Alpha-amylase enzyme Overview
Alpha-amylase is a calcium-dependent metalloenzyme that catalyzes the endohydrolysis of internal α-(1→4)-D-glucosidic linkages in large polysaccharides such as starch and glycogen, producing smaller sugars like maltose and dextrins.[5][6] It is widely distributed among living organisms; in humans it exists primarily as two isoenzymes—salivary alpha-amylase ("ptyalin") produced by salivary glands for initial carbohydrate digestion in the mouth, and pancreatic alpha-amylase secreted into the small intestine for further breakdown during digestion.[6][2] The enzyme has a characteristic three-domain structure with an eight-stranded α/β barrel catalytic domain containing key acidic residues essential for its function.[1][5] Alpha-amylases play a crucial role in nutrition by enabling efficient energy extraction from dietary carbohydrates. Clinically, serum amylase measurement serves as an important diagnostic marker for acute pancreatitis.[2] Pharmacologically, inhibition of this enzyme is targeted to manage postprandial hyperglycemia in diabetes mellitus through drugs like acarbose that competitively block its active site.[5][3]
Mechanism of Action
Competitive inhibition of the active site to reduce enzymatic breakdown of dietary starches, thereby lowering postprandial blood glucose spikes
Biological Functions
Disease Associations
Safety Considerations
- Gastrointestinal side effects with inhibitors such as acarbose or miglitol, including flatulence, diarrhea, abdominal discomfort due to undigested carbohydrates reaching the colon.
- Risk of hypoglycemia when used in combination with other antidiabetic agents.
Interacting Drugs
Associated Biomarkers
Biomarker |
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Serum amylase levels for diagnosis/monitoring of acute pancreatitis and other pancreatic diseases |