Glycoside hydrolase family 92
In molecular biology, glycoside hydrolase family 92 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]
This domain occurs within alpha-1,2-mannosidases, which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.[6]
Glycoside hydrolase family 92 includes enzymes with mannosyl-oligosaccharide α-1,2-mannosidase EC 3.2.1.113, mannosyl-oligosaccharide α-1,3-mannosidase EC 3.2.1.-, mannosyl-oligosaccharide α-1,6-mannosidase EC 3.2.1.-, α-mannosidase EC 3.2.1.24, α-1,2-mannosidase EC 3.2.1.-, α-1,3-mannosidase EC 3.2.1.- and α-1,4-mannosidase EC 3.2.1.- activities. It includes enzymes critical for the maturation of N-linked oligosaccharides and ER-associated degradation.[6]
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.
- 1 2 Liu Y, Choudhury P, Cabral CM, Sifers RN (February 1999). "Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome". J. Biol. Chem. 274 (9): 5861–7. doi:10.1074/jbc.274.9.5861. PMID 10026209.
This article incorporates text from the public domain Pfam and InterPro IPR012939
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