Glycoside hydrolase, family 65, central catalytic (IPR005195)

Short name: Glyco_hydro_65_M

Overlapping homologous superfamilies

Domain relationships



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.

The family of glycosyl hydrolases (GH65) which contains 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. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucelophilic attack on the anomeric carbon atom [PMID: 11587643]. The catalytic domain also forms the majority of the dimerisation interface.

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0003824 catalytic activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.