Direct Mg2+ binding activates adenylate kinase from Escherichia coli

Yan Wen Tan, Jeffrey A. Hanson, Haw Yang

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


We report evidence that adenylate kinase (AK) from Escherichia coli can be activated by the direct binding of a magnesium ion to the enzyme, in addition to ATP-complexed Mg2+. By systematically varying the concentrations of AMP, ATP, and magnesium in kinetic experiments, we found that the apparent substrate inhibition of AK, formerly attributed to AMP, was suppressed at low magnesium concentrations and enhanced at high magnesium concentrations. This previously unreported magnesium dependence can be accounted for by a modified random bi-bi model in which Mg2+ can bind to AK directly prior to AMP binding. A new kinetic model is proposed to replace the conventional random bi-bi mechanism with substrate inhibition and is able to describe the kinetic data over a physiologically relevant range of magnesium concentrations. According to this model, the magnesium-activated AK exhibits a 23- ± 3-fold increase in its forward reaction rate compared with the unactivated form. The findings imply that Mg2+ could be an important affecter in the energy signaling network in cells.

Original languageEnglish (US)
Pages (from-to)3306-3313
Number of pages8
JournalJournal of Biological Chemistry
Issue number5
StatePublished - Jan 30 2009
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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