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Difference between revisions of "Glycoside Hydrolase Family 187"
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* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]] | * [[Author]]: [[User:Jingjing Shen|Jingjing Shen]] | ||
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]] | * [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]] | ||
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|'''Clan''' | |'''Clan''' | ||
| − | | | + | |not known |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | | | + | |not known |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |not known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
|- | |- | ||
| − | | colspan="2" |{{CAZyDBlink}} | + | | colspan="2" |{{CAZyDBlink}}GH187.html |
|} | |} | ||
</div> | </div> | ||
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== Substrate specificities == | == 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-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.]] | |
| − | |||
| − | |||
| − | |||
== Kinetics and Mechanism == | == 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 <cite>Shen2024</cite>. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | No catalytic residues have been identified in this glycoside hydrolase family at present. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | No three-dimensional structure has been solved in this glycoside hydrolase family at present. | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Not yet identified. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: Not yet identified. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: Not yet identified. |
| − | ;First 3-D structure: | + | ;First 3-D structure: Not yet identified. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Shen2024 pmid=37940306 |
| − | |||
</biblio> | </biblio> | ||
<!-- Do not delete this Category tag --> | <!-- Do not delete this Category tag --> | ||
[[Category:Glycoside Hydrolase Families|GH187]] | [[Category:Glycoside Hydrolase Families|GH187]] | ||
| − | |||
Latest revision as of 22:46, 4 January 2024
This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.
| 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].
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.