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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]
An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid. [10] When used as a food additive, amylase has E number E1100, and may be derived from pig pancreas or mold fungi. Bacilliary amylase is also used in clothing and dishwasher detergents to dissolve starches from fabrics and dishes.
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.
A diastase (/ ˈ d aɪ ə s t eɪ z /; from Greek διάστασις, "separation") is any one of a group of enzymes that catalyses the breakdown of starch into maltose.For example, the diastase α-amylase degrades starch to a mixture of the disaccharide maltose; the trisaccharide maltotriose, which contains three α (1-4)-linked glucose residues; and oligosaccharides, known as dextrins, that ...
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.
Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene. [5] [6]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.
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