Glycoside hydrolase family 15
| Glycosyl hydrolases family 15 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Glyco_hydro_15 | ||||||||
| Pfam | PF00723 | ||||||||
| Pfam clan | CL0059 | ||||||||
| SCOP2 | 1glm / SCOPe / SUPFAM | ||||||||
| CAZy | GH15 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 15 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] y[ _]9
Glycoside hydrolase family 15 CAZY GH_15 comprises enzymes with several known activities; glucoamylase (EC 3.2.1.3); alpha-glucosidase (EC 3.2.1.20); glucodextranase (EC 3.2.1.70).
Glucoamylase (GA) catalyses the release of D-glucose from the non-reducing ends of starch and other oligo- or poly-saccharides. Studies of fungal GA have indicated 3 closely clustered acidic residues that play a role in the catalytic mechanism.[8] This region is also conserved in a recently sequenced bacterial GA.[9]
The 3D structure of the pseudo-tetrasaccharide acarbose complexed with glucoamylase II(471) from Aspergillus awamori var. X100 has been determined to 2.4A resolution.[10] The protein belongs to the mainly alpha class, and contains 19 helices and 9 strands.
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) (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 15". CAZypedia.org. Retrieved 2018-03-06.
- ^ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. hdl:21.11116/0000-0003-B7EB-6. PMID 29040563.
- ^ Sierks MR, Ford C, Reilly PJ, Svensson B (January 1990). "Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori". Protein Engineering. 3 (3): 193–8. doi:10.1093/protein/3.3.193. PMID 1970434.
- ^ Ohnishi H, Kitamura H, Minowa T, Sakai H, Ohta T (July 1992). "Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme". European Journal of Biochemistry. 207 (2): 413–8. doi:10.1111/j.1432-1033.1992.tb17064.x. PMID 1633799.
- ^ Aleshin AE, Firsov LM, Honzatko RB (June 1994). "Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution". The Journal of Biological Chemistry. 269 (22): 15631–9. doi:10.1016/S0021-9258(17)40728-9. PMID 8195212.
