Monkey liver cytochrome P450 2C9 is involved in caffeine 7-N-demethylation to form theophylline

References

• Berthou F, Flinois JP, Ratanasavanh D, et al. (1991). Evidence for the involvement of several cytochromes P-450 in the first steps of caffeine metabolism by human liver microsomes. Drug Metab Dispos 19:561–7
   PubMed Web of Science ®Google Scholar
• Berthou F, Guillois B, Riche C, et al. (1992). Interspecies variations in caffeine metabolism related to cytochrome P4501A enzymes. Xenobiotica 22:671–80
   PubMed Web of Science ®Google Scholar
• Bonati M, Latini R, Galletti F, et al. (1982). Caffeine disposition after oral doses. Clin Pharmacol Ther 32:98–106
   PubMed Web of Science ®Google Scholar
• Bonati M, Latini R, Tognoni G, et al. (1984). Interspecies comparison of in vivo caffeine pharmacokinetics in man, monkey, rabbit, rat, and mouse. Drug Metab Rev 15:1355–83
   PubMed Web of Science ®Google Scholar
• Butler MA, Iwasaki M, Guengerich FP, Kadlubar FF. (1989). Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines. Proc Natl Acad Sci USA 86:7696–700
   PubMed Web of Science ®Google Scholar
• Campbell ME, Spielberg SP, Kalow W. (1987). A urinary metabolite ratio that reflects systemic caffeine clearance. Clin Pharmac Ther 42:157–65
   PubMed Web of Science ®Google Scholar
• Grant DM, Campbell ME, Tang BK, Kalow W. (1987). Biotransformation of caffeine by microsomes from human liver. Kinetics and inhibition studies. Biochem Pharmacol 36:1251–60
   PubMed Web of Science ®Google Scholar
• Grant DM, Tang BK, Kalow W. (1983). Variability in caffeine metabolism. Clin Pharmacol Ther 33:591–602
   PubMed Web of Science ®Google Scholar
• Gu L, Gonzalez FJ, Kalow W, Tang BK. (1992). Biotransformation of caffeine, paraxanthine, theobromine and theophylline by cDNA-expressed human CYP1A2 and CYP2E1. Pharmacogenetics 2:73–7
   PubMedGoogle Scholar
• Hosoi Y, Uno Y, Murayama N, et al. (2012). Monkey liver cytochrome P450 2C19 is involved in R- and S-warfarin 7-hydroxylation. Biochem Pharmacol 84:1691–5
   PubMed Web of Science ®Google Scholar
• Iwasaki K, Murayama N, Koizumi R, et al. (2010). Comparison of cytochrome P450 3A enzymes in cynomolgus monkeys and humans. Drug Metab Pharmacokinetics 25:388–91
   PubMed Web of Science ®Google Scholar
• Iwasaki K, Uno Y. (2009). Cynomolgus monkey CYPs: a comparison with human CYPs. Xenobiotica 39:578–81
   PubMed Web of Science ®Google Scholar
• Kimura M, Shimizu M, Kiyotani K, et al. (2012). Cytochrome P450 2A6 phenotyping based on dietary caffeine intake in a Japanese population of non-smokers. Drug Metab Lett 6:67–72
   PubMedGoogle Scholar
• Kimura M, Yamazaki H, Fujieda M, et al. (2005). CYP2A6 is a principal enzyme involved in hydroxylation of 1,7-dimethylxanthine, a main caffeine metabolite, in humans. Drug Metab Dispos 33:1361–6
   PubMed Web of Science ®Google Scholar
• Kot M, Daniel WA. (2008). The relative contribution of human cytochrome P450 isoforms to the four caffeine oxidation pathways: an in vitro comparative study with cDNA-expressed P450s including CYP2C isoforms. Biochem Pharmacol 76:543–51
   PubMed Web of Science ®Google Scholar
• Kuribayashi S, Uno Y, Naito S, Yamazaki H. (2012). Different metabolites of human hepatotoxic pyrazolopyrimidine derivative 5-n-butyl-pyrazolo[1,5-a]pyrimidine produced by human, rat, and monkey cytochrome P450 1A2 and liver microsomes. Basic Clin Pharmacol Toxicol 110:405–8
   PubMed Web of Science ®Google Scholar
• Nelson DR, Zeldin DC, Hoffman SMG, et al. (2004). Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 14:1–18
