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. 1974 Jul;141(1):165–171. doi: 10.1042/bj1410165

Kinetic properties of cerebral pyruvate kinase

Peter C Nicholas 1, Herman S Bachelard 1
PMCID: PMC1168063  PMID: 4455200

Abstract

Partly purified guinea-pig brain pyruvate kinase is not activated by fructose 1,6-diphosphate and gives hyperbolic substrate-saturation curves with phosphoenolpyruvate. It is therefore different from the L-type pyruvate kinase of mammalian liver. Inhibition by MgATP2− was competitive for MgADP− but not for phosphoenolpyruvate, and the enzyme is therefore different from the M-type pyruvate kinase, which is said to be competitively inhibited by MgATP2− with respect to both substrates. The Ki(MgATP2−) value of approx. 8mm for the brain enzyme is higher than the values (about 2mm) reported for the muscle enzyme. Stimulation of enzymic activity was observed at low (1–2mm) concentrations of MgATP2−. Substrate kinetic constants were Km (MgADP−)=0.47mm, Km (phosphoenolpyruvate)=0.08mm. Free Mg2+ at very high concentrations (over 10mm) was inhibitory (Ki=20–32mm). Neither ADP3− nor 5′-AMP2− inhibited the activity. The brain enzyme was concluded to be different from both the M-type and the L-type of other mammalian organs such as muscle and liver.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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