains three additional CBM102s. Alphafold2 <cite>Mirdita2022</cite> predictions showed that two of them are highly similar to the 3D crystal structure of the C-terminal CBM102IV, but that one CBM102 is missing one of the loops shaping the pocket, which results in a very shallow cleft (Figure 2). This was speculated to represent an adaptation to highly branched laminarins <cite>Zuehlke2024</cite>.

[[File:FigSGBP.png|thumb|'''Figure 1.''' '''a''' The Alphafold2-predicted structure of the CBM102-containing SGBP of ''C. forsetii'' <cite>Zuehlke2024</cite>. The four CBM102s (I-IV, red) follow two N-terminal Ig-like domains (grey). '''b''' 3D crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP with laminaritriose (PDB ID [https://www.rcsb.org/structure/8QX6 8QX6]) <cite>Zuehlke2024</cite>. '''c''' Zooming into the binding site: residues mediating polar and CH-π interactions with laminaritriose.]]

[[File:CBM102s.png|thumb|'''Figure 2.''' Surfaces of the four CBM102s of the ''C. forsetii'' SGBP <cite>Zuehlke2024</cite>. Left: 3D crystal structure of the C-terminal CBM102IV with laminaritriose (PDB ID [https://www.rcsb.org/structure/8QX6 8QX6]). Right: Alphafold2-predicted structures (I-III). CBM102III is missing one of the groove-forming loops.]]

== Functionalities ==
The CBM102-containing SGBP is tethered to the outer membrane of ''C. forsetii'' and is abundantly produced in laminarin-grown cells <cite>Kabisch2014</cite>. With four CBM102s, the SGBP provides multiple laminarin docking sites <cite>Zuehlke2024</cite>. The protein further contains two N-terminal Ig-like domains that precede the CBM102s, which presumably act as spacers to ensure distance to the membrane and exposure of binding sites as suggested before for β-glucan-binding CBM-containing SGBPs <cite>Tamura2021</cite>. The four repeating CBM102s in the ''C. forsetii'' protein were suggested to render the SGBP an optimal 'sugar-trapping antenna' on the bacterial surface; this is supported by an elongated protein shape (''R''g 52 Å and ''D''max 178 Å) as determined by small angle X-ray scattering <cite>Zuehlke2024</cite>. Unexpectedly, isothermal titration calorimetry showed that maximum two laminarin molecules were bound by the four CBM102s and that affinity was not increased by multiple CBM102s. In bacterial metagenome-assembled genomes from phytoplankton blooms in the North Sea, CBM102 was detected together with appended catalytic modules, indicating other putative functions (for example enhancing enzyme concentration on substrate to improve catalysis) <cite>Zuehlke2024</cite>. The majority of associated catalytic modules were [[GH16]]_3s, but also rare examples of [[Glycoside_Hydrolase_Family_2|GH2]], [[GH5]]_34, [[Glycoside_Hydrolase_Family_81|GH81]], and [[Glycoside_Hydrolase_Family_162|GH162]]. Within this dataset, CBM102 also co-occurred with [[Carbohydrate_Binding_Module_Family_4|CBM4]], [[Carbohydrate_Binding_Module_Family_6|CBM6]] and [[Carbohydrate_Binding_Module_Family_103|CBM103]] in multimodular proteins. CBM102-only-proteins contained up to eight repeats of CBM102. The production of CBM102-containing proteins correlated with the course of the phytoplankton bloom, which underlines the relevance of CBM102 in marine β-glucan use.

== Family Firsts ==
;First Identified: CBM102 was first identified in an SGBP encoded in a laminarin utilization locus of ''Christiangramia forsetii'' KT0803T <cite>Zuehlke2024</cite>, a marine flavobacterium isolated from surface waters in the North Sea <cite>Eilers2001</cite>. More than 350 CBM102-containing sequences were detected in bacterial metagenome-assembled genomes (555 representative MAGs of which 201 belonged to ''Bacteroidota'') retrieved from bacterial biomass from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea. Sequences mostly belonged to Bacteroidota, but also to ''Proteobacteria'', ''Myxococcota'' and ''Actinobacteriota'' <cite>Zuehlke2024</cite>. The association with GHs (mostly [[GH16]]_3) within this dataset led to the creation of the CBM family 102.
;First Structural Characterization: The C-terminal CBM102IV of the laminarin PUL-encoded SGBP of ''C. forsetii'' KT0803T is the first structurally characterized member of the family (PDB ID [https://www.rcsb.org/structure/8QX6 8QX6]). The 3D crystal structure was obtained in complex with laminaritriose.

== References ==
<biblio>
#Zuehlke2024 pmid=38757353
#Mirdita2022 pmid=35637307
#Kabisch2014 pmid=24522261
#Tamura2021 pmid=33587952
#Eilers2001 pmid=11679337
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM102]]

Carbohydrate Binding Module Family 102

2024-11-07T10:20:12Z

Marie-Katherin Zuehlke: /* Ligand specificities */

{{CuratorApproved}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM102.html
|}
</div>


== Ligand specificities ==
The dissected C-terminal CBM102IV of a surface glycan-binding protein (SGBP; containing four CBM102s I-IV, Figure 1a) of ''Christiangramia forsetii'' KT0803T binds laminarin (from ''Laminaria digitata'') and laminarin-derived oligosaccharides as determined by affinity gel electrophoresis and/or isothermal titration calorimetry <cite>Zuehlke2024</cite>. CBM102IV has a higher affinity to laminarin (Ka ~1.04 x 105 M-1) than to laminariheptaose (Ka ~1.87 x 104 M-1) and laminaripentaose (Ka ~1.39 x 104 M-1). Laminaribiose did not bind the CBM102IV. In addition, the dissected C-terminal CBM102IV has a higher affinity to laminarin than two CBM102 tandem constructs of the SGBP (Ka ~2.76 x 104 M-1 or ~3.63 x 104 M-1) and the full length SGBP (Ka ~3.09 x 104 M-1) <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM102 displays a β-sandwich fold established by two antiparallel β-sheets forming a convex and a concave face. The 3D X-ray crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP showed that, together with two expansive loops, the concave face provides a narrow cleft to accommodate laminaritriose <cite>Zuehlke2024</cite> (Figure 1b). CBM102 thus represents a [[Carbohydrate-binding_modules|type B CBM]]. Three residues located in the concave face mediate polar interactions with laminaritriose (Lys825, Glu827 and Glu837), while one aromatic residue of each loop (Tyr790, Phe861) is involved in CH-π interaction with the ligand (Figure 1c). However, the ''C. forsetii'' protein contains three additional CBM102s. Alphafold2 <cite>Mirdita2022</cite> predictions showed that two of them are highly similar to the 3D crystal structure of the C-terminal CBM102IV, but that one CBM102 is missing one of the loops shaping the pocket, which results in a very shallow cleft (Figure 2). This was speculated to represent an adaptation to highly branched laminarins <cite>Zuehlke2024</cite>.

[[File:FigSGBP.png|thumb|'''Figure 1.''' '''a''' The Alphafold2-predicted structure of the CBM102-containing SGBP of ''C. forsetii'' <cite>Zuehlke2024</cite>. The four CBM102s (I-IV, red) follow two N-terminal Ig-like domains (grey). '''b''' 3D crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]) <cite>Zuehlke2024</cite>. '''c''' Zooming into the binding site: residues mediating polar and CH-π interactions with laminaritriose.]]

[[File:CBM102s.png|thumb|'''Figure 2.''' Surfaces of the four CBM102s of the ''C. forsetii'' SGBP <cite>Zuehlke2024</cite>. Left: 3D crystal structure of the C-terminal CBM102IV with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). Right: Alphafold2-predicted structures (I-III). CBM102III is missing one of the groove-forming loops.]]

== Functionalities ==
The CBM102-containing SGBP is tethered to the outer membrane of ''C. forsetii'' and is abundantly produced in laminarin-grown cells <cite>Kabisch2014</cite>. With four CBM102s, the SGBP provides multiple laminarin docking sites <cite>Zuehlke2024</cite>. The protein further contains two N-terminal Ig-like domains that precede the CBM102s, which presumably act as spacers to ensure distance to the membrane and exposure of binding sites as suggested before for β-glucan-binding CBM-containing SGBPs <cite>Tamura2021</cite>. The four repeating CBM102s in the ''C. forsetii'' protein were suggested to render the SGBP an optimal 'sugar-trapping antenna' on the bacterial surface; this is supported by an elongated protein shape (''R''g 52 Å and ''D''max 178 Å) as determined by small angle X-ray scattering <cite>Zuehlke2024</cite>. Unexpectedly, isothermal titration calorimetry showed that maximum two laminarin molecules were bound by the four CBM102s and that affinity was not increased by multiple CBM102s. In bacterial metagenome-assembled genomes from phytoplankton blooms in the North Sea, CBM102 was detected together with appended catalytic modules, indicating other putative functions (for example enhancing enzyme concentration on substrate to improve catalysis) <cite>Zuehlke2024</cite>. The majority of associated catalytic modules were [[GH16]]_3s, but also rare examples of [[Glycoside_Hydrolase_Family_2|GH2]], [[GH5]]_34, [[Glycoside_Hydrolase_Family_81|GH81]], and [[Glycoside_Hydrolase_Family_162|GH162]]. Within this dataset, CBM102 also co-occurred with [[Carbohydrate_Binding_Module_Family_4|CBM4]], [[Carbohydrate_Binding_Module_Family_6|CBM6]] and [[Carbohydrate_Binding_Module_Family_103|CBM103]] in multimodular proteins. CBM102-only-proteins contained up to eight repeats of CBM102. The production of CBM102-containing proteins correlated with the course of the phytoplankton bloom, which underlines the relevance of CBM102 in marine β-glucan use.

