Alpha amylase
IPR006046
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. Alpha-amylases, which belong to glycoside hydrolase family 13, are 1,4-alpha-D-glucan glucanohydrolases, which degrade both the branched and unbranched forms of starch by cleaving the internal alpha-1,4 bonds connecting the glucose monomers. The products of these reactions are maltose and maltotriose, which are further degraded to glucose by maltases. One atom of calcium is required to bind to each protein molecule to allow it to function, but excess calcium can inhibit activity by binding to amino acids that are required for the catalytic activity of the enzyme.
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.
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