Difference between revisions of "Glycoside Hydrolase Family 187"

Latest revision as of 22:46, 4 January 2024

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Glycoside Hydrolase Family GH187
Clan	not known
Mechanism	not known
Active site residues	not known
CAZy DB link
https://www.cazy.org/GH187.html

Substrate specificities

Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fucp(2,4OSO₃^-)-1→3-α-L-Fucp-1→3-α-L-Fucp(2OSO₃^-)-1→3-α-L-Fucp(2OSO₃^-) in an endo-acting manner [1]. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucans from Holothuria tubulosa and Isostichopus badionotus, namely WP_159020740.1 [1].

Figure 1. The phylogenetic tree of GH187 homologues. Sequences confirmed to exhibit α-1,3-L-fucanase activity were highlighted in red triangles.

Kinetics and Mechanism

The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol [1].

Catalytic Residues

No catalytic residues have been identified in this glycoside hydrolase family at present.

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

Shen J, Zheng L, Zhang Y, Chen G, Mei X, Chang Y, and Xue C. (2024). Discovery of a catalytic domain defines a new glycoside hydrolase family containing endo-1,3-fucanase. Carbohydr Polym. 2024;323:121442. DOI:10.1016/j.carbpol.2023.121442 | PubMed ID:37940306 [Shen2024]

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 * [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]
 * [[Responsible Curator]]:  [[User:Yaoguang Chang|Yaoguang Chang]]
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 |'''Clan'''
-|GH-x
+|not known
 |-
 |'''Mechanism'''
-|retaining/inverting
+|not known
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 |'''Active site residues'''
-|known/not known
+|not known
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 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
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 == Substrate specificities ==
-Content is to be added here.
+Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fuc''p''(2,4OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>) in an endo-acting manner <cite>Shen2024</cite>. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucans from ''Holothuria tubulosa'' and ''Isostichopus badionotus'', namely WP_159020740.1 <cite>Shen2024</cite>.
+[[File: Figure 1.jpg|thumb|''' Figure 1. The phylogenetic tree of GH187 homologues. Sequences confirmed to exhibit α-1,3-L-fucanase activity were highlighted in red triangles.]]
-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 ==
-Content is to be added here.
+The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol <cite>Shen2024</cite>.
 == Catalytic Residues ==
-Content is to be added here.
+No catalytic residues have been identified in this glycoside hydrolase family at present.
 == Three-dimensional structures ==
-Content is to be added here.
+No three-dimensional structure has been solved in this glycoside hydrolase family at present.
 == Family Firsts ==
-;First stereochemistry determination: Content is to be added here.
+;First stereochemistry determination: Not yet identified.
-;First catalytic nucleophile identification: Content is to be added here.
+;First catalytic nucleophile identification: Not yet identified.
-;First general acid/base residue identification: Content is to be added here.
+;First general acid/base residue identification: Not yet identified.
-;First 3-D structure: Content is to be added here.
+;First 3-D structure: Not yet identified.
 == References ==
 <biblio>
-#Cantarel2009 pmid=18838391
+#Shen2024 pmid=37940306
-#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 DOI:10.1042/BIO03004026].
 </biblio>
 <!-- Do not delete this Category tag -->
 [[Category:Glycoside Hydrolase Families|GH187]]