== Family Firsts ==
;First Identified: CBM102 was first identified in an SGBP encoded in a laminarin utilization locus of ''Christiangramia forsetii'' KT0803T <cite>Zuehlke2024</cite>, a marine flavobacterium isolated from surface waters in the North Sea <cite>Eilers2001</cite>. More than 350 CBM102-containing sequences were detected in bacterial metagenome-assembled genomes (555 representative MAGs of which 201 belonged to ''Bacteroidota'') retrieved from bacterial biomass from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea. Sequences mostly belonged to Bacteroidota, but also to ''Proteobacteria'', ''Myxococcota'' and ''Actinobacteriota'' <cite>Zuehlke2024</cite>. The association with GHs (mostly [[GH16]]_3) within this dataset led to the creation of the CBM family 102.
;First Structural Characterization: The C-terminal CBM102IV of the laminarin PUL-encoded SGBP of ''C. forsetii'' KT0803T is the first structurally characterized member of the family (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). The 3D crystal structure was obtained in complex with laminaritriose.

== References ==
<biblio>
#Zuehlke2024 pmid=38757353
#Mirdita2022 pmid=35637307
#Kabisch2014 pmid=24522261
#Tamura2021 pmid=33587952
#Eilers2001 pmid=11679337
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM102]]

Carbohydrate Binding Module Family 102

2024-11-07T10:19:13Z

Marie-Katherin Zuehlke: /* Structural Features */

{{CuratorApproved}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM102.html
|}
</div>


== Ligand specificities ==
The dissected C-terminal CBM102IV of a surface glycan-binding protein (SGBP; containing four CBM102s I-IV) of ''Christiangramia forsetii'' KT0803T binds laminarin (from ''Laminaria digitata'') and laminarin-derived oligosaccharides as determined by affinity gel electrophoresis and/or isothermal titration calorimetry <cite>Zuehlke2024</cite>. CBM102IV has a higher affinity to laminarin (Ka ~1.04 x 105 M-1) than to laminariheptaose (Ka ~1.87 x 104 M-1) and laminaripentaose (Ka ~1.39 x 104 M-1). Laminaribiose did not bind the CBM102IV. In addition, the dissected C-terminal CBM102IV has a higher affinity to laminarin than two CBM102 tandem constructs of the SGBP (Ka ~2.76 x 104 M-1 or ~3.63 x 104 M-1) and the full length SGBP (Ka ~3.09 x 104 M-1) <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM102 displays a β-sandwich fold established by two antiparallel β-sheets forming a convex and a concave face. The 3D X-ray crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP showed that, together with two expansive loops, the concave face provides a narrow cleft to accommodate laminaritriose <cite>Zuehlke2024</cite> (Figure 1b). CBM102 thus represents a [[Carbohydrate-binding_modules|type B CBM]]. Three residues located in the concave face mediate polar interactions with laminaritriose (Lys825, Glu827 and Glu837), while one aromatic residue of each loop (Tyr790, Phe861) is involved in CH-π interaction with the ligand (Figure 1c). However, the ''C. forsetii'' protein contains three additional CBM102s. Alphafold2 <cite>Mirdita2022</cite> predictions showed that two of them are highly similar to the 3D crystal structure of the C-terminal CBM102IV, but that one CBM102 is missing one of the loops shaping the pocket, which results in a very shallow cleft (Figure 2). This was speculated to represent an adaptation to highly branched laminarins <cite>Zuehlke2024</cite>.

[[File:FigSGBP.png|thumb|'''Figure 1.''' '''a''' The Alphafold2-predicted structure of the CBM102-containing SGBP of ''C. forsetii'' <cite>Zuehlke2024</cite>. The four CBM102s (I-IV, red) follow two N-terminal Ig-like domains (grey). '''b''' 3D crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]) <cite>Zuehlke2024</cite>. '''c''' Zooming into the binding site: residues mediating polar and CH-π interactions with laminaritriose.]]

[[File:CBM102s.png|thumb|'''Figure 2.''' Surfaces of the four CBM102s of the ''C. forsetii'' SGBP <cite>Zuehlke2024</cite>. Left: 3D crystal structure of the C-terminal CBM102IV with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). Right: Alphafold2-predicted structures (I-III). CBM102III is missing one of the groove-forming loops.]]

== Functionalities ==
The CBM102-containing SGBP is tethered to the outer membrane of ''C. forsetii'' and is abundantly produced in laminarin-grown cells <cite>Kabisch2014</cite>. With four CBM102s, the SGBP provides multiple laminarin docking sites <cite>Zuehlke2024</cite>. The protein further contains two N-terminal Ig-like domains that precede the CBM102s, which presumably act as spacers to ensure distance to the membrane and exposure of binding sites as suggested before for β-glucan-binding CBM-containing SGBPs <cite>Tamura2021</cite>. The four repeating CBM102s in the ''C. forsetii'' protein were suggested to render the SGBP an optimal 'sugar-trapping antenna' on the bacterial surface; this is supported by an elongated protein shape (''R''g 52 Å and ''D''max 178 Å) as determined by small angle X-ray scattering <cite>Zuehlke2024</cite>. Unexpectedly, isothermal titration calorimetry showed that maximum two laminarin molecules were bound by the four CBM102s and that affinity was not increased by multiple CBM102s. In bacterial metagenome-assembled genomes from phytoplankton blooms in the North Sea, CBM102 was detected together with appended catalytic modules, indicating other putative functions (for example enhancing enzyme concentration on substrate to improve catalysis) <cite>Zuehlke2024</cite>. The majority of associated catalytic modules were [[GH16]]_3s, but also rare examples of [[Glycoside_Hydrolase_Family_2|GH2]], [[GH5]]_34, [[Glycoside_Hydrolase_Family_81|GH81]], and [[Glycoside_Hydrolase_Family_162|GH162]]. Within this dataset, CBM102 also co-occurred with [[Carbohydrate_Binding_Module_Family_4|CBM4]], [[Carbohydrate_Binding_Module_Family_6|CBM6]] and [[Carbohydrate_Binding_Module_Family_103|CBM103]] in multimodular proteins. CBM102-only-proteins contained up to eight repeats of CBM102. The production of CBM102-containing proteins correlated with the course of the phytoplankton bloom, which underlines the relevance of CBM102 in marine β-glucan use.

== Family Firsts ==
;First Identified: CBM102 was first identified in an SGBP encoded in a laminarin utilization locus of ''Christiangramia forsetii'' KT0803T <cite>Zuehlke2024</cite>, a marine flavobacterium isolated from surface waters in the North Sea <cite>Eilers2001</cite>. More than 350 CBM102-containing sequences were detected in bacterial metagenome-assembled genomes (555 representative MAGs of which 201 belonged to ''Bacteroidota'') retrieved from bacterial biomass from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea. Sequences mostly belonged to Bacteroidota, but also to ''Proteobacteria'', ''Myxococcota'' and ''Actinobacteriota'' <cite>Zuehlke2024</cite>. The association with GHs (mostly [[GH16]]_3) within this dataset led to the creation of the CBM family 102.
;First Structural Characterization: The C-terminal CBM102IV of the laminarin PUL-encoded SGBP of ''C. forsetii'' KT0803T is the first structurally characterized member of the family (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). The 3D crystal structure was obtained in complex with laminaritriose.

== References ==
<biblio>
#Zuehlke2024 pmid=38757353
#Mirdita2022 pmid=35637307
#Kabisch2014 pmid=24522261
#Tamura2021 pmid=33587952
#Eilers2001 pmid=11679337
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM102]]

File:FigSGBP.png

2024-11-07T10:12:56Z

Marie-Katherin Zuehlke: Marie-Katherin Zuehlke uploaded a new version of File:FigSGBP.png

Full-length CBM102-containing SGBP and dissected CBM102-IV highlighting the binding site

File:CBM102s.png

2024-11-07T10:03:08Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 102

2024-11-07T09:45:58Z

Marie-Katherin Zuehlke:

{{CuratorApproved}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM102.html
|}
</div>


== Ligand specificities ==
The dissected C-terminal CBM102IV of a surface glycan-binding protein (SGBP; containing four CBM102s I-IV) of ''Christiangramia forsetii'' KT0803T binds laminarin (from ''Laminaria digitata'') and laminarin-derived oligosaccharides as determined by affinity gel electrophoresis and/or isothermal titration calorimetry <cite>Zuehlke2024</cite>. CBM102IV has a higher affinity to laminarin (Ka ~1.04 x 105 M-1) than to laminariheptaose (Ka ~1.87 x 104 M-1) and laminaripentaose (Ka ~1.39 x 104 M-1). Laminaribiose did not bind the CBM102IV. In addition, the dissected C-terminal CBM102IV has a higher affinity to laminarin than two CBM102 tandem constructs of the SGBP (Ka ~2.76 x 104 M-1 or ~3.63 x 104 M-1) and the full length SGBP (Ka ~3.09 x 104 M-1) <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM102 displays a β-sandwich fold established by two antiparallel β-sheets forming a convex and a concave face. The 3D X-ray crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP showed that, together with two expansive loops, the concave face provides a narrow cleft to accommodate laminaritriose <cite>Zuehlke2024</cite> (Figure 1). CBM102 thus represents a [[Carbohydrate-binding_modules|type B CBM]]. Three residues located in the concave face mediate polar interactions with laminaritriose (Lys825, Glu827 and Glu837), while one aromatic residue of each loop (Tyr790, Phe861) is involved in CH-π interaction with the ligand. However, the ''C. forsetii'' protein contains three additional CBM102s. Alphafold2 <cite>Mirdita2022</cite> predictions showed that two of them are highly similar to the 3D crystal structure of the C-terminal CBM102IV, but that one CBM102 is missing one of the loops shaping the pocket, which results in a very shallow cleft (Figure 2). This was speculated to represent an adaptation to highly branched laminarins <cite>Zuehlke2024</cite>.

