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	Inferred
CAZy DB link
https://www.cazy.org/GH37.html

Substrate specificities

GH37 glycoside hydrolases have been shown, to date, to hydrolyse only the disaccharide trehalose (α-D-glucopyranosyl-(1→1)-α-D-glucopyranoside) into two glucose units (EC 3.2.1.28).

Kinetics and Mechanism

A trehalase from flesh fly was shown to hydrolyse with inversion of stereochemistry using ¹⁸O labelled water [1]. The structural solution of the trehalase from Escherichia coli also demonstrates the active site catalytic residues are in a position consistent with an inverting mechanism [2].

Catalytic Residues

The catalytic residues have not been demonstrated unequivocally, but structural determination of the trehalase from Escherichia coli in complex with inhibitors in the active site implicate an aspartate residue (Asp312 in E. coli) as the catalytic acid and a glutamate residue (Glu496 in E. coli) as the catalytic base [2].

Three-dimensional structures

The only structural representative from GH37 to date is the trehalase from Escherichia coli, which was solved using X-ray crystallography [2]. The structure revealed a (α/α)₆ barrel fold, similar to other α-toroidal glycosidases such as those in families GH94, GH15 and GH65. GH37 falls into clan GH-G. Structures have been solved with the inhibitors validoxylamine A, 1-thiatrehazolin and casuarine analogues [2, 3, 4].

Family Firsts

First sterochemistry determination

The inversion of stereochemistry for a trehalase from the flesh fly Sarcophaga barbata was first demonstrated by Clifford in 1980 [1].

First catalytic nucleophile identification

Predicted from structure determination [2], but not shown unequivocally.

First general acid/base residue identification

Predicted from structure determination [2], but not shown unequivocally.

First 3-D structure

The GH37 trehalase from Escherichia coli was solved by X-ray crystallography [2].

References

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2. Gibson RP, Gloster TM, Roberts S, Warren RA, Storch de Gracia I, García A, Chiara JL, and Davies GJ. (2007). Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors. Angew Chem Int Ed Engl. 2007;46(22):4115-9. DOI:10.1002/anie.200604825 |