Alpha,alpha-trehalase
From Wikipedia, the free encyclopedia
alpha,alpha-trehalase | |||||||||
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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 | ||||||||
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In enzymology, an alpha,alpha-trehalase (EC 3.2.1.28) is an enzyme with system name alpha,alpha-trehalose glucohydrolase.[1][2][3][4] This enzyme catalyzes the chemical reaction
- alpha,alpha-trehalose + H2O 2 D-glucose
Thus, 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.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JF4 and 2JG0.
References
- ↑ Myrbäck, K. and Örtenblad, B. (1937). "Trehalose und Hefe. II. Trehalasewirkung von Hefepräparaten". Biochem. Z. 291: 61–69.
- ↑ Kalf, G.F. and Rieder, S.V. (1958). "The preparation and properties of trehalase". J. Biol. Chem. 230 (2): 691–698. PMID 13525386.
- ↑ Hehre, E.J., Sawai, T., Brewer, C.F., Nakano, M. and Kanda, T. (1982). "Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride". Biochemistry 21: 3090–3097. doi:10.1021/bi00256a009. PMID 7104311.
- ↑ Mori, H., Lee, J.H., Okuyama, M., Nishimoto, M., Ohguchi, M., Kim, D., Kimura, A. and Chiba, S. (2009). "Catalytic reaction mechanism based on α-secondary deuterium isotope effects in hydrolysis of trehalose by European honeybee trehalase". Biosci. Biotechnol. Biochem. 73: 2466–2473. doi:10.1271/bbb.90447. PMID 19897915.
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