[[File:Fig.1.png|thumb|'''Figure 1.''' 3D crystal structure of the C-terminal CBM102IV of the ''C. forsetii'' SGBP with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]) <cite>Zuehlke2024</cite>. Highlighted are interacting residues.]]

[[File:Fig.2.png|thumb|'''Figure 2.''' Surfaces of the four CBM102s of the ''C. forsetii'' SGBP <cite>Zuehlke2024</cite>. Left: 3D crystal structure of the C-terminal CBM102IV with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). Right: Alphafold2-predicted structures (I-III). CBM102III is missing one of the groove-forming loops.]]
== Functionalities ==
The CBM102-containing SGBP is tethered to the outer membrane of ''C. forsetii'' and is abundantly produced in laminarin-grown cells <cite>Kabisch2014</cite>. With four CBM102s, the SGBP provides multiple laminarin docking sites <cite>Zuehlke2024</cite>. The protein further contains two N-terminal Ig-like domains that precede the CBM102s, which presumably act as spacers to ensure distance to the membrane and exposure of binding sites as suggested before for β-glucan-binding CBM-containing SGBPs <cite>Tamura2021</cite>. The four repeating CBM102s in the ''C. forsetii'' protein were suggested to render the SGBP an optimal 'sugar-trapping antenna' on the bacterial surface; this is supported by an elongated protein shape (''R''g 52 Å and ''D''max 178 Å) as determined by small angle X-ray scattering <cite>Zuehlke2024</cite>. Unexpectedly, isothermal titration calorimetry showed that maximum two laminarin molecules were bound by the four CBM102s and that affinity was not increased by multiple CBM102s. In bacterial metagenome-assembled genomes from phytoplankton blooms in the North Sea, CBM102 was detected together with appended catalytic modules, indicating other putative functions (for example enhancing enzyme concentration on substrate to improve catalysis) <cite>Zuehlke2024</cite>. The majority of associated catalytic modules were [[GH16]]_3s, but also rare examples of [[Glycoside_Hydrolase_Family_2|GH2]], [[GH5]]_34, [[Glycoside_Hydrolase_Family_81|GH81]], and [[Glycoside_Hydrolase_Family_162|GH162]]. Within this dataset, CBM102 also co-occurred with [[Carbohydrate_Binding_Module_Family_4|CBM4]], [[Carbohydrate_Binding_Module_Family_6|CBM6]] and [[Carbohydrate_Binding_Module_Family_103|CBM103]] in multimodular proteins. CBM102-only-proteins contained up to eight repeats of CBM102. The production of CBM102-containing proteins correlated with the course of the phytoplankton bloom, which underlines the relevance of CBM102 in marine β-glucan use.

== Family Firsts ==
;First Identified: CBM102 was first identified in an SGBP encoded in a laminarin utilization locus of ''Christiangramia forsetii'' KT0803T <cite>Zuehlke2024</cite>, a marine flavobacterium isolated from surface waters in the North Sea <cite>Eilers2001</cite>. More than 350 CBM102-containing sequences were detected in bacterial metagenome-assembled genomes (555 representative MAGs of which 201 belonged to ''Bacteroidota'') retrieved from bacterial biomass from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea. Sequences mostly belonged to Bacteroidota, but also to ''Proteobacteria'', ''Myxococcota'' and ''Actinobacteriota'' <cite>Zuehlke2024</cite>. The association with GHs (mostly [[GH16]]_3) within this dataset led to the creation of the CBM family 102.
;First Structural Characterization: The C-terminal CBM102IV of the laminarin PUL-encoded SGBP of ''C. forsetii'' KT0803T is the first structurally characterized member of the family (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). The 3D crystal structure was obtained in complex with laminaritriose.

== References ==
<biblio>
#Zuehlke2024 pmid=38757353
#Mirdita2022 pmid=35637307
#Kabisch2014 pmid=24522261
#Tamura2021 pmid=33587952
#Eilers2001 pmid=11679337
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM102]]

Carbohydrate Binding Module Family 103

2024-11-07T09:31:36Z

Marie-Katherin Zuehlke: /* Functionalities */

{{CuratorApproved}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM103.html
|}
</div>


== Ligand specificities ==
The CBM103-containing surface glycan-binding protein (SGBP) of ''Bacteroides fluxus ''(BfSGBP-B), a strain from the human intestinal tract, binds laminarin (''Laminaria digitata'') and mixed-linkage β(1,3)/β(1,4)-glucans (MLG, from Barley) as well as MLG oligosaccharides <cite>Dejean2020 Tamura2021</cite>. The protein binds laminarin and MLG with similar affinity (Ka 8.63 X 104 M-1 and Ka 8.56 X 104 M-1, respectively) <cite>Dejean2020</cite>. Binding of laminarin-derived oligosaccharides required a degree of polymerization (DP) of more than two and affinities ranged from Kd 3.63-7.61 x 10-5 M (for DP 3-6) <cite>Tamura2021</cite>. DP3 and DP4 derived from MLG bound with similar affinities (Kd 1.23 x 10-5 M or 1.16 x 10-5 M, respectively), but a β(1,3)-glucosyl linkage at the reducing end was essential for binding.

Similarly, a dissected CBM103 of a multimodular laminarinase ([[GH16]]_3) from the marine flavobacterium ''Christiangramia forsetii'' KT0803T bound laminarin (''Laminaria digitata'') and MLG (from Icelandic moss, lichenan) as confirmed by affinity gel electrophoresis <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM103 of the ''B. fluxus'' SGBP (BfSGBP-B) displays a β-barrel fold with an additional β-strand pair and two short α-helices <cite>Tamura2021</cite> (Figure 1a). 3D crystal structures showed that reducing ends of laminarin- or MLG-derived oligosaccharides bind on the top face of the β-barrel, which provides a 'shallow binding canyon'. Therefore, CBM103 classifies as a [[Carbohydrate-binding_modules|type C CBM]]. Polar- and CH-π-interactions mediate binding to trioses derived from laminarin and MLG. Trp164, which interacts with the glucose residue at the third subsite (Figure 1b), and Trp165, Lys172 and Asp221, which interact with the reducing-end glucose at the terminal subsite, were essential for binding <cite>Tamura2021</cite>. Replacing the individual residues with alanine abolished binding in each case, as shown by affinity gel electrophoresis.

In the ''B. fluxus'' SGBP, the CBM103 follows an N-terminal ‘PKD’ domain (Figure 1a).

[[File:bfluxus_3.png|thumb|'''Figure 1.''' 3D crystal structure of the CBM103-containing SGBP of ''Bacteroides fluxus''. '''a''' The CBM103 (blue) is preceded by an N-terminal 'PKD' domain (light violet) <cite>Tamura2021</cite>. Mixed-linkage glucotriose (pink) binds on a platform of CBM103 (PDB ID [{{PDBlink}}7KV6 7KV6]). '''b''' Residues of the binding site interacting with mixed-linkage glucotriose <cite>Tamura2021</cite>. The terminal subsite (interaction subsite 1), which is interacting with the reducing-end glucose residue, is encircled.]]

== Functionalities ==
The CBM103-containing SGBP of ''B. fluxus'' (BfSGBP-B) was suggested to support glycan recognition and recruitment to the bacterial cellular surface in the human intestinal tract <cite>Tamura2021</cite>. Similarly, in 555 representative bacterial metagenome assembled genomes retrieved from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea, 43 CBM103-only sequences were identified, some of which might function as SGBPs <cite>Zuehlke2024</cite>. All detected CBM103-containing sequences (82) belonged to the phylum Bacteroidota and covered also 17 CBM103-[[Carbohydrate_Binding_Module_Family_102|CBM102]] combinations, 21 CBM103-[[GH16]]_3 combinations as well as one CBM103-[[Carbohydrate_Binding_Module_Family_6|CBM6]]-[[GH5]]_46 combination. In ''C. forsetii'', the CBM103 is attached to a [[GH16]]_3, which was suggested to increase enzyme concentration and thus catalysis <cite>Zuehlke2024</cite>.

== Family Firsts ==
;First Identified: CBM103 was first identified in an SGBP of ''B. fluxus'' (BfSGBP-B) <cite>Tamura2021</cite>, although binding of the SGBP to β-glucans was shown before <cite>Dejean2020</cite>. Later, a CBM103-containing [[GH16]]_3 of ''C. forsetii'' led to the creation of the CBM family 103 <cite>Zuehlke2024</cite>.

;First Structural Characterization: The CBM103-containing SGBP of ''B. fluxus'' represents the first 3D crystal structure, with and without ligands (PDB ID [https://www.rcsb.org/structure/7KV5 7KV5] without ligand, PDB ID [https://www.rcsb.org/structure/7KV6 7KV6] with DP3 from MLG, PDB ID [https://www.rcsb.org/structure/7KV7 7KV7] with DP3 from laminarin) <cite>Tamura2021</cite>.
== References ==
<biblio>

#Dejean2020 pmid=32265336
#Tamura2021 pmid=33587952
#Zuehlke2024 pmid=38757353
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM103]]

Carbohydrate Binding Module Family 103

2024-11-07T08:45:34Z

Marie-Katherin Zuehlke: /* Structural Features */

{{CuratorApproved}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM103.html
|}
</div>


== Ligand specificities ==
The CBM103-containing surface glycan-binding protein (SGBP) of ''Bacteroides fluxus ''(BfSGBP-B), a strain from the human intestinal tract, binds laminarin (''Laminaria digitata'') and mixed-linkage β(1,3)/β(1,4)-glucans (MLG, from Barley) as well as MLG oligosaccharides <cite>Dejean2020 Tamura2021</cite>. The protein binds laminarin and MLG with similar affinity (Ka 8.63 X 104 M-1 and Ka 8.56 X 104 M-1, respectively) <cite>Dejean2020</cite>. Binding of laminarin-derived oligosaccharides required a degree of polymerization (DP) of more than two and affinities ranged from Kd 3.63-7.61 x 10-5 M (for DP 3-6) <cite>Tamura2021</cite>. DP3 and DP4 derived from MLG bound with similar affinities (Kd 1.23 x 10-5 M or 1.16 x 10-5 M, respectively), but a β(1,3)-glucosyl linkage at the reducing end was essential for binding.

