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Glycoside Hydrolase Family 147
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- Author: ^^^Jonathon Briggs^^^
- Responsible Curator: ^^^Harry Gilbert^^^
Glycoside Hydrolase Family GH147 | |
Clan | GH-A |
Mechanism | retaining |
Active site residues | known |
CAZy DB link | |
https://www.cazy.org/GH147.html |
Substrate specificities
The founding member of GH147, BACOVA_05493 a β1,4-galactosidase demonstrates a preference towards longer oligosaccharides releasing galacopyranose from the oligosaccharide chain. BACOVA_ is unable to hydrolyse galactobiose [1].
Kinetics and Mechanism
NMR analysis of the hydrolysis product revealed a retaining mechanism of action [1].
Catalytic Residues
The catalytic nucleophile and general acid/base residues of the founding member of GH147, BACOVA_05493, were identified as Glu300 and Glu203, respectively [1].
Three-dimensional structures
Currently there is no crystal structure of any member of GH147.
Family Firsts
- First stereochemistry determination
- BACOVA_05493 from B. ovatus [1].
- First catalytic nucleophile identification
- BACOVA_05493 from B. ovatus [1].
- First general acid/base residue identification
- BACOVA_05493 from B. ovatus [1].
- First 3-D structure
- Currently not available.
References
- Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, Baslé A, Cartmell A, Terrapon N, Stott K, Lowe EC, McLean R, Shearer K, Schückel J, Venditto I, Ralet MC, Henrissat B, Martens EC, Mosimann SC, Abbott DW, and Gilbert HJ. (2018). Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. Nat Microbiol. 2018;3(2):210-219. DOI:10.1038/s41564-017-0079-1 |