Glycoside hydrolase family 5
| Cellulase (glycosyl hydrolase family 5) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Cellulase | ||||||||
| Pfam | PF00150 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR001547 | ||||||||
| PROSITE | PDOC00565 | ||||||||
| SCOP | 2exo | ||||||||
| SUPERFAMILY | 2exo | ||||||||
| OPM superfamily | 125 | ||||||||
| OPM protein | 2osx | ||||||||
| CAZy | GH5 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 5 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/Glycoside-Hydrolases.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]
Glycoside hydrolase family 5 CAZY GH_5 comprises enzymes with several known activities including endoglucanase (EC 3.2.1.4); beta-mannanase (EC 3.2.1.78); exo-1,3-glucanase (EC 3.2.1.58); endo-1,6-glucanase (EC 3.2.1.75); xylanase (EC 3.2.1.8); endoglycoceramidase (EC 3.2.1.123).
The microbial degradation of cellulose and xylans requires several types of enzymes. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of these families is known as the cellulase family A[6] or as the glycosyl hydrolases family 5.[7] One of the conserved regions in this family contains a conserved glutamic acid residue which is potentially involved[8] in the catalytic mechanism.
In a recent study using Molecular Dynamics simulations, a considerable correlation between thermal stability and structural rigidity of members of family 5 with solved structures has been proved.[9]
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.
- ↑ Henrissat B, Tomme P, Claeyssens M, Mornon JP, Lemesle L (1989). "Cellulase families revealed by hydrophobic cluster analysis". Gene. 81 (1): 83–95. doi:10.1016/0378-1119(89)90339-9. PMID 2806912.
- ↑ Henrissat B (1991). "A classification of glycosyl hydrolases based on amino acid sequence similarities". Biochem. J. 280: 309–316. doi:10.1042/bj2800309. PMC 1130547. PMID 1747104.
- ↑ Haiech J, Chippaux M, Barras F, Py B, Bortoli-German I (1991). "Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis". Protein Eng. 4 (3): 325–333. doi:10.1093/protein/4.3.325. PMID 1677466.
- ↑ Badieyan, S; Bevan DR; Zhang C (January 2012). "Study and design of stability in GH5 cellulases.". Biotechnology and Bioengineering. 109 (1): 31–44. doi:10.1002/bit.23280. PMID 21809329.