Glycoside hydrolase family 17

Glycoside hydrolase, family 17
crystal structure at 1.45- resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome
Identifiers
Symbol	Glyco_hydro_17
Pfam	PF00332
Pfam clan	CL0058
InterPro	IPR000490
PROSITE	PDOC00507
SCOP	1ghs
SUPERFAMILY	1ghs
CAZy	GH17
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, Glycoside hydrolase family 17 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 17 CAZY GH_17 comprises enzymes with several known activities; endo-1,3-beta-glucosidase (EC 3.2.1.39); lichenase (EC 3.2.1.73); exo-1,3-glucanase (EC 3.2.1.58). Currently these enzymes have only been found in plants and in fungi.

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.

This article incorporates text from the public domain Pfam and InterPro IPR000490