A kinetic study of rabbit muscle pyruvate kinase.
The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg(2+) 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, Mg(2+), pyruvate and MgATP, and that dead-end complexes, between pyruvate, ADP and Mg(2+), 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.
D000244:Adenosine Diphosphate; D000818:Animals; D001665:Binding Sites; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003201:Computers; D007700:Kinetics; D008274:Magnesium; D008433:Mathematics; D008954:Models, Biological; D009132:Muscles / Q000201:enzymology*; D010728:Phosphoenolpyruvate; D011485:Protein Binding; D011770:Pyruvate Kinase / Q000378:metabolism*; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet
D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D011770:Pyruvate Kinase; D008274:Magnesium