Introducing transglycosylation activity in a liquefying α‐amylase

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Abstract
By mutating Ala‐289 by Phe or Tyr in the Bacillus stearothermophilus α‐amylase, we induced this enzyme to perform alcoholytic reactions, a function not present in the wild‐type enzyme. This residue was selected from homology analysis with neopullulanase, where the residue has been implicated in the control of transglycosylation [Kuriki et al. (1996) J. Biol. Chem. 271, 17321–17329]. We made some inferences about the importance of electrostatic and geometrical modifications in the active site environment of the amylase to explain the behavior of the modified enzyme.