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
http://www.cazy.org/fam/GH37.html

Substrate specificities

GH37 enzymes 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. The structural solution of the trehalase from Escherichia coli demonstrates the active site catalytic residues are in a position consistent with an inverting mechanism.

Catalytic Residues

  Normal  0          false  false  false    EN-GB  X-NONE  X-NONE                                       MicrosoftInternetExplorer4                                      The catalytic residues have not been demonstrates 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.

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

1. 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 |
2. Cardona F, Parmeggiani C, Faggi E, Bonaccini C, Gratteri P, Sim L, Gloster TM, Roberts S, Davies GJ, Rose DR, and Goti A. (2009). Total syntheses of casuarine and its 6-O-alpha-glucoside: complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families. Chemistry. 2009;15(7):1627-36. DOI:10.1002/chem.200801578 |