Similarly, a dissected CBM103 of a multimodular laminarinase ([[GH16]]_3) from the marine flavobacterium ''Christiangramia forsetii'' KT0803T bound laminarin (''Laminaria digitata'') and MLG (from Icelandic moss, lichenan) as confirmed by affinity gel electrophoresis <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM103 of the ''B. fluxus'' SGBP (BfSGBP-B) displays a β-barrel fold with an additional β-strand pair and two short α-helices <cite>Tamura2021</cite> (Figure 1a). 3D crystal structures showed that reducing ends of laminarin- or MLG-derived oligosaccharides bind on the top face of the β-barrel, which provides a 'shallow binding canyon'. Therefore, CBM103 classifies as a [[Carbohydrate-binding_modules|type C CBM]]. Polar- and CH-π-interactions mediate binding to trioses derived from laminarin and MLG. Trp164, which interacts with the glucose residue at the third subsite (Figure 1b), and Trp165, Lys172 and Asp221, which interact with the reducing-end glucose at the terminal subsite, were essential for binding <cite>Tamura2021</cite>. Replacing the individual residues with alanine abolished binding in each case, as shown by affinity gel electrophoresis.

In the ''B. fluxus'' SGBP, the CBM103 follows an N-terminal ‘PKD’ domain (Figure 1a).

[[File:bfluxus_3.png|thumb|'''Figure 1.''' 3D crystal structure of the CBM103-containing SGBP of ''Bacteroides fluxus''. '''a''' The CBM103 (blue) is preceded by an N-terminal 'PKD' domain (light violet) <cite>Tamura2021</cite>. Mixed-linkage glucotriose (pink) binds on a platform of CBM103 (PDB ID [{{PDBlink}}7KV6 7KV6]). '''b''' Residues of the binding site interacting with mixed-linkage glucotriose <cite>Tamura2021</cite>. The terminal subsite (interaction subsite 1), which is interacting with the reducing-end glucose residue, is encircled.]]

== Functionalities ==
The CBM103-containing SGBP of ''B. fluxus'' (BfSGBP-B) was suggested to support glycan recognition and recruitment to the bacterial cellular surface in the human intestinal tract <cite>Tamura2021</cite>. Similarly, in 555 representative bacterial metagenome assembled genomes retrieved from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea, 43 CBM103-only sequences were identified, some of which might function as SGBPs <cite>Zuehlke2024</cite>. All detected CBM103-containing sequences (82) belonged to the phylum Bacteroidota and covered also 17 CBM103-[[Carbohydrate_Binding_Module_Family_102|CBM102]] combinations, 21 CBM103-[[GH16]]_3 combinations as well as one CBM103-[[Carbohydrate_Binding_Module_Family_6|CBM6]]-[[GH5]]_46 combination. In ''C. forsetii'', the CBM103 is attached to a [[GH16]]_3, which was suggested to increase catalysis <cite>Zuehlke2024</cite>.

== Family Firsts ==
;First Identified: CBM103 was first identified in an SGBP of ''B. fluxus'' (BfSGBP-B) <cite>Tamura2021</cite>, although binding of the SGBP to β-glucans was shown before <cite>Dejean2020</cite>. Later, a CBM103-containing [[GH16]]_3 of ''C. forsetii'' led to the creation of the CBM family 103 <cite>Zuehlke2024</cite>.

;First Structural Characterization: The CBM103-containing SGBP of ''B. fluxus'' represents the first 3D crystal structure, with and without ligands (PDB ID [https://www.rcsb.org/structure/7KV5 7KV5] without ligand, PDB ID [https://www.rcsb.org/structure/7KV6 7KV6] with DP3 from MLG, PDB ID [https://www.rcsb.org/structure/7KV7 7KV7] with DP3 from laminarin) <cite>Tamura2021</cite>.
== References ==
<biblio>

#Dejean2020 pmid=32265336
#Tamura2021 pmid=33587952
#Zuehlke2024 pmid=38757353
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM103]]

File:Bfluxus 3.png

2024-11-07T08:03:37Z

Marie-Katherin Zuehlke:

File:FigSGBP.png

2024-11-06T13:30:06Z

Marie-Katherin Zuehlke:

Full-length CBM102-containing SGBP and dissected CBM102-IV highlighting the binding site

File:Fig.1.png

2024-11-06T13:23:32Z

Marie-Katherin Zuehlke: Marie-Katherin Zuehlke reverted File:Fig.1.png to an old version

3D crystal structure of the C-terminal CBM102 of the C. forsetii SGBP together with laminaritriose.

File:Fig.1.png

2024-11-06T13:19:43Z

Marie-Katherin Zuehlke: Marie-Katherin Zuehlke uploaded a new version of File:Fig.1.png

3D crystal structure of the C-terminal CBM102 of the C. forsetii SGBP together with laminaritriose.

Carbohydrate Binding Module Family 103

2024-09-12T14:11:47Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM103.html
|}
</div>


== Ligand specificities ==
The CBM103-containing surface glycan-binding protein (SGBP) of ''Bacteroides fluxus ''(BfSGBP-B), a strain from the human intestinal tract, binds laminarin (''Laminaria digitata'') and mixed-linkage β(1,3)/β(1,4)-glucans (MLG, from Barley) as well as oligosaccharides thereof <cite>Dejean2020 Tamura2021</cite>. The protein binds laminarin and MLG with similar affinity (Ka 8.63 X 104 M-1 and Ka 8.56 X 104 M-1, respectively) <cite>Dejean2020</cite>. Binding of laminarin-derived oligosaccharides required a degree of polymerization (DP) of more than two and affinities ranged from Kd 3.63-7.61 x 10-5 M (DP3-6) <cite>Tamura2021</cite>. DP3 and DP4 derived from MLG were binding with similar affinities (Kd 1.23 x 10-5 M or 1.16 x 10-5 M, respectively), but a β(1,3)-glucosyl linkage at the reducing end was essential for binding.

Similarly, a dissected CBM103 of a multimodular laminarinase (GH16_3) of the marine flavobacterium ''Christiangramia forsetii'' KT0803T was binding laminarin (''Laminaria digitata'') and MLG (from Icelandic moss, lichenan) as confirmed by affinity gel electrophoresis <cite>Zuehlke2024</cite>.
== Structural Features ==
The CBM103 of the ''B. fluxus'' SGBP (BfSGBP-B) displays a β-barrel fold with an additional β-strand pair and two short α-helices <cite>Tamura2021</cite> (Figure 1). 3D crystal structures showed that reducing ends of laminarin- or MLG-derived oligosaccharides bind on the top face of the β-barrel, which provides a 'shallow binding canyon'. Therefore, CBM103 classifies as a [[Carbohydrate-binding_modules|type C CBM]]. Polar- and CH-π-interactions mediate binding to trioses derived from laminarin and MLG, with Trp164 (third subsite), Trp165, Lys172 and Asp221 (all terminal subsite) demonstrated to be indispensable <cite>Tamura2021</cite>. In the ''B. fluxus'' SGBP, the CBM103 follows an N-terminal ‘PKD’ domain.

[[File:Bfluxus.png|thumb|'''Figure 1.''' 3D crystal structure of the CBM103-containing SGBP of ''Bacteroides fluxus'', which is preceded by an N-terminal 'PKD' domain (light blue) <cite>Tamura2021</cite>. Mixed-linkage glucotriose (pink) binds on a platform of CBM103 (PDB ID [{{PDBlink}}7KV6 7KV6])]]

== Functionalities ==
The CBM103-containing SGBP of ''B. fluxus'' (BfSGBP-B) was suggested to support glycan recognition and its recruiting to the cellular surface in the human intestinal tract <cite>Tamura2021</cite>. Similarly, in 555 representative bacterial metagenome assembled genomes retrieved from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea, 43 CBM103-only sequences were identified, some of which might function as SGBPs <cite>Zuehlke2024</cite>. All detected CBM103-containing sequences (82) belonged to the phylum ''Bacteroidota'' and covered also 17 CBM103-[[Carbohydrate_Binding_Module_Family_102|CBM102]] combinations, 21 CBM103-GH16_3 combinations as well as one CBM103-[[Carbohydrate_Binding_Module_Family_6|CBM6]]-GH5_46 combination. In ''C. forsetii'', the CBM103 is attached to a GH16_3, which was suggested to increase catalysis <cite>Zuehlke2024</cite>.

== Family Firsts ==
;First Identified
CBM103 was first identified in an SGBP of ''B. fluxus'' (BfSGBP-B) <cite>Tamura2021</cite>, although binding of the SGBP to β-glucans was shown before <cite>Dejean2020</cite>. Later, a CBM103-containing GH16_3 of ''C. forsetii'' led to the creation of the CBM family 103 <cite>Zuehlke2024</cite>.

