Some kinetic properties of pyruvate kinase from Phycomyces blakesleeanus |
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| Institution: | 1. Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;2. Department of Biomedical, Metabolic and Neural Science, University of Modena and Reggio Emilia, Center for Neuroscience and Neurotechnology, 41125 Modena, Italy;1. Department of Molecular Biology and Genetics, Section for Crop Genetics and Biotechnology, Aarhus University, Forsogsvej 1, 4200 Slagelse, Denmark;2. Wageningen University, 6708PB Wageningen, The Netherlands |
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| Abstract: | - 1.1. Pyruvate kinase from mycelium of Phycomyces blakesleeanus NRRL 1555(−) has been partially purified and some kinetic properties has been investigated at pH 7.5.
- 2.2. Positive homotropic interactions were observed with phosphoenolpyruvate and Mg2+, showing Hill coefficient values of 2.8 and 2.5, respectively, whereas hyperbolic kinetics are found when ADP was the variable substrate.
- 3.3. Fructose 1,6-bisphosphate acts as a heterotropic allosteric activator, markedly decreasing the S0.5 value for phosphoenolpyruvate saturation curve from a sigmoidal to a hyperbolic form.
- 4.4. ATP inhibits pyruvate kinase from mycelium of Phycomyces blakesleeanus. ATP appears to be a non-competitive inhibitor with respect PEP and competitive inhibitor with respect ADP.
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