L-Phenylalanine inhibition of muscle pyruvate kinase |
| |
Authors: | T. Norman Palmer Bhanu R. Odedra |
| |
Affiliation: | (1) Department of Biochemistry, Charing Cross Hospital Medical School, Fulham Palace Road, W6 8RF London, U.K.;(2) Present address: Clinical Nutrition and Metabolism Unit, London School of Hygiene and Tropical Medicine, Hospital for Tropical Diseases, St. Pancras Way, NW1 2PE London, U.K. |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|