InterPro domain: IPR013780

O-Glycosyl hydrolases ( 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 [ 1 , 2 ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.

This entry represents the all-beta domain superfamily that is found in several members of the glycosyl hydrolase family 13 and other glycosyl hydrolases. It is usually located C-terminal to the catalytic beta/alpha barrel domain. The structure of this domain has been found to be a Greek key beta-sheet fold [ 3 , 4 , 5 , 6 ].

1. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 92, 7090-4
2. Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-9
3. Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. J. Mol. Biol. 246, 545-59
4. Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J. Mol. Biol. 326, 177-88
5. Crystal structure of the covalent intermediate of amylosucrase from Neisseria polysaccharea. Biochemistry 43, 3104-10
6. The molecular defect leading to Fabry disease: structure of human alpha-galactosidase. J. Mol. Biol. 337, 319-35