Glycoside hydrolase family 31
| Glycosyl hydrolases family 31 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structure of the yici thiosugar michaelis complex | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_31 | ||||||||
| Pfam | PF01055 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR000322 | ||||||||
| PROSITE | PDOC00120 | ||||||||
| CAZy | GH31 | ||||||||
| Membranome | 523 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 31 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 31 CAZY GH_31 comprises enzymes with several known activities; alpha-glucosidase (EC 3.2.1.20), alpha-galactosidase (EC 3.2.1.22); glucoamylase (EC 3.2.1.3), sucrase-isomaltase (EC 3.2.1.48) (EC 3.2.1.10); alpha-xylosidase (EC 3.2.1); alpha-glucan lyase (EC 4.2.2.13).
Glycoside hydrolase family 31 groups a number of glycosyl hydrolases on the basis of sequence similarities[8][9][10] An aspartic acid has been implicated[11] in the catalytic activity of sucrase, isomaltase, and lysosomal alpha-glucosidase.
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. 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 31". 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. PMID 29040563.
- ^ 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.
- ^ Kinsella BT, Hogan S, Larkin A, Cantwell BA (December 1991). "Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase". European Journal of Biochemistry. 202 (2): 657–64. doi:10.1111/j.1432-1033.1991.tb16420.x. PMID 1761061.
- ^ Naim HY, Niermann T, Kleinhans U, Hollenberg CP, Strasser AW (December 1991). "Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene". FEBS Letters. 294 (1–2): 109–12. doi:10.1016/0014-5793(91)81353-A. PMID 1743281. S2CID 6086792.
- ^ Hermans MM, Kroos MA, van Beeumen J, Oostra BA, Reuser AJ (July 1991). "Human lysosomal alpha-glucosidase. Characterization of the catalytic site". The Journal of Biological Chemistry. 266 (21): 13507–12. doi:10.1016/S0021-9258(18)92727-4. PMID 1856189.