title: Regulatory mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. II. Theory.
abstract: 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.
authors.affiliation: Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, USA.
authors.forename: Babak
authors.initials: B
authors.lastname: Andi
authors.forename: Paul F
authors.initials: PF
authors.lastname: Cook
mesh_terms: 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
chemical_list: D012964:Sodium; C021365:homocitrate synthase; D007652:Oxo-Acid-Lyases; D008239:Lysine