Glycoside hydrolase family 30
| O-Glycosyl hydrolase family 30 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of a xylanase from glycoside hydrolase family 5.[1] | |||||||||||
| Identifiers | |||||||||||
| Symbol | Glyco_hydro_30 | ||||||||||
| Pfam | PF02055 | ||||||||||
| Pfam clan | CL0058 | ||||||||||
| InterPro | IPR001139 | ||||||||||
| SCOP2 | 1nof / SCOPe / SUPFAM | ||||||||||
| OPM superfamily | 125 | ||||||||||
| OPM protein | 1ogs | ||||||||||
| |||||||||||
In molecular biology, glycoside hydrolase family 30 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.[2][3][4] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6]
Glycoside hydrolase family 30 CAZY GH_30 includes the mammalian glucosylceramidases. Human acid beta-glucosidase (D-glucosyl-N-acylsphingosine glucohydrolase), cleaves the glucosidic bonds of glucosylceramide and synthetic beta-glucosides.[7] Any one of over 50 different mutations in the gene of glucocerebrosidase have been found to affect activity of this hydrolase, producing variants of Gaucher disease, the most prevalent lysosomal storage disease.[7][8]
References
- ^ Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A (July 2003). "First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis". Biochemistry. 42 (28): 8411–22. doi:10.1021/bi034144c. PMID 12859186.
- ^ 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.
- ^ a b Legler G, Desnick RJ, Dinur T, Osiecki KM, Gatt S, Grabowski GA (1986). "Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site". Proc. Natl. Acad. Sci. U.S.A. 83 (6): 1660–1664. doi:10.1073/pnas.83.6.1660. PMC 323143. PMID 3456607.
- ^ Iwasawa K, Ida H, Eto Y (1997). "Differences in origin of the 1448C mutation in patients with Gaucher disease". Acta Paediatr. Jpn. Overseas Ed. 39 (4): 451–453. PMID 9316290.