{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


[[File: CE15_CAZypedia_Figure.png|thumb|right|400px|'''Figure 1. Comparison of structurally determined CE15 members.''' The CE15s (A) ''St''GE2 from ''Thermothelomyces thermophila'' (PDB ID [{{PDBlink}}4g4j 4G4J]), (B) ''Ot''CE15A from ''Opitutus terrae'' (PDB ID [{{PDBlink}}6gs0 6GS0]), and (C) ''Tt''CE15A from ''Teredinibacter turnerae'' (PDB ID [{{PDBlink}}6hsw 6HSW]) are shown in cartoon representation. The catalytic triad in each enzyme is shown as sticks and the methyl ester of 4-''O''-methyl glucuronoate first observed in ''St''GE2 is shown in all structures as green sticks. While all CE15 members contain the alpha/beta hydrolase fold, the most prominent difference across the CE15 family observed to-date are the presence, absence, or variety of inserted regions that protrude and build-up ridges around the active site (the differently colored regions in the ''Ot''CE15A and ''Tt''CE15A). The extent to which these regions affect the enzyme’s substrate specificity has yet to be fully elucidated.]]

== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
Representative structures of CE15 enzymes from bacterial and fungal sources have been determined, including ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'', PDB [{{PDBlink}}3pic 3pic]) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (''Sporotrichum thermophile'', PDB [{{PDBlink}}4g4g 4g4g], [{{PDBlink}}4g4i 4g4i], and [{{PDBlink}}4g4j 4g4j]) <cite>Charavgi2013</cite>, marine metagenome sequence MZ0003 (PDB [{{PDBlink}}6ehn 6ehn]) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB [{{PDBlink}}6grw 6grw] and [{{PDBlink}}6gs0 6gs0]) and ''Su''CE15C (PDB [{{PDBlink}}6gry 6gry] and [{{PDBlink}}6gu8 6gu8]) <cite>Arnlingbaath2018</cite> (see the CAZy database for a [http://www.cazy.org/CE15_structure.html continuously updated list]). All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Spanikova2006 pmid=16876163
#Arnlingbaath2018 pmid=30083226
#Desanti2016 pmid=27433797
#Mosbech2018 pmid=29560026
#Derrico2016 pmid=26712478
#Arnlingbaath2016 pmid=27397104
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
#Desanti2017 pmid=29222424
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

File:CE15 CAZypedia Figure.png

2019-07-11T17:56:03Z

Scott Mazurkewich: CE15 structures

CE15 structures

Carbohydrate Esterase Family 15

2019-01-28T13:50:10Z

Scott Mazurkewich:

{{UnderConstruction}}
* [[Author]]: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
* [[Responsible Curator]]: ^^^Johan Larsbrink^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE15'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE15.html
|}
</div>


== Substrate specificity ==
All CE15 enzymes characterized to-date are glucuronoyl esterases, cleaving esters of D-glucuronic acid. The first reported glucuronoyl esterase was ''Sc''GE1 from the white-rot fungus ''Schizophyllum commune'', and the activity was demonstrated by TLC on a methyl ester of 4-''O''-methyl-D-glucuronic acid <cite>Spanikova2006</cite>. While CE15 members are found in both fungal and bacterial species, several bacterial CE15 enzymes are more promiscuous than their fungal counterparts and are active also on esters of galacturonoate <cite>Arnlingbaath2018</cite>. Feruloyl- and acetyl esterase activities have been reported for certain CE15 enzymes as side activities <cite>Desanti2016 Mosbech2018</cite>. The proposed physiological role of CE15 enzymes is to hydrolyze lignin-carbohydrate ester linkages between lignin and glucuronoxylan in plant cell walls, and a few studies have demonstrated their activity on lignocellulose-derived materials and plant biomass <cite>Derrico2016 Arnlingbaath2016 Mosbech2018 </cite>.

