Glycoside Hydrolase Family 37

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• Author: ^^^Tracey Gloster^^^
• Responsible Curator: ^^^Gideon Davies^^^

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Glycoside Hydrolase Family GH37
Clan	GH-G
Mechanism	Inverting
Active site residues	known
CAZy DB link
http://www.cazy.org/fam/GH37.html

Substrate specificities

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Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

The only structural representative from GH37 to date is the trehalase from Escherichia coli, which was solved using X-ray crystallography [1]. The structure revealed a (α/α)₆ barrel fold, and was placed into clan GH-G. Structures have been solved with the inhibitors validoxylamine A, 1-thiatrehazolin and a casuarine analogue [1, 2].

Family Firsts

First sterochemistry determination

Cite some reference here, with a short (1-2 sentence) explanation [3].

First catalytic nucleophile identification

Cite some reference here, with a short (1-2 sentence) explanation [4].

First general acid/base residue identification

Cite some reference here, with a short (1-2 sentence) explanation [5].

First 3-D structure

The GH37 trehalase from Escherichia coli was solved by X-ray crystallography [1].

References

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[[Category:Glycoside Hydrolase Families|GH037]]