Α,α-Trehalase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by BU RoBOT (talk | contribs) at 13:44, 10 August 2016 (→‎References: Sort into more specific stub template based on presence in Category:EC 3.2 or subcategories (Task 25)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

alpha,alpha-trehalase
Identifiers
EC no.3.2.1.28
CAS no.9025-52-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

  1. ^ Myrbäck K, Örtenblad B (1937). "Trehalose und Hefe. II. Trehalasewirkung von Hefepräparaten". Biochem. Z. 291: 61–69.
  2. ^ Kalf GF, Rieder SV (February 1958). "The purification and properties of trehalase". The Journal of Biological Chemistry. 230 (2): 691–8. PMID 13525386.
  3. ^ Hehre EJ, Sawai T, Brewer CF, Nakano M, Kanda T (June 1982). "Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with alpha- and beta-D-glucosyl fluoride". Biochemistry. 21 (13): 3090–7. doi:10.1021/bi00256a009. PMID 7104311.
  4. ^ Mori H, Lee JH, Okuyama M, Nishimoto M, Ohguchi M, Kim D, Kimura A, Chiba S (November 2009). "Catalytic reaction mechanism based on alpha-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.