Glycoside hydrolase family 53

Glycosyl hydrolase family 53
crystal structure of beta-1,4-galactanase from aspergillus aculeatus at 100k
Identifiers
Symbol Glyco_hydro_53
Pfam PF07745
Pfam clan CL0058
InterPro IPR011683
SCOP 1fob
CAZy GH53

In molecular biology, glycoside hydrolase family 53 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]

These enzymes are endo-1,4- beta-galactanases EC 3.2.1.89. The structure of this domain is known [6] and has a TIM barrel fold.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41477. 
  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. ^ Ryttersgaard C, Lo Leggio L, Coutinho PM, Henrissat B, Larsen S (December 2002). "Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A". Biochemistry 41 (51): 15135–43. PMID 12484750. 

This article incorporates text from the public domain Pfam and InterPro IPR011683