;First Structural Characterization
The CBM103-containing SGBP of ''B. fluxus'' represents the first 3D crystal structure, with and without ligands (PDB ID [https://www.rcsb.org/structure/7KV5 7KV5] without ligand, PDB ID [https://www.rcsb.org/structure/7KV6 7KV6] with DP3 from MLG, PDB ID [https://www.rcsb.org/structure/7KV7 7KV7] with DP3 from laminarin) <cite>Tamura2021</cite>.
== References ==
<biblio>

#Dejean2020 pmid=32265336

#Tamura2021 pmid=33587952

#Zuehlke2024 pmid=38757353
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM103]]

Carbohydrate Binding Module Family 102

2024-09-12T13:25:05Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM102.html
|}
</div>


== Ligand specificities ==
The dissected C-terminal CBM102 of a surface glycan-binding protein (SGBP; containing four CBM102s) of ''Christiangramia forsetii'' KT0803T is binding laminarin (from ''Laminaria digitata'') and laminarin-derived oligosaccharides, which was confirmed by affinity gel electrophoresis and/or isothermal titration calorimetry <cite>Zuehlke2024</cite>. The CBM102 had a higher affinity to laminarin (Ka ~1.04 x 105 M-1) than to laminariheptaose (Ka ~1.87 x 104 M-1) and laminaripentaose (Ka ~1.39 x 104 M-1). Laminaribiose was not binding.

In addition, the dissected C-terminal CBM102 had a higher affinity to laminarin than two CBM102 tandem constructs of the SGBP (Ka ~2.76 x 104 M-1 or ~3.63 x 104 M-1) and the full length SGBP (Ka ~3.09 x 104 M-1) <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM102 displays a β-sandwich fold established by two antiparallel β-sheets forming a convex and a concave face. The 3D X-ray crystal structure of the C-terminal CBM102 of the ''C. forsetii'' SGBP showed that together with two expansive loops, the concave face provides a narrow cleft to accommodate laminaritriose <cite>Zuehlke2024</cite> (Figure 1). CBM102 thus represents a [[Carbohydrate-binding_modules|type B CBM]]. Three residues located in the concave face mediate polar interactions with laminaritriose (Lys825, Glu827 and Glu837), while one aromatic residue of each loop (Tyr790, Phe861) is involved in CH-π interaction with the ligand. However, the ''C. forsetii'' protein contains three additional CBM102s. Alphafold2 <cite>Mirdita2022</cite> predictions showed that two of them are highly similar to the 3D crystal structure of the C-terminal CBM102, but that one CBM102 is missing one of the loops shaping the pocket, which results in a very shallow cleft (Figure 2). This was speculated to represent an adaptation to highly branched laminarins <cite>Zuehlke2024</cite>.

[[File:Fig.1.png|thumb|'''Figure 1.''' 3D crystal structure of the C-terminal CBM102 of the ''C. forsetii'' SGBP with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]) <cite>Zuehlke2024</cite>. Highlighted are interacting residues.]]

[[File:Fig.2.png|thumb|'''Figure 2.''' Surfaces of the four CBM102s of the ''C. forsetii'' SGBP <cite>Zuehlke2024</cite>. Left: 3D crystal structure of the C-terminal CBM102 (IV) with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). Right: Alphafold2-predicted structures (I-III). Module III is missing one of the loops, which form the groove.]]
== Functionalities ==
The CBM102-containing SGBP is tethered to the outer membrane of ''C. forsetii'' and is abundantly produced in laminarin-grown cells <cite>Kabisch2014</cite>. With four CBM102s, the SGBP provides multiple laminarin docking sites <cite>Zuehlke2024</cite>. The protein further contains two N-terminal Ig-like domains that precede the CBM102s, which presumably act as spacers to ensure distance to the membrane and exposure of binding sites as suggested before for β-glucan-binding CBM-containing SGBPs <cite>Tamura2021</cite>. The multiplicity of CBM102 in the ''C. forsetii'' protein was suggested to render the SGBP an optimal 'sugar-trapping antenna' on the bacterial surface, which was supported by an elongated protein shape as determined by small angle X ray scattering <cite>Zuehlke2024</cite>. However, isothermal titration calorimetry showed that two laminarin molecules were binding at maximum and that affinity was not increased by multiple CBM102s. In bacterial metagenome-assembled genomes from phytoplankton blooms in the North Sea, CBM102 was detected together with appended catalytic modules, indicating also other functions (increased catalysis) <cite>Zuehlke2024</cite>. The majority of associated catalytic modules were GH16_3s, but also rare examples of [[Glycoside_Hydrolase_Family_2|GH2]], GH5_34, [[Glycoside_Hydrolase_Family_81|GH81]], [[Glycoside_Hydrolase_Family_162|GH162]]. Within this dataset, CBM102 also co-occurred with [[Carbohydrate_Binding_Module_Family_4|CBM4]], [[Carbohydrate_Binding_Module_Family_6|CBM6]] and [[Carbohydrate_Binding_Module_Family_103|CBM103]] in multimodular proteins. CBM102-only-proteins contained up to eight repeats of CBM102. The production of CBM102-containing proteins correlated with the course of the phytoplankton bloom, which underlines the relevance of CBM102 in marine β-glucan use.

== Family Firsts ==
;First Identified
CBM102 was first identified in an SGBP encoded in a laminarin utilization locus of ''Christiangramia forsetii'' KT0803T <cite>Zuehlke2024</cite>, a marine flavobacterium isolated from surface waters in the North Sea <cite>Eilers2001</cite>. More than 350 CBM102-containing sequences were detected in bacterial metagenome-assembled genomes (555 representative MAGs of which 201 belonged to ''Bacteroidota'') retrieved from bacterial biomass from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea. Sequences mostly belonged to ''Bacteroidota'', but also to ''Proteobacteria'', ''Myxococcota'' and ''Actinobacteriota'' <cite>Zuehlke2024</cite>. The association with GHs (mostly GH16_3) within this dataset led to the creation of the CBM family 102.
;First Structural Characterization
The C-terminal CBM102 of the laminarin PUL-encoded SGBP of ''C. forsetii'' KT0803T is the first structurally characterized member of the family (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). The 3D crystal structure was obtained in complex with laminaritriose.

== References ==
<biblio>
#Zuehlke2024 pmid=38757353
#Mirdita2022 pmid=35637307
#Kabisch2014 pmid=24522261
#Tamura2021 pmid=33587952
#Eilers2001 pmid=11679337
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM102]]

Carbohydrate Binding Module Family 102

2024-09-09T15:37:43Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM102.html
|}
</div>


== Ligand specificities ==
The dissected C-terminal CBM102 of a surface glycan-binding protein (SGBP; containing four CBM102s) of ''Christiangramia forsetii'' KT0803T is binding laminarin (from ''Laminaria digitata'') and laminarin-derived oligosaccharides, which was confirmed by affinity gel electrophoresis and/or isothermal titration calorimetry <cite>Zuehlke2024</cite>. The CBM102 had a higher affinity to laminarin (Ka ~1.04 x 105 M-1) than to laminariheptaose (Ka ~1.87 x 104 M-1) and laminaripentaose (Ka ~1.39 x 104 M-1). Laminaribiose was not binding.

In addition, the dissected C-terminal CBM102 had a higher affinity to laminarin than two CBM102 tandem constructs of the SGBP (Ka ~2.76 x 104 M-1 or ~3.63 x 104 M-1) and the full length SGBP (Ka ~3.09 x 104 M-1) <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM102 displays a β-sandwich fold established by two antiparallel β-sheets forming a convex and a concave face. The 3D X-ray crystal structure of the C-terminal CBM102 of the ''C. forsetii'' SGBP showed that together with two expansive loops, the concave face provides a narrow cleft to accommodate laminaritriose <cite>Zuehlke2024</cite> (Figure 1). CBM102 thus represents a [[Carbohydrate-binding_modules|type B CBM]]. Three residues located in the concave face mediate polar interactions with laminaritriose (Lys825, Glu827 and Glu837), while one aromatic residue of each loop (Tyr790, Phe861) is involved in CH-π interaction with the ligand. However, the ''C. forsetii'' protein contains three additional CBM102s. Alphafold2 <cite>Mirdita2022</cite> predictions showed that two of them are highly similar to the 3D crystal structure of the C-terminal CBM102, but that one CBM102 is missing one of the loops shaping the pocket, which results in a very shallow cleft (Figure 2). This was speculated to represent an adaptation to highly branched laminarins <cite>Zuehlke2024</cite>.

[[File:Fig.1.png|thumb|'''Figure 1.''' 3D crystal structure of the C-terminal CBM102 of the ''C. forsetii'' SGBP with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]) <cite>Zuehlke2024</cite>. Highlighted are interacting residues.]]

[[File:Fig.2.png|thumb|'''Figure 2.''' Surfaces of the four CBM102s of the ''C. forsetii'' SGBP <cite>Zuehlke2024</cite>. Left: 3D crystal structure of the C-terminal CBM102 (IV) with laminaritriose (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). Right: Alphafold2-predicted structures (I-III). Module III is missing one of the loops, which form the groove.]]
== Functionalities ==
The CBM102-containing SGBP is tethered to the outer membrane of ''C. forsetii'' and is abundantly produced in laminarin-grown cells <cite>Kabisch2014</cite>. With four CBM102s, the SGBP provides multiple laminarin docking sites <cite>Zuehlke2024</cite>. The protein further contains two N-terminal Ig-like domains that precede the CBM102s, which presumably act as spacers to ensure distance to the membrane and exposure of binding sites as suggested before for β-glucan binding SGBPs <cite>Tamura2021</cite>. The multiplicity of CBM102 in the ''C. forsetii'' protein was suggested to render the SGBP an optimal 'sugar-trapping antenna' on the bacterial surface, which was supported by an elongated protein shape as determined by small angle X ray scattering <cite>Zuehlke2024</cite>. However, isothermal titration calorimetry showed that two laminarin molecules were binding at maximum and that affinity was not increased by multiple CBM102s. In bacterial metagenome-assembled genomes from phytoplankton blooms in the North Sea, CBM102 was detected together with catalytic modules, indicating also other functions (increased catalysis) <cite>Zuehlke2024</cite>. The majority of associated catalytic modules were GH16_3s, but also rare examples of [[Glycoside_Hydrolase_Family_2|GH2]], GH5_34, [[Glycoside_Hydrolase_Family_81|GH81]], [[Glycoside_Hydrolase_Family_162|GH162]]. Within this dataset, CBM102 also co-occurred with [[Carbohydrate_Binding_Module_Family_4|CBM4]], [[Carbohydrate_Binding_Module_Family_6|CBM6]] and [[Carbohydrate_Binding_Module_Family_103|CBM103]]. CBM102-only-proteins contained up to eight repeats of CBM102. The production of CBM102-containing proteins correlated with the course of the phytoplankton bloom, which underlines the relevance of CBM102 in marine β-glucan use.

