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Difference between revisions of "Glycoside Hydrolase Family 168"

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(Added Jingjing Shen as Author)
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== Substrate specificities ==
 
== Substrate specificities ==
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Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium Wenyingzhuangia funcanilytica CZ1127T, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a random endo-acting manner <cite>Shen2020</cite>. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from Isostichopus badionotus, namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1.  
 
 
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
 
 
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
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As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis.  
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
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Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A.
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
Content is to be added here.
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No three-dimensional structure has been solved in this glycoside hydrolase family at present.
  
 
== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
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;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: Content is to be added here.
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;First catalytic nucleophile identification: Not yet identified.
;First general acid/base residue identification: Content is to be added here.
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;First general acid/base residue identification: Not yet identified.
;First 3-D structure: Content is to be added here.
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;First 3-D structure: Not yet identified.
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Cantarel2009 pmid=18838391
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#Shen2020 pmid=32849348
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].
 
 
</biblio>
 
</biblio>
  
 
<!-- Do not delete this Category tag -->
 
<!-- Do not delete this Category tag -->
 
[[Category:Glycoside Hydrolase Families|GH168]]
 
[[Category:Glycoside Hydrolase Families|GH168]]

Revision as of 05:49, 18 June 2023

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Glycoside Hydrolase Family GH168
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
https://www.cazy.org/GH168.html


Substrate specificities

Members of glycoside hydrolase family 168 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium Wenyingzhuangia funcanilytica CZ1127T, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a random endo-acting manner [1]. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from Isostichopus badionotus, namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1.

Kinetics and Mechanism

As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis.

Catalytic Residues

Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A.

Three-dimensional structures

No three-dimensional structure has been solved in this glycoside hydrolase family at present.

Family Firsts

First stereochemistry determination
Not yet identified.
First catalytic nucleophile identification
Not yet identified.
First general acid/base residue identification
Not yet identified.
First 3-D structure
Not yet identified.

References

  1. Shen J, Chang Y, Zhang Y, Mei X, and Xue C. (2020). Discovery and Characterization of an Endo-1,3-Fucanase From Marine Bacterium Wenyingzhuangia fucanilytica: A Novel Glycoside Hydrolase Family. Front Microbiol. 2020;11:1674. DOI:10.3389/fmicb.2020.01674 | PubMed ID:32849348 [Shen2020]