Biology:Alpha,alpha-trehalase
From HandWiki
| α,α-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 / QuickGO | ||||||||
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An α,α-trehalase (EC 3.2.1.28) is an enzyme with systematic name α,α-trehalose glucohydrolase.[1][2][3][4] This enzyme catalyzes the chemical reaction
- α,α-trehalose + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 2 D-glucose
Thus, the two substrates of this enzyme are αα-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. It is also called trehalase, and it participates in starch and sucrose metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JF4 and 2JG0.
References
- ↑ "Trehalose und Hefe. II. Trehalasewirkung von Hefepräparaten". Biochem. Z. 291: 61–69. 1937.
- ↑ "The purification and properties of trehalase". The Journal of Biological Chemistry 230 (2): 691–8. February 1958. PMID 13525386.
- ↑ "Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride". Biochemistry 21 (13): 3090–7. June 1982. doi:10.1021/bi00256a009. PMID 7104311.
- ↑ "Catalytic reaction mechanism based on α-secondary deuterium isotope effects in hydrolysis of trehalose by European honeybee trehalase". Bioscience, Biotechnology, and Biochemistry 73 (11): 2466–73. November 2009. doi:10.1271/bbb.90447. PMID 19897915.
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