Glycoside hydrolase family 37

Trehalase
Identifiers
Symbol Trehalase
Pfam PF01204
Pfam clan CL0059
InterPro IPR001661
PROSITE PDOC00717
CAZy GH37

In molecular biology, glycoside hydrolase family 37 is a family of glycoside hydrolases.

Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. [5]

Glycoside hydrolase family 37 CAZY GH_37 comprises enzymes with only one known activity; trehalase (EC 3.2.1.28). Trehalase is the enzyme responsible for the degradation of the disaccharide alpha,alpha-trehalose yielding two glucose subunits.[6] It is an enzyme found in a wide variety of organisms and whose sequence has been highly conserved throughout evolution.

References

  1. ^ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41477. 
  2. ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779. 
  3. ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
  4. ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
  5. ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
  6. ^ Kopp M, Holzer H, Muller H (1993). "Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae". J. Biol. Chem. 268 (7): 4766–4774. PMID 8444853. 

This article incorporates text from the public domain Pfam and InterPro IPR001661