Acetate kinase from Veillonella alcalescens. Regulation of enzyme activity by succinate and substrates

C. M. Bowman, R. O. Valdez, J. S. Nishimura

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20 Scopus citations


Acetate kinase of V. alcalescens has been shown to be a highly regulated enzyme exhibiting two levels of control: the requirement for succinate as a heterotropic allosteric effector, and cooperative binding at the substrate level. Succinate addition was necessary for enzymatic activity in both the direction of acyl phosphate synthesis and that of ATP synthesis. Control at the substrate level was apparent in the cooperative binding (Hill coefficients of 2) of acetyl phosphate, ATP, and ADP. Typical Michaelis kinetic data were observed for succinate (K(a) = 20 mM for acetyl phosphate synthesis, 0.4 mM for ATP synthesis), acetate, and propionate. The primary effect of succinate was to increase the apparent V(max) of the enzymatic reaction for the variable substrates, ATP, ADP, and acetyl phosphate. The results are interpreted as evidence that, as a heterotropic effector of the acetate kinase reaction, succinate may regulate levels of propionyl CoA (produced from propionyl phosphate by action of phosphotransacetylase), a compound required for the conversion of succinate to propionate. Acetate kinase has been shown to be a probable dimeric protein composed of two subunits of molecular weight 44,000 each.

Original languageEnglish (US)
Pages (from-to)3117-3121
Number of pages5
JournalJournal of Biological Chemistry
Issue number10
StatePublished - 1976
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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