Biotransformation Reactions

The Practice of Medicinal Chemistry: Second Edition

Volumn , Issue , 2003, Pages 517-543

  Magdalou, Jacques ^a   Fournel Gigleux, Sylvie ^a   Ouzzine, Mohamed ^a   Testa, Bernard ^b  

^a UNIVERSITÉ DE LORRAINE   (France)

^b UNIVERSITY OF LAUSANNE   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; BIOCHEMISTRY; BIOCHIPS; ENZYME ACTIVITY; FORECASTING; LEAD COMPOUNDS; METABOLITES;

BIOTRANSFORMATION REACTIONS; CHEMICAL PATHWAYS; CHEMICAL PROCESS; COMBINATORIAL CHEMISTRY; DRUG DISCOVERY PROCESS; DRUG METABOLISMS; DRUG-METABOLIZING ENZYMES; REACTION MECHANISM;

BIOCONVERSION;

EID: 27444435166     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012744481-9/50035-0     Document Type: Chapter

References (22)

1. Silverman R.B. The Organic Chemistry of Drug Design and Drug Action 1992, Academic Press, New York.
2. Testa B., Jenner P. Drug Metabolism. Chemical and Biochemical Aspects 1976, Marcel Dekker, San Diego.
3. Stenlake J.B. Foundations of Molecular Pharmacology, The Chemical Basis of Drug Action 1979, 2. The Athlone Press-University of London, New York.
4. Yamada T., Morisseau C., Maxwell J.E., Argiriadi M.A., Christianson D.W., Hammock B.D. Biochemical evidence for the involvement of tyrosine in epoxide activation during the catalytic cycle of epoxide hydrolase. J. Biol. Chem. 2000, 275:23082-23088.
5. Nebert D.W. Drug-metabolizing enzymes in ligand-modulated transcription. Biochem. Pharmacol. 1994, 47:25-37.
6. Jaggi R., Addison R.S., Suther B.D., Dickinson R.G. Conjugation of desmethylnaproxen in the rat, a novel acylglucuronide-sulfate diconjugate as a major biliary metabolite. Drug Metab. Dispos. 2002, 30:161-166.
7. Lau E.Y., Bruice T.C. Comparison of the dynamics for ground-state and transition-state structures of the active site of catechol-O-methyltransferase. J. Am. Chem. Soc. 2000, 122:7165-7171.
8. Männisto P.T., Kaakkola S. Catechol-O-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors. Pharmacol. Rev. 1999, 51:593-628.
9. Rodrigues-Lima F., Deloménie C., Goodfellow G.H., Grant D.M., Dupret J.M. Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: evidence for the conservation of a cysteine protease catalytic domain and an active loop. Biochem. J. 2001, 356:327-334.
10. Vessey D.A., Kelley M. Characterization of the reaction mechanism for the XL-I form of bovine liver xenobiotic/medium chain fatty acid:CoA ligase. Biochem. J. 2001, 357:283-288.
11. Ouzzine M., Magdalou J., Burchell B., Fournel-Gigleux S. An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyltransferase 1A6 to the endoplasmic reticulum. J. Biol. Chem. 1999, 274:31401-31409.
12. Ritter J.K. Roles of glucuronidation and UDP-glucuronosyltransferases in xenobiotic bioactivation reactions. Chem. Biol. Interactions 2000, 129:171-193.
13. Georges H., Jarecki I., Netter P., Magdalou J., Lapicque F. Glycation of human serum albumin by acylglucuronides of nonsteroidal anti-inflammatory drugs of the series of phenylpropionates. Life Sci. 1999, 65:151-156.
14. Ouzzine M., Antonio L., Burchell B., Netter P., Fournel-Gigleux S., Magdalou J. Importance of histidine residues for the function of the human liver UDP-glucuronosyltransferase UGT1A6: evidence for the catalytic role of histidine 370. Mol. Pharm. 2001, 58:1609-1615.
15. Said M., Battaglia E., Elass A., Cano V., Ziegler J.C., et al. Mechanism of inhibition of rat liver bilirubin UDP-glucuronosyltransferase by triphenylalkyl derivatives. J. Biochem. Mol. Toxicol. 1998, 12:19-27.
16. Battaglia E., Elass A., Drake R.R., Paul P., Treat S., et al. Characterization of a new class of inhibitors of the recombinant human liver UDP-glucuronosyltransferase, UGT1A6. Biochim. Biophys. Acta 1995, 1243:9-14.
17. Coughtrie M.W., Sharp S., Maxwell K., Innes N.P. Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem. Biol. Interactions 1998, 109:3-27.
18. Glatt H. Sulfotransferases in the bioactivation of xenobiotics. Chem. Biol. Interactions 2000, 129:141-170.
19. Negishi M., Pedersen L.G., Petrotchenko E., Shevtsov S., Gorokhov A., Kakuta Y., Pedersen L.C. Structure and function of sulfotransferases. Arch. Biochem. Biophys. 2001, 390:149-157.
20. Duffel M.W., Marshal A.D., McPhie P., Sharma V., Jakoby W.B. Enzymatic aspects of the phenol (aryl) sulfotransferases. Drug Metabab. Rev. 2001, 33:369-395.
21. Dajani R., Cleasby A., Neu M., Wonacott A.J., Jhoti H., et al. X-ray crystal structure of human dopamine sulfotransferase. SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity. J. Biol. Chem. 1999, 274:37862-37868.
22. Armstrong R.N. Mechanistic imperatives for the evolution of glutathione transferase. Curr. Opin. Chem. Biol. 1998, 2:618-623.