| 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.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JF4 and 2JG0.
- ^ 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. 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.
| 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.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JF4 and 2JG0.
- ^ 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. 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.