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  • Title: Chemical specificity of pyruvate kinase from yeast.
    Author: Blumberg K, Stubbe J.
    Journal: Biochim Biophys Acta; 1975 Mar 28; 384(1):120-6. PubMed ID: 1093568.
    Abstract:
    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.
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