The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg2+ catalysed by rabbit muscle pyruvate kinase. The experimental results indicate that the reaction mechanism is equilibrium random-order in type, that the substrates and products are phosphoenolpyruvate, ADP, Mg2+, pyruvate and MgATP, and that dead-end complexes, between pyruvate, ADP and Mg2+, form randomly and exist in equilibrium with themselves and other substrate complexes. Values were determined for the Michaelis, dissociation and inhibition constants of the reaction and are compared with values ascertained by previous workers.
Research Article| February 01 1973
A kinetic study of rabbit muscle pyruvate kinase
Biochem J (1973) 131 (2): 223–236.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
S. Ainsworth, N. Macfarlane; A kinetic study of rabbit muscle pyruvate kinase. Biochem J 1 February 1973; 131 (2): 223–236. doi: https://doi.org/10.1042/bj1310223
Download citation file: