Bioactivation of N-substituted N′-(4-imidazole-ethyl)thioureas by human FMO1 and FMO3

References

• Cantrell AS, Engelhardt P, Högberg M, Jaskunas SR, Gunnar Johansson N, Jordan CL, Kangasmetsä J, Kinnick MD, Lind P, Morin JM, Jr, Muesing MA, Noreén R, Öberg B, Pranc P, Sahlberg C, Ternansky RJ, Vasileff RT, Vrang L, West SJ, Zhang H. Phenethylthiazolylthiourea (PETT) compounds as a new class of HIV-1 reverse transcriptase inhibitors. 2. Synthesis and further strucure-activity relationship studies of PETT analogs. Journal of Medical Chemistry 1996; 39: 4261–4274
   PubMed Web of Science ®Google Scholar
• Cashman JR. Human flavin-containing monooxygenase: substrate specificity and role in drug metabolism. Current Drug Metabolism 2000; 1: 181–191
   PubMed Web of Science ®Google Scholar
• Cashman JR, Hanzlik RP. Oxidation and other reactions of thiobenzamide derivatives of relevance to their hepatotoxicity. Journal of Organic Chemistry 1982; 47: 4645–4650
   Web of Science ®Google Scholar
• Cherrington NJ, Cao Y, Cherrington JW, Rose RL, Hodgson E. Physiological factors affecting protein expression of flavin-containing monooxygenases 1, 3 and 5. Xenobiotica 1998; 28: 673–682
   PubMed Web of Science ®Google Scholar
• D’Cruz OJ, Dong Y, Uckun FM. Potent dual anti-HIV and spermicidal activities of novel oxovanadium(V) complexes with thiourea non-nucleoside inhibitors of HIV-1 reverse transcriptase. Biochemical and Biophysical Research Communications 2003; 302: 253–264
   PubMed Web of Science ®Google Scholar
• D’Cruz OJ, Venkatachalam TK, Mao C, Qazi S, Uckun FM. Structural requirements for potent anti-human immunodificiency virus (HIV) and sperm-immobilizing activities of cyclohexenyl thiourea and urea non-nucleoside inhibitors of HIV-1 reverse transcriptase. Biology and Reproduction 2002; 67: 1959–1974
   PubMed Web of Science ®Google Scholar
• Doerge DR, Corbett MD. Primary amine oxidation by a flavinhydroperoxide. A study of the basis for the substrate specificity of the flavoprotein monooxygenase. Biochemistry and Pharmacology 1984; 33: 3615–3619
   PubMedGoogle Scholar
• Forrest JAH, Shearman DJC, Spence R, Celestin LR. Neutropenia associated with metiamide. Lancet 1975; 0: 392–393
   Google Scholar
• Guo W-XA, Poulsen LL, Ziegler DM. Use of thiocarbamides as selective substrate probes for isoforms of flavin-containing monooxygenases. Biochemistry and Pharmacology 1992; 44: 2029–2037
   PubMed Web of Science ®Google Scholar
• Guo W-XA, Ziegler DM. Estimation of flavin-containing monooxygenase activities in crude tissue preparations by thiourea dependent oxidation of thiocholine. Annals of Biochemistry 1991; 198: 143–148
   Google Scholar
• Henderson MC, Krueger SK, Stevens JF, Williams DE. Human flavin-containing monooxygenase form 2 S-oxygenation: sulfenic acid formation from thioureas and oxidation of glutathione. Chemical Research in Toxicology 2004; 17: 633–640
   PubMed Web of Science ®Google Scholar
• Hernandez D, Janmohamed A, Chandan P, Phillips IR, Shephard EA. Organization and evolution of the flavin-containing monooxygenase genes of human and mouse: identification of novel gene and pseudogene clusters. Pharmacogenetics 2004; 14: 117–130
   PubMedGoogle Scholar
• Högberg M, Morrison I. HIV-1 non-nucleoside reverse transcriptase inhibitors. Experimental Opinions Therapy Patents 2000; 10: 1189–1199
   Web of Science ®Google Scholar
• Kim YM, Ziegler DM. Size limits of thiocarbamides accepted as substrates by human flavin-containing monooxygenase. Drug Metabolism and Disposition 2000; 28: 1003–1006
   PubMed Web of Science ®Google Scholar
• Lang DH, Yeung CK, Peter RM, Ibarra C, Gasser R, Itagaki K, Philpot RM, Rettie AE. Isoform specificity of trimethylamine N-oxygenation by human flavin-containing monooxygenase (FMO) and P450 enzymes: selective catalysis by FMO3. Biochemistry and Pharmacology 1998; 56: 1005–1012
   PubMed Web of Science ®Google Scholar
• Nagata T, Williams DE, Ziegler DM. Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: differences due to substrate size. Chemical Research in Toxicology 1990; 3: 372–376
   PubMed Web of Science ®Google Scholar
• Onderwater RCA, Commandeur JNM, Groot EJ, Sitters A, Menge WMPB, Vermeulen NPE. Cytotoxicity of a series of mono- and di-substituted thiourea in freshly isolated rat hepatocytes: a preliminary structure-toxicity relationship study. Toxicology 1998; 125: 117–129
   PubMedGoogle Scholar
• Onderwater RCA, Commandeur JNM, Menge WMPB, Vermeulen NPE. Activation of microsomal glutathione S-transferase and inhibition of cytochrome P450 1A1 activity as a model system to detect protein alkylation by thiourea-containing compounds in rat liver microsomes. Chemical Research in Toxicology 1999; 12: 396–402
   PubMed Web of Science ®Google Scholar
• Onderwater RCA, Commandeur JNM, Vermeulen NPE. Comparative cytotoxicity of N-substituted N′-(4-imidazole-ethyl)thiourea towards precision-cut rat liver slices. Toxicology 2004; 197: 81–91
   PubMedGoogle Scholar
• Poulsen LL, Hyslop RM, Ziegler DM. S-Oxygenation of N-substituted thioureas catalyzed by the pig liver microsomal FAD-containing monooxygenase. Archives in Biochemisty and Biophysics 1979; 198: 78–88
   PubMed Web of Science ®Google Scholar
• Poulsen LL, Ziegler DM. Multisubstrate flavin-containing monooxygenases: applications of mechanism to specificity. Chemico-Biology Interactions 1995; 96: 57–73
   PubMed Web of Science ®Google Scholar
• Shehin-Johnson SE, Williams DE, Larsen-Su S, Stresser DM, Hines RN. Tissue-specific expression of flavin-containing monooxygenase (FMO) forms 1 and 2 in the rabbit. Journal of Pharmology and Experimental Therapy 1995; 272: 1293–1299
   PubMed Web of Science ®Google Scholar
• Smith PB, Crespi C. Thiourea toxicity in mouse C3H/10T1/2 cells expressing human flavin dependent monooxygenase 3. Biochemistry and Pharmacology 2002; 63: 1941–1948
   PubMed Web of Science ®Google Scholar
• Vollinga RC, Menge WMPB, Leurs R, Timmerman H. New analogs of burimamide as potent and selective histamine H3 receptor antagonists: the effect of chain length variation of the alkyl spacer and modifications of the N-thiourea substituent. Journal of Medical Chemistry 1995; 38: 2244–2250
   PubMedGoogle Scholar
• Ziegler DM. An overview of the mechanism, substrate specificities, and structure of FMOs. Drug Metabolism Reviews 2002; 34: 503–511
   PubMed Web of Science ®Google Scholar