InterPro domain: IPR015341

This entry represents a domain found in members of the glycosyl hydrolases families 38. This domain is found in the central region that adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase [ 1 ].

Glycoside hydrolase family 38 GH38 comprises enzymes with only one known activity; alpha-mannosidase ( 3.2.1.24 ) ( 3.2.1.114 ).

Lysosomal alpha-mannosidase is necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. The enzyme catalyses the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis (AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains.

1. The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation. J. Mol. Biol. 327, 631-44