Glycoside Hydrolase Family 187

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• Author: Jingjing Shen
• Responsible Curator: Yaoguang Chang

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Glycoside Hydrolase Family GH187
Clan	GH-x
Mechanism	retaining/inverting
Active site residues	known/not known
CAZy DB link
http://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 a random endo-acting manner. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucan from Holothuria tubulosa and Isostichopus badionotus, namely WP_159020740.1.

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: [1, 2].

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.

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

1. 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. DOI:10.1042/BIO03004026.

2. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |