Acetate kinase from Veillonella alcalescens. Regulation by succinate and substrates.
The kinetic properties of acetate kinase from Veillonella alcalescens were investigated. In the presence of high concentrations of nucleotide both forward and reverse reactions were observed. In the presence of succinate the degree of cooperativity between subunits of the homodimer decreased, i.e. the Hill coefficient, n, decreased from 2.5 to 1.4 for acetyl phosphate in the presence of succinate. At low substrate concentrations hyperbolic kinetic data were observed with succinate. We have proposed a modified version of the concerted symmetry model to describe the kinetics observed with this enzyme. The primary differentiating feature of the proposed model is the requirement for activator ligand binding for catalysis. In the absence of succinate, the substrate (acetate or acetyl phosphate) also functions as an activating ligand.
D000084:Acetate Kinase / Q000378:metabolism*; D000085:Acetates / Q000494:pharmacology; D000494:Allosteric Regulation; D001667:Binding, Competitive; D007700:Kinetics; D008433:Mathematics; D010770:Phosphotransferases / Q000378:metabolism*; D011485:Protein Binding; D013386:Succinates / Q000494:pharmacology*; D014678:Veillonella / Q000201:enzymology*
D000085:Acetates; D013386:Succinates; D010770:Phosphotransferases; D000084:Acetate Kinase