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α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]
Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene. [3] This gene is found in many organisms. Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and g
Enzymes containing this domain belong to family 13 of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose .
Glucan 1,4-alpha-maltohydrolase (EC 3.2.1.133, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with systematic name 4-alpha-D-glucan alpha-maltohydrolase. [ 1 ] [ 2 ] This enzyme catalyses the following chemical reaction
A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases. [3] The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme.
Glucan 1,4-α-glucosidase (EC 3.2.1.3, glucoamylase, amyloglucosidase, γ-amylase, lysosomal α-glucosidase, acid maltase, exo-1,4-α-glucosidase, glucose amylase, γ-1,4-glucan glucohydrolase, acid maltase, 1,4-α-D-glucan glucohydrolase) is an enzyme located on the brush border of the small intestine with systematic name 4-α-D-glucan glucohydrolase.
Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside] bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas .
Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity. Recombinant enzyme studies have shown that its N-terminal catalytic domain has highest activity against maltose, while the C-terminal domain has a broader substrate specificity and activity against glucose oligomers. [7]