[33] Isotope exchange studies of regulatory enzymes: “Fingerprint” kinetic patterns for modifier action
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Elsevier
Reference56 articles.
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1. Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-I. Equilibrium isotope exchange kinetics.;Journal of Biological Chemistry;1993-03
2. Regulatory Behavior of Escherichia coli Aspartate Transcarbamylase Altered by Site-specific Mutation of Tyr240 → Phe in the Catalytic Chain;Journal of Biological Chemistry;1989-10
3. Site-specific Mutation of Tyr240 → Phe in the Catalytic Chain of Escherichia coli Aspartate Transcarbamylase;Journal of Biological Chemistry;1989-10
4. Kinetic consequences of site-specific mutation of Glu-239 → Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzyme;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1989-03
5. Effectors of Escherichia coli aspartate transcarbamoylase differentially perturb aspartate binding rather than the T-R transition.;Journal of Biological Chemistry;1988-03
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