Glycoside hydrolase family 70

Glycosyl hydrolase family 70
Identifiers
Symbol Glyco_hydro_70
Pfam PF02324
Pfam clan CL0058
InterPro IPR003318
CAZy GH70

In molecular biology, glycoside hydrolase family 70 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 family includes glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) (EC 2.4.1.5CAZY GH_70) which catalyse the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules.[6] Some members of this family contain a cell wall-binding repeat.

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 41477Freely accessible. PMID 7624375.
  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. Croux C, Monchois V, Willemot RM, Remaud-simeon M, Monsan P (1996). "Cloning and sequencing of a gene coding for a novel dextransucrase from Leuconostoc mesenteroides NRRL B-1299 synthesizing only alpha (1-6) and alpha (1-3) linkages". Gene. 182 (1–2): 23–32. doi:10.1016/S0378-1119(96)00443-X. PMID 8982063.

This article incorporates text from the public domain Pfam and InterPro IPR003318

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