== Family Firsts ==
;First Identified
CBM102 was first identified in an SGBP encoded in a laminarin utilization locus of ''Christiangramia forsetii'' KT0803T <cite>Zuehlke2024</cite>, a marine flavobacterium isolated from surface waters in the North Sea <cite>Eilers2001</cite>. More than 350 CBM102-containing sequences were detected in bacterial metagenome-assembled genomes (555 representative MAGs of which 201 belonged to ''Bacteroidota'') retrieved from bacterial biomass from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea. Sequences mostly belonged to ''Bacteroidota'', but also to ''Proteobacteria'', ''Myxococcota'' and ''Actinobacteriota'' <cite>Zuehlke2024</cite>. The association with GHs (mostly GH16_3) within this dataset led to the creation of the CBM family 102.
;First Structural Characterization
The C-terminal CBM102 of the laminarin PUL-encoded SGBP of ''C. forsetii'' KT0803T is the first structurally characterized member of the family (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). The 3D crystal structure was obtained in complex with laminaritriose.

== References ==
<biblio>
#Zuehlke2024 pmid=38757353
#Mirdita2022 pmid=35637307
#Kabisch2014 pmid=24522261
#Tamura2021 pmid=33587952
#Eilers2001 pmid=11679337
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM102]]

Carbohydrate Binding Module Family 103

2024-09-09T15:16:23Z

Marie-Katherin Zuehlke:

File:Bfluxus.png

2024-09-09T14:13:46Z

Marie-Katherin Zuehlke:

The CBM103-containing SGBP of Bacteroides fluxus (BfSGBP-B), which is preceded by an N-terminal 'PKD' domains.

Carbohydrate Binding Module Family 102

2024-09-06T13:49:28Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM102.html
|}
</div>


== Ligand specificities ==
The dissected C-terminal CBM102 of a surface glycan-binding protein (SGBP; containing four CBM102s) of ''Christiangramia forsetii'' KT0803T is binding laminarin (from ''Laminaria digitata'') and laminarin-derived oligosaccharides, which was confirmed by affinity gel electrophoresis and/or isothermal titration calorimetry <cite>Zuehlke2024</cite>. The CBM102 had a higher affinity to laminarin (Ka ~1.04 x 105 M-1) than to laminariheptaose (Ka ~1.87 x 104 M-1) and laminaripentaose (Ka ~1.39 x 104 M-1). Laminaribiose was not binding.

In addition, the dissected C-terminal CBM102 had a higher affinity to laminarin than two CBM102 tandem constructs of the SGBP (Ka ~2.76 x 104 M-1 or ~3.63 x 104 M-1) and the full length SGBP (Ka ~3.09 x 104 M-1) <cite>Zuehlke2024</cite>.

== Structural Features ==
The CBM102 displays a β-sandwich fold established by two antiparallel β-sheets forming a convex and a concave face. The 3D X-ray crystal structure of the C-terminal CBM102 of the ''C. forsetii'' SGBP showed that together with two expansive loops, the concave face provides a narrow cleft to accommodate laminaritriose <cite>Zuehlke2024</cite>. CBM102 thus represents a [[Carbohydrate-binding_modules|type B CBM]]. Three residues located in the concave face mediate polar interactions with laminaritriose (Lys825, Glu827 and Glu837), while one aromatic residue of each loop (Tyr790, Phe861) is involved in CH-π interaction with the ligand. However, the ''C. forsetii'' protein contains three additional CBM102s. Alphafold2 <cite>Mirdita2022</cite> predictions showed that two of them are highly similar to the 3D crystal structure of the C-terminal CBM102, but that one CBM102 is missing one of the loops shaping the pocket, which results in a very shallow cleft. This was speculated to represent an adaptation to highly branched laminarins <cite>Zuehlke2024</cite>.
[[File:Fig.1.png|thumb|3D crystal structure of C-terminal CBM102 of the ''C. forsetii'' SGBP with laminaritriose. Highlighted are interacting residues.]]

[[File:Fig.2.png|thumb|Surfaces of the four CBM102s of the ''C. forsetii'' SGBP. Left: 3D crystal structure of the C-terminal CBM102 (IV) with laminaritriose. Right: Alphafold2-predicted structures (I-III). Module III is missing one of the loops, which form the groove.]]
== Functionalities ==
The CBM102-containing SGBP is tethered to the outer membrane of ''C. forsetii'' and is abundantly produced in laminarin-grown cells <cite>Kabisch2014</cite>. With four CBM102s, the SGBP provides multiple laminarin docking sites <cite>Zuehlke2024</cite>. The protein further contains two N-terminal Ig-like domains that precede the CBM102s, which presumably act as spacers to ensure distance to the membrane and exposure of binding sites as suggested before for β-glucan binding SGBPs <cite>Tamura2021</cite>. The multiplicity of CBM102 in the ''C. forsetii'' protein was suggested to render the SGBP an optimal 'sugar-trapping antenna' on the bacterial surface, which was supported by an elongated protein shape as determined by small angle X ray scattering <cite>Zuehlke2024</cite>. However, isothermal titration calorimetry showed that two laminarin molecules were binding at maximum and that affinity was not increased by multiple CBM102s. In bacterial metagenome-assembled genomes from phytoplankton blooms in the North Sea, CBM102 was detected together with catalytic modules, indicating also other functions (increased catalysis) <cite>Zuehlke2024</cite>. The majority of associated catalytic modules were GH16_3s, but also rare examples of GH2, GH5_34, GH81, GH162. Within this dataset, CBM102 also co-occurred with CBM4 and CBM6. CBM102-only-proteins contained up to eight repeats of CBM102. The production of CBM102-containing proteins correlated with the course of the phytoplankton bloom, which underlines the relevance of CBM102 in marine β-glucan use.

== Family Firsts ==
;First Identified
CBM102 was first identified in an SGBP encoded in a laminarin utilization locus of ''Christiangramia forsetii'' KT0803T <cite>Zuehlke2024</cite>, a marine flavobacterium isolated from surface waters in the North Sea <cite>Eilers2001</cite>. 362 CBM102-containing sequences were detected in bacterial metagenome-assembled genomes (555 representative MAGs of which 201 belonged to ''Bacteroidota'') retrieved from bacterial biomass from phytoplankton blooms of three respective years (2016, 2018 and 2020) in the North Sea. Sequences mostly belonged to ''Bacteroidota'', but also to ''Proteobacteria'', ''Myxococcota'' and ''Actinobacteriota'' <cite>Zuehlke2024</cite>. The association with GHs (mostly GH16_3) within this dataset led to the creation of the CBM family 102.
;First Structural Characterization
The C-terminal CBM102 of the laminarin PUL-encoded SGBP of ''C. forsetii'' KT0803T is the first structurally characterized member of the family (PDB ID [https://www.rcsb.org/structure/unreleased/8QX6 8QX6]). The 3D crystal structure was obtained in complex with laminaritriose.

== References ==
<biblio>
#Zuehlke2024 pmid=38757353
#Mirdita2022 pmid=35637307
#Kabisch2014 pmid=24522261
#Tamura2021 pmid=33587952
#Eilers2001 pmid=11679337
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM102]]

File:Fig.2.png

2024-09-06T13:34:39Z

Marie-Katherin Zuehlke:

The surface of the 4 CBM102s of the C. forsetii SGBP. Left: 3D crystal structure of the C-terminal CBM102 (IV) with laminaritriose. Right: Alphafold2 predicted structures.

File:Fig.1.png

2024-09-06T13:18:22Z

Marie-Katherin Zuehlke:

3D crystal structure of the C-terminal CBM102 of the C. forsetii SGBP together with laminaritriose.

User:Marie-Katherin Zuehlke

2024-09-06T10:10:36Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 44

2023-01-10T08:21:25Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM44.html
|}
</div>


== Ligand specificities ==
CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and thus classifies as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 104 M-1), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 104 M-1). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.

== Structural Features ==
Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding (Figure 1), as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>.

[[File:pkd-cbm44.png|thumb|200px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]

== Functionalities ==
Carbohydrate binding and targeting were described as functions of CBM44. While carbohydrate binding was confirmed by AGE and ITC, the [[Carbohydrate-binding modules|targeting effect]] was analyzed by the ability of CBM44 to maintain enzyme activity of [[GH44]] (Cel44A) exposed to a substrate mixture <cite>Najmudin2006</cite>. The ensemble of a [[GH44]] and a CBM44 was found in the multimodular cellulase CtCel9D-Cel44A from ''Acetivibrio thermocellus'' and ligand spectra of both modules are consistent <cite>Najmudin2006</cite>. In the targeting experiment, the fused [[GH44]]-CBM44 construct was compared to the truncated [[GH44]]. In separate xyloglucan or carboxymethylcellulose incubations, the activity of GH44-CBM44 was comparable to that of [[GH44]] alone. In a next step, substrate mixtures were used. These mixtures also contained laminarin and pustulan, which were not degraded. While [[GH44]] activity was decreased, activity was restored by [[GH44]]-CBM44. Thus, given the complex carbohydrates present in plant cell walls, CBM44 may guide the enzyme to its target sugars. Such effects have also been achieved in synthetic CBM44-enzyme chimeras, e.g. [[GH12]] or [[GH28]] <cite>#Furtado2015 #Carli2022</cite>.

== Family Firsts ==
;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase ''Ct''Cel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.
;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>.

