Affordable Access

Publisher Website

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

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
334
Issue
1
Identifiers
DOI: 10.1016/0014-5793(93)81687-u
Keywords
  • Adenylate Kinase
  • Ump-Cmp Kinase
  • Site-Directed Mutagenesis
  • Substrate Specificity
  • Amp-Binding
Disciplines
  • Biology

Abstract

Abstract Adenylate kinase is highly specific for AMP as phosphoryl acceptor. We have found that the replacement of Thr 39 by Ala in the chicken muscle enzyme, alone or together with the replacement of Leu 66 by 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 Thr 39 has a V max value for CMP comparable to that of CMP-UMP kinase.

There are no comments yet on this publication. Be the first to share your thoughts.