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 .
^ 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 .
Activity Regulation Classification Kinetics Types