Jump to content

Glycoside hydrolase family 31

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Rjwilmsi (talk | contribs) at 06:55, 13 August 2016 (top: Journal cites:, added 1 DOI using AWB (12076)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Glycosyl hydrolases family 31
structure of the yici thiosugar michaelis complex
Identifiers
SymbolGlyco_hydro_31
PfamPF01055
Pfam clanCL0058
InterProIPR000322
PROSITEPDOC00120
CAZyGH31
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]

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[6][7][8] An aspartic acid has been implicated[9] in the catalytic activity of sucrase, isomaltase, and lysosomal alpha-glucosidase.

References

  1. ^ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
  2. ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
  3. ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
  4. ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
  5. ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
  6. ^ Henrissat B (December 1991). "A classification of glycosyl hydrolases based on amino acid sequence similarities". Biochem. J. 280 (2): 309–16. doi:10.1042/bj2800309. PMC 1130547. PMID 1747104.
  7. ^ 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". Eur. J. Biochem. 202 (2): 657–64. doi:10.1111/j.1432-1033.1991.tb16420.x. PMID 1761061.
  8. ^ 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 Lett. 294 (1–2): 109–12. doi:10.1016/0014-5793(91)81353-A. PMID 1743281.
  9. ^ van Beeumen J, Kroos MA, Oostra BA, Hermans MM, Reuser AJ (1991). "Human lysosomal alpha-glucosidase. Characterization of the catalytic site". J. Biol. Chem. 266 (21): 13507–13512. PMID 1856189.
This article incorporates text from the public domain Pfam and InterPro: IPR000322