Glycoside Hydrolase Family 147

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• Author: ^^^Jonathon Briggs^^^
• Responsible Curator: ^^^Harry Gilbert^^^

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Glycoside Hydrolase Family GH147
Clan	GH-A
Mechanism	retaining
Active site residues	known
CAZy DB link
http://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

1. 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 |