== References ==
<biblio>
#Najmudin2006 pmid=16314409
#Sugiyama2000 Sugiyama H, Hisamichi K, Usui T, Sakai K, Ishiyama J (2000). ''A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution.'' J Mol Struct. 2000;'''556'''(1-3):173-7. [https://doi.org/10.1016/S0022-2860(00)00630-X DOI: 10.1016/S0022-2860(00)00630-X].
#Furtado2015 pmid=25605422
#Carli2022 Carli S, Meleiro LP, Salgado JCS, Ward RJ (2022). ''Synthetic carbohydrate-binding module-endogalacturonase chimeras increase catalytic efficiency and saccharification of lignocellulose residues''. Biomass Conv Bioref. 2022. [https://doi.org/10.1007/s13399-022-02716-6 DOI: 10.1007/s13399-022-02716-6].
#Ahsan1996 pmid=8824619
#Arai2003 pmid=12511497
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM044]]

File:Pkd-cbm44.png

2023-01-10T08:14:10Z

Marie-Katherin Zuehlke: Marie-Katherin Zuehlke uploaded a new version of File:Pkd-cbm44.png

Three-dimensional structure of the PKD-CBM44

File:Pkd-cbm44.png

2023-01-10T08:09:21Z

Marie-Katherin Zuehlke: Marie-Katherin Zuehlke uploaded a new version of File:Pkd-cbm44.png

Three-dimensional structure of the PKD-CBM44

Carbohydrate Binding Module Family 44

2023-01-09T16:22:16Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM44.html
|}
</div>


== Ligand specificities ==
CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and thus classifies as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 104 M-1), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 104 M-1). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.

== Structural Features ==
Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding (Figure 1), as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>.

[[File:pkd-cbm44.png|thumb|300px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]

== Functionalities ==
Carbohydrate binding and targeting were described as functions of CBM44. While carbohydrate binding was confirmed by AGE and ITC, the [[Carbohydrate-binding modules|targeting effect]] was analyzed by the ability of CBM44 to maintain enzyme activity of [[GH44]] (Cel44A) exposed to a substrate mixture <cite>Najmudin2006</cite>. The ensemble of a [[GH44]] and a CBM44 was found in the multimodular cellulase CtCel9D-Cel44A from ''Acetivibrio thermocellus'' and ligand spectra of both modules are consistent <cite>Najmudin2006</cite>. In the targeting experiment, the fused [[GH44]]-CBM44 construct was compared to the truncated [[GH44]]. In separate xyloglucan or carboxymethylcellulose incubations, the activity of GH44-CBM44 was comparable to that of [[GH44]] alone. In a next step, substrate mixtures were used. These mixtures also contained laminarin and pustulan, which were not degraded. While [[GH44]] activity was decreased, activity was restored by [[GH44]]-CBM44. Thus, given the complex carbohydrates present in plant cell walls, CBM44 may guide the enzyme to its target sugars. Such effects have also been achieved in synthetic CBM44-enzyme chimeras, e.g. [[GH12]] or [[GH28]] <cite>#Furtado2015 #Carli2022</cite>.

== Family Firsts ==
;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase ''Ct''Cel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.
;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>.

== References ==
<biblio>
#Najmudin2006 pmid=16314409
#Sugiyama2000 Sugiyama H, Hisamichi K, Usui T, Sakai K, Ishiyama J (2000). ''A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution.'' J Mol Struct. 2000;'''556'''(1-3):173-7. [https://doi.org/10.1016/S0022-2860(00)00630-X DOI: 10.1016/S0022-2860(00)00630-X].
#Furtado2015 pmid=25605422
#Carli2022 Carli S, Meleiro LP, Salgado JCS, Ward RJ (2022). ''Synthetic carbohydrate-binding module-endogalacturonase chimeras increase catalytic efficiency and saccharification of lignocellulose residues''. Biomass Conv Bioref. 2022. [https://doi.org/10.1007/s13399-022-02716-6 DOI: 10.1007/s13399-022-02716-6].
#Ahsan1996 pmid=8824619
#Arai2003 pmid=12511497
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM044]]

Carbohydrate Binding Module Family 44

2023-01-09T16:21:05Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM44.html
|}
</div>


== Ligand specificities ==
CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and thus classifies as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 104 M-1), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 104 M-1). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.

== Structural Features ==
Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding, as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>.

[[File:pkd-cbm44.png|thumb|300px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]

== Functionalities ==
Carbohydrate binding and targeting were described as functions of CBM44. While carbohydrate binding was confirmed by AGE and ITC, the [[Carbohydrate-binding modules|targeting effect]] was analyzed by the ability of CBM44 to maintain enzyme activity of [[GH44]] (Cel44A) exposed to a substrate mixture <cite>Najmudin2006</cite>. The ensemble of a [[GH44]] and a CBM44 was found in the multimodular cellulase CtCel9D-Cel44A from ''Acetivibrio thermocellus'' and ligand spectra of both modules are consistent <cite>Najmudin2006</cite>. In the targeting experiment, the fused [[GH44]]-CBM44 construct was compared to the truncated [[GH44]]. In separate xyloglucan or carboxymethylcellulose incubations, the activity of GH44-CBM44 was comparable to that of [[GH44]] alone. In a next step, substrate mixtures were used. These mixtures also contained laminarin and pustulan, which were not degraded. While [[GH44]] activity was decreased, activity was restored by [[GH44]]-CBM44. Thus, given the complex carbohydrates present in plant cell walls, CBM44 may guide the enzyme to its target sugars. Such effects have also been achieved in synthetic CBM44-enzyme chimeras, e.g. [[GH12]] or [[GH28]] <cite>#Furtado2015 #Carli2022</cite>.

== Family Firsts ==
;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase ''Ct''Cel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.
;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>.

== References ==
<biblio>
#Najmudin2006 pmid=16314409
#Sugiyama2000 Sugiyama H, Hisamichi K, Usui T, Sakai K, Ishiyama J (2000). ''A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution.'' J Mol Struct. 2000;'''556'''(1-3):173-7. [https://doi.org/10.1016/S0022-2860(00)00630-X DOI: 10.1016/S0022-2860(00)00630-X].
#Furtado2015 pmid=25605422
#Carli2022 Carli S, Meleiro LP, Salgado JCS, Ward RJ (2022). ''Synthetic carbohydrate-binding module-endogalacturonase chimeras increase catalytic efficiency and saccharification of lignocellulose residues''. Biomass Conv Bioref. 2022. [https://doi.org/10.1007/s13399-022-02716-6 DOI: 10.1007/s13399-022-02716-6].
#Ahsan1996 pmid=8824619
#Arai2003 pmid=12511497
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM044]]

File:Pkd-cbm44.png

2023-01-09T15:56:27Z

Marie-Katherin Zuehlke:

Three-dimensional structure of the PKD-CBM44

Carbohydrate Binding Module Family 44

2023-01-09T12:56:19Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM44.html
|}
</div>


== Ligand specificities ==
CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and thus classifies as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 104 M-1), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 104 M-1). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.

== Structural Features ==
Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding, as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>.

== Functionalities ==
Carbohydrate binding and targeting were described as functions of CBM44. While carbohydrate binding was confirmed by AGE and ITC, the [[Carbohydrate-binding modules|targeting effect]] was analyzed by the ability of CBM44 to maintain enzyme activity of [[GH44]] (Cel44A) exposed to a substrate mixture <cite>Najmudin2006</cite>. The ensemble of a [[GH44]] and a CBM44 was found in the multimodular cellulase CtCel9D-Cel44A from ''Acetivibrio thermocellus'' and ligand spectra of both modules are consistent <cite>Najmudin2006</cite>. In the targeting experiment, the fused [[GH44]]-CBM44 construct was compared to the truncated [[GH44]]. In separate xyloglucan or carboxymethylcellulose incubations, the activity of GH44-CBM44 was comparable to that of [[GH44]] alone. In a next step, substrate mixtures were used. These mixtures also contained laminarin and pustulan, which are not degraded. While [[GH44]] activity now decreased, activity was restored by [[GH44]]-CBM44. Thus, given the complex carbohydrates present in plant cell walls, CBM44 may guide the enzyme to its target sugars. Such effects have also been achieved in synthetic CBM44-enzyme chimeras, e.g. [[GH12]] or [[GH28]] <cite>#Furtado2015 #Carli2022</cite>.

== Family Firsts ==
;First Identified
CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase CtCel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a CBM30 and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as a PKD module and a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.
;First Structural Characterization
The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>.

== References ==
<biblio>
#Najmudin2006 pmid=16314409
#Sugiyama2000 Sugiyama H, Hisamichi K, Usui T, Sakai K, Ishiyama J (2000). ''A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution.'' J Mol Struct. 2000;'''556'''(1-3):173-7. [https://doi.org/10.1016/S0022-2860(00)00630-X DOI: 10.1016/S0022-2860(00)00630-X].
#Furtado2015 pmid=25605422
#Carli2022 Carli S, Meleiro LP, Salgado JCS, Ward RJ (2022). ''Synthetic carbohydrate-binding module-endogalacturonase chimeras increase catalytic efficiency and saccharification of lignocellulose residues''. Biomass Conv Bioref. 2022. [https://doi.org/10.1007/s13399-022-02716-6 DOI: 10.1007/s13399-022-02716-6].
#Ahsan1996 pmid=8824619
#Arai2003 pmid=12511497
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM044]]

Carbohydrate Binding Module Family 44

2023-01-09T12:53:50Z

Marie-Katherin Zuehlke:

{{UnderConstruction}}
* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]
* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM44.html
|}
</div>


== Ligand specificities ==
CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and thus classifies as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 104 M-1), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 104 M-1). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.

== Structural Features ==
Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding, as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>.