   PubMedGoogle Scholar
• Rendic S, Guengerich FP. (2012). Contributions of human enzymes in carcinogen metabolism. Chem Res Toxicol 25:1316–83
   PubMed Web of Science ®Google Scholar
• Saruwatari J, Nakagawa K, Shindo J, et al. (2002). A population phenotyping study of three drug-metabolizing enzymes in Kyushu, Japan, with use of the caffeine test. Clin Pharmacol Ther 72:200–8
   PubMed Web of Science ®Google Scholar
• Tjia JF, Colbert J, Back DJ. (1996). Theophylline metabolism in human liver microsomes: inhibition studies. J Pharmacol Exp Ther 276:912–17
   PubMed Web of Science ®Google Scholar
• Uehara S, Murayama N, Nakanishi Y, et al. (2011). Immunochemical detection of cytochrome P450 enzymes in liver microsomes of 27 cynomolgus monkeys. J Pharmacol Exp Ther 339:654–61
   PubMed Web of Science ®Google Scholar
• Uehara S, Murayama N, Yamazaki H, Uno Y. (2010). A novel CYP2A26 identified in cynomolgus monkey liver metabolizes coumarin. Xenobiotica 40:621–9
   PubMed Web of Science ®Google Scholar
• Uno Y, Fujino H, Kito G, et al. (2006). CYP2C76, a novel cytochrome P450 in cynomolgus monkey, is a major CYP2C in liver, metabolizing tolbutamide and testosterone. Molec Pharmacol 70:477–86
   PubMed Web of Science ®Google Scholar
• Uno Y, Hosaka S, Matsuno K, et al. (2007a). Characterization of cynomolgus monkey cytochrome P450 (CYP) cDNAs: is CYP2C76 the only monkey-specific CYP gene responsible for species differences in drug metabolism? Arch Biochem Biophys 466:98–105
   PubMed Web of Science ®Google Scholar
• Uno Y, Iwasaki K, Yamazaki H, Nelson DR. (2011a). Macaque cytochromes P450: nomenclature, transcript, gene, genomic structure, and function. Drug Metab Rev 43:346–61
   PubMed Web of Science ®Google Scholar
• Uno Y, Kumano T, Kito G, et al. (2007b). CYP2C76-mediated species difference in drug metabolism: a comparison of pitavastatin metabolism between monkeys and humans. Xenobiotica 37:30–43
   PubMed Web of Science ®Google Scholar
• Uno Y, Matsuno K, Murayama N, et al. (2011b). Metabolism of P450 probe substrates by cynomolgus monkey CYP2C76. Basic Clin Pharmacol Toxicol 109:315–18
   PubMed Web of Science ®Google Scholar
• Uno Y, Matsushita A, Osada N, et al. (2010a). Genetic variants of CYP3A4 and CYP3A5 in cynomolgus and rhesus macaques. Drug Metab Dispos 38:209–14
   PubMed Web of Science ®Google Scholar
• Uno Y, Uehara S, Kohara S, et al. (2011c). Newly identified CYP2C93 is a functional enzyme in rhesus monkey, but not in cynomolgus monkey. PLoS One 6:e16923
   Web of Science ®Google Scholar
• Uno Y, Uehara S, Kohara S, et al. (2010b). Cynomolgus monkey CYP2D44 newly identified in liver, metabolizes bufuralol, and dextromethorphan. Drug Metab Dispos 38:1486–92
   PubMed Web of Science ®Google Scholar
• Uno Y, Uehara S, Murayama N, Yamazaki H. (2011d). CYP1D1, pseudogenized in human, is expressed and encodes a functional drug-metabolizing enzyme in cynomolgus monkey. Biochem Pharmacol 81:442–50
   PubMed Web of Science ®Google Scholar
• Wester MR, Yano JK, Schoch GA, et al. (2004). The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0-Å resolution. J Biol Chem 279:35630–7
   PubMed Web of Science ®Google Scholar
• Yamazaki H, Nakamura M, Komatsu T, et al. (2002). Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli. Protein Expr Purif 24:329–37
   PubMed Web of Science ®Google Scholar
• Yamazaki H, Shaw PM, Guengerich FP, Shimada T. (1998). Roles of cytochrome P450 1A2 and 3A4 in the oxidation of estradiol and estrone in human liver microsomes. Chem Res Toxicol 11:659–65
   PubMed Web of Science ®Google Scholar