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 [1]. The structural solution of the trehalase from Escherichia coli 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

Cite some reference here, with a short (1-2 sentence) explanation

  Normal  0          false  false  false    EN-GB  X-NONE  X-NONE                                       MicrosoftInternetExplorer4                                                                                                                                                                                                                                                                                                                             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

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

First general acid/base residue identification

Cite some reference here, with a short (1-2 sentence) explanation [6].

First 3-D structure

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

References

1. Clifford KH (1980). Stereochemistry of the hydrolysis of trehalose by the enzyme trehalase prepared from the flesh fly Sarcophaga barbata. Eur J Biochem. 1980;106(1):337-40. DOI:10.1111/j.1432-1033.1980.tb06028.x |
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 |
3. 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 |
4. Cardona F, Goti A, Parmeggiani C, Parenti P, Forcella M, Fusi P, Cipolla L, Roberts SM, Davies GJ, and Gloster TM. (2010). Casuarine-6-O-alpha-D-glucoside and its analogues are tight binding inhibitors of insect and bacterial trehalases. Chem Commun (Camb). 2010;46(15):2629-31. DOI:10.1039/b926600c |