The Behavior and Significance of Slow‐Binding Enzyme Inhibitors
Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjectsPublished 1 January 1988
John F. Morrison, Christopher T. Walsh
Citations838
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Abstract
Introduction Characteristics of Progress Curves for Slow-Binding Inhibitors Specific Cases of Slow-Binding Inhibition Concluding REmarks
Keywords
Computer ScienceBiochemistry, Genetics and Molecular Biology
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53 Citations1980JoAnne Stubbe, Robert H. Abeles
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46 Citations1985Vern L. Schramm, David C. Baker
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25 Citations1985Raymond L. Blakley, Lennie Cocco
Stopped-flow measurements of protein fluorescence quenching when methotrexate (MTX) binds to dihydrofolate reductase (isoenzyme II) of Streptococcus faecium (SFDHFR II) analyze as the sum of two differentials: a rapid binding phase and a second phase for which the observed rate constant is independent of metotrexate concentration.
Biochemistry3-Fluoro-3-deoxycitrate: a probe for mechanistic study of citrate-utilizing enzymes
23 Citations1982Steven E. Rokita, Paul A. Srere +1 more
The interaction of a novel fluorinated analogue of citrate, 3-fluoro-3-deoxycitrate (3-fluorocitrate), with the four known citrate-processing enzymes is described in this report.
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular EnzymologyKinetic study on the slow inhibition of epidermis tyrosinase by m-coumaric acid
23 Citations1984Juana Cabanes, Francisco Garcı́a-Carmona +3 more
Kinetic data correspond to that for a postulated mechanism that involves rapid formation of a reduced enzyme-m-coumaric acid complex that subsequently undergoes a relatively slow reversible reaction.
Biochemical PharmacologyKinetics of inhibition of angiotensin converting enzyme by captopril and by enalapril diacid
16 Citations1984Charles H. Reynolds
Inhibition of angiotensin converting enzyme by captopril and by the active diacid derivative of enalapril was reinvestigated, finding that the release of these inhibitors from the enzyme may be slow enough to affect the duration of their hypotensive action.
Journal of Biological ChemistryKinetics of the interaction of N-(phosphonacetyl)-L-aspartate with the catalytic subunit of aspartate transcarbamoylase. A slow conformational change subsequent to binding.
14 Citations1986Robert E. Cohen, H. K. Schachman
The conformational change subsequent to PALA binding leads to a 10-fold increase in the equilibrium constant for complex formation, understood in terms of the two-step binding scheme where rapid dissociation of the initial ligand X enzyme complex is measured by the NMR technique and the slow isomerization of the complex is responsible for the bulk of the stopped flow signal.
Molecular biology, biochemistry, and biophysicsSuicide Substrates: Mechanism-Based Inactivators of Specific Target Enzymes
5 Citations1980Christopher T. Walsh
This paper presents mechanistic studies on how citrate was cleaved to acetyl CoA and oxalacetate by the cytoplasmic citrate cleavage enzyme (ATP citrate lyase), discovered by Lipmann and Srere some years earlier in 1953.
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