Alpha,alpha-trehalase
From Wikipedia, the free encyclopedia
| alpha,alpha-trehalase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 3.2.1.28 | ||||||
| CAS number | 9025-52-9 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
|
|||||||
 |
This article is an orphan, as few or no other articles link to it. Please introduce links to this page from related articles; suggestions may be available. (December 2007) |
In enzymology, an alpha,alpha-trehalase (EC 3.2.1.28) is an enzyme that catalyzes the chemical reaction
- alpha,alpha-trehalose + H2O
2 D-glucose
2 D-glucoseThus, the two substrates of this enzyme are alpha,alpha-trehalose and H2O, whereas its product is D-glucose.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha,alpha-trehalose glucohydrolase. This enzyme is also called trehalase. This enzyme participates in starch and sucrose metabolism.
[edit] Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JF4 and 2JG0.
[edit] References
- KALF GF, RIEDER SV (1958). "The purification and properties of trehalase". J. Biol. Chem. 230 (2): 691–8. PMID 13525386.
- Myrback K and Ortenblad B (1937). "Trehalose und Hefe. II. Trehalasewirkung von Hefepraparaten". Biochem. Z. 291: 61–69.
 |
This hydrolase article is a stub. You can help Wikipedia by expanding it. |
