, Volume 11, Issue 1, pp 63–67 | Cite as

Interaction of aluminum ion with ATP. Mechanism of the aluminum inhibition of glycerol kinase and its reversal by spermine

  • Masataka Yoshino
  • Keiko Murakami
  • Keiichi Kawano


Aluminum ion inhibited yeast glycerol kinase competitively with respect to the substrate MgATP. The K value of the enzyme for aluminum ion was about 3 μM. Spermine at physiological concentrations prevented glycerol kinase from the inhibition by aluminum ion. Nuclear magnetic resonance spectroscopy showed the specific elimination by spermine of aluminum from the metal-ATP complex, but no dissociation of MgATP complex by spermine. Inhibition by aluminum ion of glycerol kinase as well as hexokinase can reduce the utilization of energy fuel in yeast. Change in polyamine concentration may control energy production in vivo, and is responsible for the development of age-related aluminum toxicity. © Rapid Science 1998.

aluminum ion glycerol kinase NMR spermine yeast 


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Copyright information

© Kluwer Academic Publishers 1998

Authors and Affiliations

  • Masataka Yoshino
    • 1
  • Keiko Murakami
    • 1
  • Keiichi Kawano
    • 2
  1. 1.Department of BiochemistryAichi Medical University NagakuteJapan
  2. 2.Division of Biological Sciences, Graduate School of ScienceHokkaido University SapporoJapan

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