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
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure 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 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

• GH31 in CAZypedia

References

1. 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.
2. 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.
3. 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.
4. "Home". CAZy.org. Retrieved 2018-03-06.
5. 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.
6. "Glycoside Hydrolase Family 31". CAZypedia.org. Retrieved 2018-03-06.
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.

This article incorporates text from the public domain Pfam and InterPro: IPR000322