Chemical specificity of pyruvate kinase from yeast.
Three analogs of phosphoenolpyruvic acid: (Z)-phosphoenol-3-fluoropyruvate, (Z)-phosphoenol-3-bromopyruvate and (Z)-phosphoenol-alpha-ketobutyrate were found to be substrates for yeast pyruvate kinase (ATP: pyruvate (Z)-O-phosphotransferase, EC 2.7.1.40)with maximal velocities much greater than those found for rabbit muscle pyruvate kinase. The analogs exhibited sigmoidal kinetics, which become hyperbolic upon addition of the allosteric effector, fructose 1,6-diphosphate. Moreover, the reaction of (Z)-phosphoenol-3-bromopyruvate with ADP to produce bromopyruvic acid and ATP irreversibly inhibited the enzyme with a half-life of 32 min.[1]References
- Chemical specificity of pyruvate kinase from yeast. Blumberg, K., Stubbe, J. Biochim. Biophys. Acta (1975) [Pubmed]
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