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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]] |
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].
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.