Glycoside hydrolase family 52
| Glyco_hydro_52 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Glyco_hydro_52 | ||||||||
| Pfam | PF03512 | ||||||||
| InterPro | IPR000852 | ||||||||
| CAZy | GH52 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 52 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 52 CAZY GH_52 comprises enzymes with only one known activity; beta-xylosidase (EC 3.2.1.37).
Proteins harboring beta-xylosidase and xylanase activities [6] have been identified in the Gram-positive, facultative thermophilic aerobe Bacillus stearothermophilus 21.[6] This microbe, which functions in xylan degradation, can utilise xylan as a sole source of carbon. The enzyme hydrolyses 1,4-beta-D-xylans, removing successive D-xylose residues from the non-reducing termini. It also hydrolyses xylobiose.
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 Baba T, Shinke R, Nanmori T (July 1994). "Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus stearothermophilus 21". Appl. Environ. Microbiol. 60 (7): 2252–8. PMC 201640. PMID 8074507.
This article incorporates text from the public domain Pfam and InterPro IPR000852