v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | 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 [ ]. Glycoside hydrolase family 38 comprises enzymes with only one known activity; alpha-mannosidase ( ) ( ). 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. |
Short Name | Glyco_hydro_38_cen |