Amylases: enzymatic mechanisms

Basic Life Sci. 1981;18:151-82. doi: 10.1007/978-1-4684-3980-9_10.


Many types of amylases are found throughout the animal, vegetable and microbial kingdoms. They have evolved along different pathways to enable the organism to convert insoluble starch (or glycogen) into low molecular weight, water soluble dextrins and sugars. Alpha amylases are dextrinogenic and can attack the interior of starch molecules. The products retain the alpha anomeric configuration. Beta amylases act only at the non-reducing chain ends and liberate only beta maltose. Both alpha and beta amylases exhibit multiple (repetitive) attack, that is, after the initial catalytic cleavage, the enzyme may remain attached to the substrate and lead to several more cleavages before dissociation of the enzyme-substrate complex. Amylases have extended substrate binding sites, in the range 4-9 glucose units. This enables the enzyme to stress the substrate and lower the activation energy for hydrolysis. Similarly the enzyme exerts a torsion on the glucose unit at the catalytic site, inducing a transition state conformation (oxycarbonium ion). Alpha and beta amylases differ in the stereospecific hydration of the oxycarbonium ion, in the sequence of liberation of the right-hand vs the left-hand product, and the direction of motion of the retained substrate to give multiple attack.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amylases / metabolism*
  • Bacillus subtilis / enzymology
  • Binding Sites
  • Kinetics
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • alpha-Amylases / metabolism


  • Amylases
  • alpha-Amylases