| Autor: |
Palmer, T. Norman, Odedra, Bhanu R. |
| Zdroj: |
Bioscience Reports; October 1982, Vol. 2 Issue: 10 p825-833, 9p |
| Abstrakt: |
The allosteric inhibition of Ml-type pyruvate kinase from rabbit skeletal muscle by phenylalanine is reciprocally dependent on Mg2+ and phosphoenolpyruvate concentrations. At pH 8, phenylalanine acts as a competitive inhibitor with respect to Mg2+ and phosphoenolpyruvate, and vice versa. Phenylalanine introduces sigmoidicity into the dependence of the reaction velocity on [Mg2+]. In vitro kinetic analysis indicates that phenylalanine inhibition of muscle pyruvate kinase is unlikely to have regulatory significance in vivo. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
Full text from SpringerLink