Glycoside Hydrolase Family 164

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• Author: ^^^Zachary Armstrong^^^
• Responsible Curator: ^^^Gideon Davies^^^

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Glycoside Hydrolase Family GH164
Clan	GH-x
Mechanism	retaining/inverting
Active site residues	known/not known
CAZy DB link
https://www.cazy.org/GH164.html

Substrate specificities

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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

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Catalytic Residues

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Three-dimensional structures

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Figure 1. The trimeric structure of Bs164 is shown in panel A. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain. B shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.

Family Firsts

First sterochemistry determination

Bacteroides salyersiae β-mannosidase by NMR [3]

First catalytic nucleophile identification

Bacteroides salyersiae β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants [3]

First general acid/base residue identification

Bacteroides salyersiae β-mannosidase by kinetic analysis of mutants [3]

First 3-D structure of a GH1 enzyme

Bacteroides salyersiae β-mannosidase [3]

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. Download PDF version.

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 |