Glycoside hydrolase family 3
In molecular biology, glycoside hydrolase family 3 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 3 CAZY GH_3 comprises enzymes with a number of known activities; beta-glucosidase (EC 3.2.1.21); beta-xylosidase (EC 3.2.1.37); N-acetyl beta-glucosaminidase (EC 3.2.1.52); glucan beta-1,3-glucosidase (EC 3.2.1.58); cellodextrinase (EC 3.2.1.74); exo-1,3-1,4-glucanase (EC 3.2.1). These enzymes are two-domain globular proteins that are N-glycosylated at three sites.[6]
External links
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.
- ↑ Varghese JN, Fincher GB, Hrmova M (1999). "Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase". Structure 7 (2): 179–190. doi:10.1016/S0969-2126(99)80024-0. PMID 10368285.
This article incorporates text from the public domain Pfam and InterPro IPR001764
This article incorporates text from the public domain Pfam and InterPro IPR002772
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