Regulatory mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. II. Theory.
In this study, rate equations that predict the regulatory kinetic behavior of homocitrate synthase were derived, and simulation of the predicted behavior was carried out over a range of values for the kinetic parameters. The data obtained allow application of the resulting expressions to enzyme systems that exhibit activation and inhibition as a result of the interaction of effectors at multiple sites in the free enzyme. Homocitrate synthase was used as an example in terms of its activation by Na+ binding to the active enzyme conformer at an allosteric site, inhibition by binding to the active site, and inhibition by lysine binding to the less active enzyme conformer.
Andi
Babak
B
Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, USA.
Cook
Paul F
PF
D000494:Allosteric Regulation / Q000502:physiology; D007700:Kinetics; D008239:Lysine / Q000378:metabolism; D008954:Models, Biological; D008956:Models, Chemical; D007652:Oxo-Acid-Lyases / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012964:Sodium / Q000378:metabolism
D012964:Sodium; C021365:homocitrate synthase; D007652:Oxo-Acid-Lyases; D008239:Lysine