== Three-dimensional structures ==
As of January 2019, five structures of CE15 enzymes have been determined: ''Tr''GE (Cip2) from ''T. reesei'' (''Hypocrea jecorina'') (PDB: 3pic) <cite>Pokkuluri2011</cite>, ''St''GE2 from ''Thermothelomyces thermophila'' (previously ''Sporotrichum thermophile'' (PDB: 4g4g, 4g4i and 4g4j) <cite>Charavgi2013</cite>, MZ0003 (PDB: 6ehn; cloned from a marine metagenome) <cite>Desanti2017</cite>, ''Ot''CE15A (PDB: 6grw and 6gs0) and ''Su''CE15C (PDB: 6gry and 6gu8) <cite>Arnlingbaath2018</cite>. All structurally determined CE15 enzymes share an alpha/beta hydrolase fold, consisting of a three-layer alpha-beta-alpha sandwich with the active site in a solvent-exposed cleft. The structures of the bacterial enzymes determined thus far exhibit sizeable inserts which result in much deeper active site pockets compared to the shallow active sites seen in fungal glucuronoyl esterase structures <cite>Desanti2017 Arnlingbaath2018 </cite>.

== Catalytic Residues and Mechanism ==
All CE15 enzymes are serine-type hydrolases, containing a catalytic triad of Glu/Asp-His-Ser <cite>Pokkuluri2011 Charavgi2013 Desanti2017 Arnlingbaath2018</cite>. The position of the acidic residue of the triad is not similarly positioned in all CE15 members as the residue can be found on different loops of the conserved fold <cite>Desanti2017</cite>. A conserved arginine found in all of the CE15 structures, proximal to the catalytic triad, has been proposed to stabilize the formation of the oxyanion during catalysis <cite>Arnlingbaath2018</cite>.

== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.
;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.

== References ==
<biblio>
#Spanikova2006 pmid=16876163
#Arnlingbaath2018 pmid=30083226
#Desanti2016 pmid=27433797
#Mosbech2018 pmid=29560026
#Derrico2016 pmid=26712478
#Arnlingbaath2016 pmid=27397104
#Pokkuluri2011 pmid=21661060
#Charavgi2013 pmid=23275164
#Desanti2017 pmid=29222424
</biblio>

[[Category:Carbohydrate Esterase Families|CE015]]

User:Scott Mazurkewich

2018-12-07T06:48:27Z

Scott Mazurkewich:

[[Image:Scott_Mazurkewich.jpg|200px|right]]
'''Post Doctoral Researcher''' at the Department of Biology and Biological Engineering, [http://www.chalmers.se Chalmers University of Technology].

== Background ==
Scott obtained both his BSc and PhD from the [https://www.uoguelph.ca/ University of Guelph] in Canada. His PhD work, completed under the supervision of [https://www.uoguelph.ca/mcb/people/dr-stephen-seah, Stephen Seah], was on structure-function studies of enzymes involved in the metabolism of aromatic lignin fragments in <i>Pseudomonas</i> <cite>Wang2010, Mazurkewich2014, Mazurkewich2016</cite>. Shortly after completing his PhD studies, he started a post-doctoral research position with ^^^Johan Larsbrink^^^ at Chalmers University. There he has been working collaboratively with ^^^Jenny Arnling Bååth^^^ and ^^^Leila Lo Leggio^^^ on structure-function studies of bacterial [[CE15]] members.

== Selected papers ==

<biblio>
#Wang2010 pmid=20843800
#Mazurkewich2014 pmid=24359411
#Mazurkewich2016 pmid=26867578
#ArnlingBaath2018 pmid=30083226
</biblio>


[[Category:Contributors|Mazurkewich,Scott]]

2018-12-06T19:59:38Z

Scott Mazurkewich:

[[Image:Blank_user-200px.png|200px|right]]
'''This is an empty template to help you get started with composing your User page.'''

Scott obtained both his BSc and PhD from the University of Guelph in Canada. His PhD work, completed under the supervision of Stephen Seah, was on structure-function studies of enzymes involved in the metabolism of aromatic lignin fragments in Pseudomonas. Shortly after completing his PhD studies he took up a post-doctoral research position with Johan Larsbrink at the Chalmers University of Technology where he has been working collaboratively with Jenny AB and Leila Lo Leggio on structure-function studies of bacterial CE15 members.

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----

<biblio>
#ArnlingBaath2018a pmid=30083226

</biblio>


[[Category:Contributors|Mazurkewich,Scott]]