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
- ↑ 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. - ↑ 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.
- ↑ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- ↑ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- ↑ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- ↑ 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