Mechanisms of inhibition of xenobiotic-metabolizing enzymes

References

• Abriola D. P., Fields R., Stein S., MacKerell A. D., Jr., Pietruszko R. Active site of human liver aldehyde dehydrogenase. Biochemistry 1987; 26: 5679–5684
   PubMed Web of Science ®Google Scholar
• Ashour M. B. A., Hammock B. D. Substituted trifluoroketones as potent, selective inhibitors of mammalian carboxylesterases. Biochemical Pharmacology 1987; 36: 1869–1879
   PubMedGoogle Scholar
• Beyeler S., Testa B., Perrissoud D. Flavonoids as inhibitors of rat liver monooxygenase activities. Biochemical Pharmacology 1988; 37: 1971–1979
   PubMed Web of Science ®Google Scholar
• Borchardt R. T. Catechol-O-methyltransferase. 4. In vitro inhibition by 3-hydroxy-4-pyrones, 3-hydroxy-2-pyrones, and 3-hydroxy-4-pyridones. Journal of Medicinal Chemistry 1973; 16: 581–583
   PubMedGoogle Scholar
• Borchardt R. T., Bhatia P. Catechol O, methyltransferase. 12. Affinity labeling of the active site with the oxidation products of 5,6-dihydroxyindole. Journal of Medicinal Chemistry 1982; 25: 263–271
   PubMedGoogle Scholar
• Bornheim L. M., Underwood M. C., Caldera P., Rettie A. E., Trager W. F., Wrighton S. A., Almira Correia M. Inactivation of multiple hepatic cytochrome P-450 isozymes in rats by allylisopropylacetamide: mechanistic implications. Molecular Pharmacology 1987; 32: 299–308
   PubMedGoogle Scholar
• Broom A. D. Rational design of enzyme inhibitors: multisubstrate analogue inhibitors. Journal of Medicinal Chemistry 1989; 32: 2–7
   PubMed Web of Science ®Google Scholar
• Cheng B. Y., Origitano T. C., Collins M. A. Inhibition of catechol O-methyltransferase by 6,7-dihydroxy-3,4-dihydroisoquinolines related to dopamine: demonstration using liquid chromatography and a novel substrate for O-methylation. Journal of Neurochemistry 1987; 48: 779–786
   PubMedGoogle Scholar
• Goodhart P. J., DeWolf W. E., Jr., Kruse L. I. Mechanism-based inactivation of dopamine β-hydroxylase by p-cresol and related alkylphenols. Biochemistry 1987; 26: 2576–2583
   PubMed Web of Science ®Google Scholar
• Gupta S. P. QSAR studies of enzyme inhibitors. Chemical Reviews 1987; 87: 1183–1253
   Google Scholar
• Kellis J. T., Jr., Childers W. E., Robinson C. H., Vickery L. E. Inhibition of aromatase cytochrome P-450 by 10-oxirane and 10-thiirane substituted androgens. Journal of Biological Chemistry 1987; 262: 4421–4426
   PubMed Web of Science ®Google Scholar
• Kruse L. I., Kaiser C., DeWolf W. E., Jr., Frazee J. S., Ross S. T., Wawro J., Wise M., Flaim K. E., Sawyer J. L., Erickson R. W., Ezekiel M., Ohlstein E. H., Berkowitz B. A. Multisubstrate inhibitors of dopamine β-hydroxylase. 2. Structure-activity relationships at the phenylethylamine binding site. Journal of Medicinal Chemistry 1987; 30: 486–494
   PubMed Web of Science ®Google Scholar
• Lunetta J. M., Sugiyama K., Almira Correia M. Secobarbital-mediated inactivation of rat liver cytochrome P-450b: a mechanistic reappraisal. Molecular Pharmacology 1989; 35: 10–17
   PubMed Web of Science ®Google Scholar
• Manno M., De Matteis F., King L. J. The mechanism of the suicidal, reductive inactivation of microsomal cytochrome P-450 by carbon tetrachloride. Biochemical Pharmacology 1988; 37: 1981–1990
   PubMed Web of Science ®Google Scholar
• May S. W., Wimalasena K., Herman H. H., Fowler L. C., Ciccarello M. C., Pollock S. H. Novel antihypertensives targeted at dopamine β-monooxygenase: turnover-dependent cofactor depletion by phenyl aminoethyl selenide. Journal of Medicinol Chemistry 1988; 31: 1066–1068
   PubMed Web of Science ®Google Scholar
• Mfsnil M. M., Testa B., Jenner P. In vitro, inhibition by stiripentol of rat brain cytochrome P-450-mediated naphthalene hydroxylation. Xenobiotica 1988; 18: 1097–1106
   PubMedGoogle Scholar
• Mesnil M. M., Testa B., Jennfr P. Ex vivo, inhibition of rat brain cytochrome P-450 activity by stiripentol. Biochemical Pharmacology 1988; 37: 3619–3622
   PubMedGoogle Scholar
• Murray M. Mechanisms of the inhibition of cytochrome P-450-mediated drug oxidation by therapeutic agents. Drug Metabolism Reviews 1987; 18: 55–81
   PubMed Web of Science ®Google Scholar
• Özer N., Özer I. Differential reactivity of active sites in human plasma cholinesterase toward 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. Archives of Biochemistry and Biophysics 1987; 255: 89–94
   PubMedGoogle Scholar
• Poulos T. L. Cytochrome P-450: molecular architecture, mechanism and prospects for rational inhibitor design. Pharmaceutical Research 1988; 5: 67–75
   PubMed Web of Science ®Google Scholar
• Poulos T. L., Howard A. J. Crystal structure of metyrapone- and phenylimidazole-inhibited complexes of cytochrome P-450cam. Biochemistry 1987; 26: 8165–8174
   PubMed Web of Science ®Google Scholar
• Schloss J. V. Significance of slow-binding enzyme inhibition and its relationship to reaction-intermediate analogues. Accounts in Chemical Research 1988; 21: 348–353
   Web of Science ®Google Scholar
• Testa B., Jenner P. Inhibitors of cytochrome P-450s and their mechanism of action. Drug Metabolism Reviews 1981; 12: 1–117
   PubMed Web of Science ®Google Scholar
• Thakker D. R., Boehlert C., Kirk K. L., Antkowiak R., Creveling C. R. Regioselectivity of catechol O-methyltransferase. The effect of pH on the site of O-methylation of fluorinated norepinephrines. Journal of Biological Chemistry 1986; 261: 178–184
   PubMedGoogle Scholar
• Wahlström A., Persson K., Rane A. Metabolic interaction between morphine and naloxone in human liver. A common pathway of glucuronidation?. Drug Metabolism and Disposition 1989; 17: 218–220
   PubMed Web of Science ®Google Scholar
• Walsh C. Suicide substrates: mechanism-based enzyme inactivators. Tetrahedron 1982; 38: 871–909
   Web of Science ®Google Scholar