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 | 117 | ||||||||
| OPM protein | 2osx | ||||||||
| CAZy | GH5 | ||||||||
| Membranome | 1365 | ||||||||
| |||||||||
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 web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]
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[8] or as the glycosyl hydrolases family 5.[9] One of the conserved regions in this family contains a conserved glutamic acid residue which is potentially involved[10] 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.[11]
External links
References
- ↑ Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- ↑ Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ↑ Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 ( Pt 2) (Pt 2): 695–6. PMC 1217404. PMID 8687420.
- ↑ "Home". CAZy.org. Retrieved 2018-03-06.
- ↑ Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490–5. doi:10.1093/nar/gkt1178. PMID 24270786.
- ↑ "Glycoside Hydrolase Family 5". CAZypedia.org. Retrieved 2018-03-06.
- ↑ "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes". Glycobiology. 28 (1): 3–8. December 2018. doi:10.1093/glycob/cwx089. PMID 29040563.
- ↑ Henrissat B, Claeyssens M, Tomme P, Lemesle L, Mornon JP (September 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 (December 1991). "A classification of glycosyl hydrolases based on amino acid sequence similarities". The Biochemical Journal. 280 ( Pt 2): 309–16. doi:10.1042/bj2800309. PMC 1130547. PMID 1747104.
- ↑ Py B, Bortoli-German I, Haiech J, Chippaux M, Barras F (February 1991). "Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis". Protein Engineering. 4 (3): 325–33. 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.