α,α-Trehalase
| α,α-Trehalase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.28 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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 2 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
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JF4 and 2JG0.
References
[edit]- ^ Myrbäck K, Örtenblad B (1937). "Trehalose und Hefe. II. Trehalasewirkung von Hefepräparaten". Biochem. Z. 291: 61–69.
- ^ Kalf GF, Rieder SV (February 1958). "The purification and properties of trehalase". The Journal of Biological Chemistry. 230 (2): 691–8. doi:10.1016/S0021-9258(18)70491-2. PMID 13525386.
- ^ Hehre EJ, Sawai T, Brewer CF, Nakano M, Kanda T (June 1982). "Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride". Biochemistry. 21 (13): 3090–7. doi:10.1021/bi00256a009. PMID 7104311.
- ^ Mori H, Lee JH, Okuyama M, Nishimoto M, Ohguchi M, Kim D, Kimura A, Chiba S (November 2009). "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. doi:10.1271/bbb.90447. PMID 19897915. S2CID 22774772.