== Functionalities ==
Carbohydrate binding and targeting were described as functions of CBM44. While carbohydrate binding was confirmed by AGE and ITC, the [[Carbohydrate-binding modules|targeting effect]] was analyzed by the ability of CBM44 to maintain enzyme activity of [[GH44]] (Cel44A) exposed to a substrate mixture. The ensemble of a [[GH44]] and a CBM44 was found in the multimodular cellulase CtCel9D-Cel44A from ''Acetivibrio thermocellus'' and ligand spectra of both modules are consistent <cite>Najmudin2006</cite>. In the targeting experiment, the fused [[GH44]]-CBM44 construct was compared to the truncated [[GH44]]. In separate xyloglucan or carboxymethylcellulose incubations, the activity of GH44-CBM44 was comparable to that of [[GH44]] alone. In a next step, substrate mixtures were used. These mixtures also contained laminarin and pustulan, which are not degraded. While [[GH44]] activity now decreased, activity was restored by [[GH44]]-CBM44. Thus, given the complex carbohydrates present in plant cell walls, CBM44 may guide the enzyme to its target sugars. Such effects have also been achieved in synthetic CBM44-enzyme chimeras, e.g. [[GH12]] or [[GH28]] <cite>#Furtado2015 #Carli2022</cite>.

== Family Firsts ==
;First Identified
CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase CtCel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a CBM30 and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as a PKD module and a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.
;First Structural Characterization
The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>.

== References ==
<biblio>
#Najmudin2006 pmid=16314409
#Sugiyama2000 Sugiyama H, Hisamichi K, Usui T, Sakai K, Ishiyama J (2000). ''A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution.'' J Mol Struct. 2000;'''556'''(1-3):173-7. [https://doi.org/10.1016/S0022-2860(00)00630-X DOI: 10.1016/S0022-2860(00)00630-X].
#Furtado2015 pmid=25605422
#Carli2022 Carli S, Meleiro LP, Salgado JCS, Ward RJ (2022). ''Synthetic carbohydrate-binding module-endogalacturonase chimeras increase catalytic efficiency and saccharification of lignocellulose residues''. Biomass Conv Bioref. 2022. [https://doi.org/10.1007/s13399-022-02716-6 DOI: 10.1007/s13399-022-02716-6].
#Ahsan1996 pmid=8824619
#Arai2003 pmid=12511497
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM044]]

Carbohydrate Binding Module Family 44

2023-01-09T12:10:52Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 44

2023-01-09T09:51:15Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 44

2023-01-09T09:49:32Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 44

2023-01-09T09:21:40Z

Marie-Katherin Zuehlke:

User:Marie-Katherin Zuehlke

2023-01-09T08:51:59Z

Marie-Katherin Zuehlke:

User:Marie-Katherin Zuehlke

2023-01-09T08:14:59Z

Marie-Katherin Zuehlke:

User:Marie-Katherin Zuehlke

2023-01-09T08:06:47Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 44

2023-01-06T15:47:02Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 44

2023-01-06T15:37:48Z

Marie-Katherin Zuehlke:

Carbohydrate Binding Module Family 44

2023-01-06T15:25:14Z

Marie-Katherin Zuehlke:

User:Marie-Katherin Zuehlke

2023-01-06T15:23:51Z

Marie-Katherin Zuehlke:

[[File:Portrait Marie Zuehlke klein.jpg|thumb]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).

Please find me on ResearchGate.

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables ''Bacillus licheniformis'' to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium ''Cupriavidus basilensis'' – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L, Préchoux A, Zühlke MK, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading ''Cupriavidus basilensis''. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by ''Bacillus amyloliquefaciens'': Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zühlke,Marie-Katherin]]

User:Marie-Katherin Zuehlke

2023-01-06T15:22:38Z

Marie-Katherin Zuehlke:

[[File:Portrait Marie Zuehlke klein.jpg|thumb]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).

Please find me on ResearchGate.

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables ''Bacillus licheniformis'' to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium ''Cupriavidus basilensis'' – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L, Préchoux A, Zühlke MK, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.*authors contributed equally

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading ''Cupriavidus basilensis''. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by ''Bacillus amyloliquefaciens'': Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zühlke,Marie-Katherin]]

User:Marie-Katherin Zuehlke

2023-01-06T15:21:13Z

Marie-Katherin Zuehlke:

[[File:Portrait Marie Zuehlke klein.jpg|thumb]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).

Please find me on ResearchGate.

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables ''Bacillus licheniformis'' to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium ''Cupriavidus basilensis'' – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L, Préchoux A, Zühlke MK, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.*authors contributed equally

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading ''Cupriavidus basilensis''. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by ''Bacillus amyloliquefaciens'': Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zuehlke,Marie-Katherin]]

User:Marie-Katherin Zuehlke

2023-01-06T15:20:43Z

Marie-Katherin Zuehlke:

[[File:Portrait Marie Zuehlke klein.jpg|thumb]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).
Please find me on ResearchGate.

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables ''Bacillus licheniformis'' to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium ''Cupriavidus basilensis'' – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L, Préchoux A, Zühlke MK, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.*authors contributed equally

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading ''Cupriavidus basilensis''. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by ''Bacillus amyloliquefaciens'': Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zuehlke,Marie-Katherin]]

File:Portrait Marie Zuehlke klein.jpg

2023-01-06T15:18:51Z

Marie-Katherin Zuehlke:

Marie

Carbohydrate Binding Module Family 44

2023-01-06T15:11:35Z

Marie-Katherin Zuehlke:

User:Marie-Katherin Zuehlke

2023-01-06T14:42:57Z

Marie-Katherin Zuehlke:

[[Image:Blank_user-200px.png|200px|right]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables ''Bacillus licheniformis'' to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium ''Cupriavidus basilensis'' – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L, Préchoux A, Zühlke MK, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.*authors contributed equally

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading ''Cupriavidus basilensis''. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by ''Bacillus amyloliquefaciens'': Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zuehlke,Marie-Katherin]]

User:Marie-Katherin Zuehlke

2023-01-06T14:40:36Z

Marie-Katherin Zuehlke:

[[Image:Blank_user-200px.png|200px|right]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables Bacillus licheniformis to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium Cupriavidus basilensis – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L, Préchoux A, Zühlke MK, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.*authors contributed equally

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading Cupriavidus basilensis. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by Bacillus amyloliquefaciens: Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zuehlke,Marie-Katherin]]

User:Marie-Katherin Zuehlke

2023-01-06T14:39:09Z

Marie-Katherin Zuehlke:

[[Image:Blank_user-200px.png|200px|right]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables Bacillus licheniformis to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium Cupriavidus basilensis – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L*, Préchoux A*, Zühlke MK*, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.*authors contributed equally

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading Cupriavidus basilensis. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by Bacillus amyloliquefaciens: Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zuehlke,Marie-Katherin]]

User:Marie-Katherin Zuehlke

2023-01-06T14:36:43Z

Marie-Katherin Zuehlke:

[[Image:Blank_user-200px.png|200px|right]]

All my life I have been interested in environmental issues and thus studied (micro)biology. My PhD thesis was dedicated to the bacterial transformation of bisphenols, which are released from plastics and disrupt the endocrine system (laboratory Frieder Schauer). I focused on the structural elucidation of produced transformation products and their risk assessment. As a Post Doc, I have expanded this by the perspective of bacterial physiology and the proteins involved in degradation processes. Here, I am investigating the bacterial breakdown of algal sugars using proteomics and by detailed functional analysis of specific proteins. I am based at the University of Greifswald, Germany, and Station Biologique de Roscoff, France (teams Thomas Schweder and Mirjam Czjzek).

Beidler I, Robb CS, Vidal-Melgosa S, Zühlke MK, Bartosik D, Solanki V, Markert S, Becher D, Schweder T, Hehemann JH (2022). Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan. ISME J.

Dutschei T, Zühlke MK, Welsch N, Eisenack T, Hilkmann M, Krull J, Stühle C, Brott S, Dürwald A, Reisky L, Hehemann JH, Becher, D, Schweder T, Bornscheuer UT (2022). Metabolic engineering enables Bacillus licheniformis to grow on the marine polysaccharide ulvan. Microb. Cell Fact. 21(1): 207.

Dürwald A, Zühlke MK, Schlüter R, Gebbe R, Bartosik D, Unfried F, Becher D, Schweder T (2021). Reaching out in anticipation: bacterial membrane extensions represent a permanent investment in polysaccharide sensing and utilization. Environ. Microbiol. 23: 3149-3163.

Zühlke MK, Schlüter R, Mikolasch A, Henning AK, Giersberg M, Lalk M, Kunze G, Schweder T, Urich T, Schauer F (2020). Biotransformation of bisphenol A analogues by the biphenyl degrading bacterium Cupriavidus basilensis – a structure-biotransformation relationship. Appl. Microbiol. Biotechnol. 104:3569-3583

Reisky L*, Préchoux A*, Zühlke MK*, Bäumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Tao S, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH (2019). A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. 12(12):2894-2906. Nature Chem. Biol.*authors contributed equally

Zühlke MK, Schlüter R, Mikolasch A, Zühlke D, Giersberg M, Schindler H, Henning AK, Frenzel H, Hammer E, Lalk M, Bornscheuer UT, Riedel K, Kunze G, Schauer F (2017). Biotransformation and reduction of estrogenicity of bisphenol A by the biphenyl-degrading Cupriavidus basilensis. Appl. Microbiol. Biotechnol. 101(9):3743-3758.

Zühlke MK, Schlüter R, Henning AK, Lipka M, Mikolasch A, Schumann P, Giersberg M, Kunze G, Schauer F (2016). A novel mechanism of conjugate formation of bisphenol A and its analogues by Bacillus amyloliquefaciens: Detoxification and reduction of estrogenicity of bisphenols. Int. Biodeterior. Biodegrad. 109:165-173.

----


[[Category:Contributors|Zuehlke,Marie-Katherin]]