Site-directed mutagenesis of AMP-binding residues in adenylate kinase Alteration of substrate specificity

  • Okajima T
  • Tanizawa K
  • Fukui T
  • 3


    Mendeley users who have this article in their library.
  • 19


    Citations of this article.


Adenylate kinase is highly specific for AMP as phosphoryl acceptor. We have found that the replacement of Thr39by Ala in the chicken muscle enzyme, alone or together with the replacement of Leu66by Ile, caused remarkable increases in CMP and UMP activities with a concomitant decrease in AMP activity; therefore, the resulting mutant enzymes show CMP and UMP activities/AMP activity ratios much higher than the wild-type enzyme. The mutant enzyme in which Ala is substituted for Thr39has a Vmaxvalue for CMP comparable to that of CMP-UMP kinase. © 1993.

Author-supplied keywords

  • AMP-binding
  • Adenylate kinase
  • Site-directed mutagenesis
  • Substrate specificity
  • UMP-CMP kinase

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Toshihide Okajima

  • Katsuyuki Tanizawa

  • Toshio Fukui

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free