Glycoside hydrolase family 38, N-terminal domain

Definition

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 [[cite:PMID:7624375], [cite:PMID:8535779]]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website. Glycoside hydrolase family 38 [cazy:GH38] comprises enzymes with only one known activity; alpha-mannosidase ([ec:3.2.1.24]) ([ec: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. This entry represents the N-terminal domain of the glycoside hydrolase 38 family protein.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• MAN2A1
• MAN2A2
• MAN2B1
• MAN2B2
• MAN2C1