Glycoside hydrolase family 12

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Glycosyl hydrolase family 12
comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability
Identifiers
SymbolGlyco_hydro_12
PfamPF01670
Pfam clanCL0004
InterProIPR002594
SCOP21nlr / SCOPe / SUPFAM
CAZyGH12
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, Glycoside hydrolase family 12 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 12 CAZY GH_12 comprises enzymes with the following activities: endoglucanase (EC 3.2.1.4), xyloglucan hydrolase (EC 3.2.1.151), β-1,3-1,4-glucanase (EC 3.2.1.73) and xyloglucan endotransglycosylase (EC 3.2.1.207). These enzymes were formerly known as cellulase family H.

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 41477. 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.
This article incorporates text from the public domain Pfam and InterPro: IPR002594