Pathways & interactions
Glycoside hydrolase family 65, N-terminal domain superfamily (IPR037018)
Short name: Glyco_hydro_65_N_sf
- Glycoside hydrolase, family 65, N-terminal (IPR005196)
- Putative carbohydrate binding domain (IPR009342)
- Glycosyl hydrolase 94 (IPR010383)
- Galactose mutarotase-like domain superfamily (IPR011013)
- Cellobionic acid phosphorylase, N-terminal (IPR037814)
- NdvB, GH94N domain 1 (IPR037820)
- Cellobiose phosphorylase, N-terminal (IPR037825)
- N,N'-diacetylchitobiose phosphorylase, N-terminal (IPR037828)
O-Glycosyl 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 glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [PMID: 7624375, PMID: 8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.
This entry represents the N-terminal domain superfamily of the glycoside hydrolase family 65 proteins. The family of glycosyl hydrolases (GH65) containing this domain includes vacuolar acid trehalase and maltose phosphorylase. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity [PMID: 11587643] although its precise function remains unknown.
- G3DSA:126.96.36.199 (G3DSA:188.8.131.52)