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Difference between revisions of "Glycoside Hydrolase Family 37"
| Line 32: | Line 32: | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | A trehalase from flesh fly was shown to hydrolyse with inversion of stereochemistry using | + | A trehalase from flesh fly was shown to hydrolyse with inversion of stereochemistry using <sup>18</sup>O 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 == | == 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 == | == Three-dimensional structures == | ||
Revision as of 11:38, 8 October 2010
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Tracey Gloster^^^
- Responsible Curator: ^^^Gideon Davies^^^
| 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
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