Stereospecific oxidation of the (S)-enantiomer of RS-8359, a selective and reversible monoamine oxidase A (MAO-A) inhibitor, by aldehyde oxidase

References

• Beedham C. 1985. Molybdenum hydroxylase as drug-metabolizing enzymes. Drug Metabolism Reviews 16:119–156.
   PubMed Web of Science ®Google Scholar
• Beedham C. 1987. Molybdenum hydroxylases: Biological distribution and substrate-inhibitor specificity. Progress in Medical Chemistry 24:85–121.
   PubMedGoogle Scholar
• Beedham C. 1997. The role of non-P450 enzymes in drug oxidation. Pharmacy World Science 19:255–263.
   PubMed Web of Science ®Google Scholar
• Beedham C. 2002. Molybdenum hydroxylases. In: Ioannides C, editor. Enzyme systems that metabolise drugs and other xenobiotics. London: Wiley. pp 147–187.
   Google Scholar
• Beedham C, Al-Tayib Y, Smith JA. 1992. The role of guinea pig and rabbit hepatic aldehyde oxidase in the oxidative in vitro metabolism of cinchona alkaloids. Drug Metabolism and Disposition 20:889–895.
   PubMed Web of Science ®Google Scholar
• Caldwell J, Winter SM. 1988. The pharmacological and toxicological significance of the stereochemistry of drug disposition. Xenobiotica 18:59–70.
   PubMed Web of Science ®Google Scholar
• Drayer DE. 1986. Pharmacodynamic and pharmacokinetic differences between drug enantiomers in human: An overview. Clinical Pharmacology and Therapeutics 40:125–133.
   PubMed Web of Science ®Google Scholar
• Gutzwiller J, Uskokovic MR. 1973. Reinvestigation of the classical synthesis of cinchona alkaloids. II. The synthesis of quinine and its naturally occurring diastereomers from quinotoxine. Helvetica Chimica Acta 56:1494–1503.
   Web of Science ®Google Scholar
• Holmes RS. 1979. Genetics, ontogeny and testosterone inducibility of aldehyde oxidase isozymes in the mouse: Evidence of two genetic loci (Aox-1 and Aox-2) closely linked on Chromosome 1. Biochemical Genetics 17:517–527.
   PubMed Web of Science ®Google Scholar
• Iwata N, Tonohiro T, Kozuka M, Kumagae Y, Takasaki W, Tanaka Y. 1996, A novel selective and reversible MAO-A inhibitor, RS-8359: Its pharmacological properties and metabolism. International Academy for Biomedical Drug and Research 11:285–286.
   Google Scholar
• Iwata N, Yokoyama T. 1987. RS-2232 and 8359, a new reversible and specific inhibitors of A form of MAO. Pharmacology and Toxicology 60\(Suppl. 1):25P.
   Google Scholar
• Jamali F, Mehvar R, Pasutto FM. 1989. Enantioselective aspects of drug action and disposition: Therapeutic pitfalls. Journal of Pharmaceutical Sciences 78:695–715.
   PubMed Web of Science ®Google Scholar
• Kaye B, Rance DJ, Waring L. 1985. Oxidative metabolism of carbazeran in vitro by liver cytosol of baboon and man. Xenobiotica 15:237–242.
   PubMed Web of Science ®Google Scholar
• Ohkubo K, Sakiyama S, Fujimura S. 1983. Purification and characterization of N'-methylnicotinamide oxidase I and II separated from rat liver. Archives of Biochemistry and Biophysics 221:534–542.
   PubMed Web of Science ®Google Scholar
• Plenker A, Puchler K, Volz HP. 1997. The effects of RS-8359 on cardiovascular function in healthy subjects and depressed patients. International Clinical Psychopharmacology 12:S25–S29.
   Web of Science ®Google Scholar
• Puchler K, Sasahara K, Plenker A, Nitanai T, Witte PU. 1997. The pharmacokinetic profile of RS-8359. International Clinical Psychopharmacology 12:S11–S16.
   Web of Science ®Google Scholar
• Rajagopalan Ky. 1980. Xanthine oxidase and aldehyde oxidase. In: Jacoby WB, editor. Enzymatic basis of detoxification. London: Academic Press. pp. 295–309.
   Google Scholar
• Rashidi MR, Smith JA, Clarke SE, Beedham C. 1997. In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit and rat liver. Drug Metabolism and Disposition 25:806–813.
   Web of Science ®Google Scholar
• Stell JGP, Warne AJ, Lee-Woolley C. 1989. Purification of rabbit liver aldehyde oxidase by affinity chromatography on benzamidine sepharose 6B. Journal of Chromatography 475:363–372.
   PubMed Web of Science ®Google Scholar
• Takasaki W, Yamamura M, Nozaki A, Nitanai T, Sasahara K, Itoh K, Tanaka Y. 2005. Stereoselective pharmacokinetics of RS-8359, a selective and reversible MAO-A inhibitor, by species-dependent metabolizing enzymes. Chirality 17:135–141.
   PubMed Web of Science ®Google Scholar
• Takasaki W, Yamamura M, Shigehara E, Suzuki Y, Tonohiro T, Hara T, Tanaka Y. 1999. Stereoselective pharmacokinetics of RS-8359, a selective and reversible inhibitor of A-type monoamine oxidase, in rats, mice, dogs, and monkeys. Biological and Pharmaceutical Bulletin 22:498–503.
   PubMed Web of Science ®Google Scholar
• Testa B, Mayer JM. 1988. Stereoselective drug metabolism and its significance in drug research. Progress in Drug Research 32:249–303.
   PubMedGoogle Scholar
• Tucker GT, Lennard MS. 1990. Enantiomer specific pharmacokinetics. Pharmacology and Therapeutics 45:309–329.
   PubMed Web of Science ®Google Scholar
• Wright RM, Clayton DK, Riley MG, McManaman JI,, Repine JE. 1999. cDNA cloning, sequencing and characterization of male and female rat liver aldehyde oxidase (rA0X1)-differences in redox status may distinguish male and female forms of hepatic AOX. Journal of Biological Chemistry 274:3878–3886.
   PubMed Web of Science ®Google Scholar
• Yokoyama T, Karube T, Iwata N. 1989. Comparative studies of the effects of RS-8359 and safrazine on monoamine oxidase in vitro and in vivo in mouse brain. Journal of Pharmacy and Pharmacology 41:32–36.
   PubMed Web of Science ®Google Scholar
• Yoshihara S, Tatsumi K. 1986. Kinetic and inhibition studies on reduction of diphenylsulphoxide by guinea pig liver aldehyde oxidase. Archives of Biochemistry and Biophysics 249:8–14.
   PubMed Web of Science ®Google Scholar