Glycoside hydrolase family 10
| Glycoside hydrolase, family 10 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the catalytic domain of xylanase a from streptomyces halstedii jm8 | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_10 | ||||||||
| Pfam | PF00331 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR001000 | ||||||||
| PROSITE | PDOC00510 | ||||||||
| SCOP2 | 2exo / SCOPe / SUPFAM | ||||||||
| CAZy | GH10 | ||||||||
| |||||||||
In molecular biology, Glycoside hydrolase family 10 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 10 CAZY GH_10 comprises enzymes with a number of known activities; xylanase (EC 3.2.1.8); endo-1,3-beta-xylanase (EC 3.2.1.32); cellobiohydrolase (EC 3.2.1.91). These enzymes were formerly known as cellulase family F.
The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) (exoglucanases), or xylanases (EC 3.2.1.8).[8][9] 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 F[10] or as the glycosyl hydrolases family 10.[11]
References
[edit]- ^ 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. Bibcode:1995PNAS...92.7090H. 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): 695–6. doi:10.1042/bj3160695. 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. PMC 3965031. PMID 24270786.
- ^ "Glycoside Hydrolase Family 10". CAZypedia.org. Retrieved 2018-03-06.
- ^ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes". Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. hdl:21.11116/0000-0003-B7EB-6. PMID 29040563.
- ^ Béguin P (1990). "Molecular biology of cellulose degradation". Annual Review of Microbiology. 44: 219–48. doi:10.1146/annurev.mi.44.100190.001251. PMID 2252383.
- ^ Gilkes NR, Henrissat B, Kilburn DG, Miller RC, Warren RA (June 1991). "Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families". Microbiological Reviews. 55 (2): 303–15. doi:10.1128/MMBR.55.2.303-315.1991. PMC 372816. PMID 1886523.
- ^ 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 (2): 309–16. doi:10.1042/bj2800309. PMC 1130547. PMID 1747104.
