Glycoside Hydrolase Family 78

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• Author:
• Responsible Curator: ^^^Zui Fujimoto^^^

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Glycoside Hydrolase Family GH78
Clan
Mechanism	inverting
Active site residues	known/not known
CAZy DB link
https://www.cazy.org/GH78.html

Substrate specificities

Family GH78 glycoside hydrolases are found in bacteria and fungi. The characterized activity of this family is α-L-rhamnosidase (EC 3.2.1.40). α-L-Rhamnosidases catalyze the hydrolysis of α-L-rhamnosyl-linkages in L-rhamnose containing compounds, such as naringin and rutin, or rhamnogalacturonan and arabinogalactan-protein.

Kinetics and Mechanism

GH78 enzymes hydrolyze glycosidic bonds through an acid base-assisted single displacement or inverting mechanism elucidated by proton NMR [Zverlov2000].

Catalytic Residues

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Three-dimensional structures

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Family Firsts

First stereochemistry determination

Clostridium stercorarium α-L-rhamnosidase RamA by ¹H-NMR.

First catalytic nucleophile identification

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First general acid/base residue identification

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First 3-D structure

α-L-rhamnosidase B (BsRhaB) from Bacillus sp. GL1 [Cui2007].

References

1. 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 |

2. Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382

1. Zverlov2000 pmid=10632887
2. Cui2007 pmid=17936784