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Introducing transglycosylation activity in a liquefying α‐amylase
Author(s) -
Saab-Rincón Gloria,
del-Rı́o Gabriel,
Santamarı́a Rosa I,
López-Munguı́a Agustı́n,
Soberón Xavier
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00671-7
Subject(s) - amylase , residue (chemistry) , enzyme , chemistry , active site , homology (biology) , stereochemistry , biochemistry , amino acid
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.