메뉴 건너뛰기




Volumn 37, Issue 9, 2009, Pages 1948-1955

Influence of N-terminal domain histidine and proline residues on the substrate selectivities of human UDP-glucuronosyltransferase 1A1, 1A6, 1A9, 2B7, and 2B10

Author keywords

[No Author keywords available]

Indexed keywords

1 NITROPYRENE; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A1; GLUCURONOSYLTRANSFERASE 1A6; GLUCURONOSYLTRANSFERASE 1A9; GLUCURONOSYLTRANSFERASE 2B10; GLUCURONOSYLTRANSFERASE 2B7; HISTIDINE; HYMECROMONE; LAMOTRIGINE; MUTANT PROTEIN; NAPROXEN; PROLINE; TRIFLUOPERAZINE; UNCLASSIFIED DRUG;

EID: 70349089346     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.109.028225     Document Type: Article
Times cited : (47)

References (36)
  • 1
    • 33846967445 scopus 로고    scopus 로고
    • Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7: Identification of a critical aromatic amino acid residue at position 33
    • DOI 10.1111/j.1742-4658.2007.05670.x
    • Barre L, Fournel-Gigleux S, Finel M, Netter P, Magdalou J, and Ouzzine M (2007) Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7: identification of critical aromatic amino acid residue at position 33. FEBS J 274:1256-1264. (Pubitemid 46246600)
    • (2007) FEBS Journal , vol.274 , Issue.5 , pp. 1256-1264
    • Barre, L.1    Fournel-Gigleux, S.2    Finel, M.3    Netter, P.4    Magdalou, J.5    Ouzzine, M.6
  • 2
    • 26444551640 scopus 로고    scopus 로고
    • S-naproxen and desmethylnaproxen glucuronidation by human liver microsomes and recombinant human UDP-glucuronosyltransferases (UGT): Role of UGT2B7 in the elimination of naproxen
    • DOI 10.1111/j.1365-2125.2005.02446.x
    • Bowalgaha K, Elliot DJ, Mackenzie PI, Knights KM, Swedmark S, and Miners JO (2005) S-Naproxen and desmethylnaproxen glucuronidation by human liver microsomes and recombinant human UDP-glucuronosyltransferases (UGT): role of UGT2B7 in the elimination of naproxen. Br J Clin Pharmacol 60:423-433. (Pubitemid 41428474)
    • (2005) British Journal of Clinical Pharmacology , vol.60 , Issue.4 , pp. 423-433
    • Bowalgaha, K.1    Elliot, D.J.2    Mackenzie, P.I.3    Knights, K.M.4    Swedmark, S.5    Miners, J.O.6
  • 3
    • 35148893148 scopus 로고    scopus 로고
    • Glucuronidation of nicotine and cotinine by UGT2B10: Loss of function by the UGT2B10 codon 67 (Asp>Tyr) polymorphism
    • DOI 10.1158/0008-5472.CAN-07-2245
    • Chen G, Blevins-Primeau AS, Dellinger RW, Muscat JE, and Lazarus P (2007) Glucuronidation of nicotine and cotinine by UGT2B10: loss of function by the UGT2B10 codon 67 (Asp>Tyr) polymorphism. Cancer Res 67:9024-9029. (Pubitemid 47535885)
    • (2007) Cancer Research , vol.67 , Issue.19 , pp. 9024-9029
    • Chen, G.1    Blevins-Primeau, A.S.2    Dellinger, R.W.3    Muscat, J.E.4    Lazarus, P.5
  • 5
    • 0033612288 scopus 로고    scopus 로고
    • Alteration of human UDP-Glucuronosyltransferase UGT2B17 regio-specificity by a single amino acid substitution
    • DOI 10.1006/jmbi.1999.2735
    • Dubois SG, Beaulieu M, Levesque E, Hum DW, and Belanger A (1999) Alteration of human UDP-glucuronosyltransferase UGT2B17 regio-selectivity by a single amino acid substitution. J Mol Biol 289:29-39. (Pubitemid 29278361)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.1 , pp. 29-39
    • Dubois, S.G.1    Beaulieu, M.2    Levesque, E.3    Hum, D.W.4    Belanger, A.5
  • 8
    • 15244342411 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferases and clinical drug-drug interactions
    • Kiang TK, Ensom MH, and Chang TK (2005) UDP-glucuronosyltransferases and clinical drug-drug interactions. Pharmacol Ther 106:97-132.
    • (2005) Pharmacol Ther , vol.106 , pp. 97-132
    • Kiang, T.K.1    Ensom, M.H.2    Chang, T.K.3
  • 9
    • 34748850636 scopus 로고    scopus 로고
    • Critical roles of residues 36 and 40 in the phenol and tertiary amine aglycone substrate selectivities of UDP-glucuronosyltransferases 1A3 and 1A4
    • DOI 10.1124/mol.107.037952
    • Kubota T, Lewis BC, Elliot DJ, Mackenzie PI, and Miners JO (2007) Critical roles of residues 36 and 40 in the phenol and tertiary amine aglycone substrate selectivities of UDP-glucuronosyltransferases 1A3 and 1A4. Mol Pharmacol 72:1054-1062. (Pubitemid 47481428)
    • (2007) Molecular Pharmacology , vol.72 , Issue.4 , pp. 1054-1062
    • Kubota, T.1    Lewis, B.C.2    Elliot, D.J.3    Mackenzie, P.I.4    Miners, J.O.5
  • 10
    • 33947429721 scopus 로고    scopus 로고
    • Amino terminal domains of human UDP-glucuronosyltransferases (UGT) 2B7 and 2B15 associated with substrate selectivity and autoactivation
    • DOI 10.1016/j.bcp.2006.12.021, PII S0006295206008549
    • Lewis BC, Mackenzie PI, Elliot DJ, Burchell B, Bhasker CR, and Miners JO (2007) Amino terminal domains of human UDP-glucuronosyltransferases (UGT) 2B7 and 2B15 associated with substrate selectivity and autoactivation. Biochem Pharmacol 73:1463-1473. (Pubitemid 46452582)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.9 , pp. 1463-1473
    • Lewis, B.C.1    Mackenzie, P.I.2    Elliot, D.J.3    Burchell, B.4    Bhasker, C.R.5    Miners, J.O.6
  • 11
    • 34249946792 scopus 로고    scopus 로고
    • Adaptive evolution of multiple-variable exons and structural diversity of drug-metabolizing enzymes
    • DOI 10.1186/1471-2148-7-69
    • Li C and Wu Q (2007) Adaptive evolution of multiple variable exons and structural diversity of drug-metabolizing enzymes. BMC Evol Biol 7:69. (Pubitemid 46876381)
    • (2007) BMC Evolutionary Biology , vol.7 , pp. 69
    • Li, C.1    Wu, Q.2
  • 12
    • 37549030552 scopus 로고    scopus 로고
    • Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferase 1A
    • Li D, Fournel-Gigleux S, Barré L, Mulliert G, Netter P, Magdalou J, and Ouzzine M (2007) Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferase 1A. J Biol Chem 282:36514-36524.
    • (2007) J Biol Chem , vol.282 , pp. 36514-36524
    • Li, D.1    Fournel-Gigleux, S.2    Barré, L.3    Mulliert, G.4    Netter, P.5    Magdalou, J.6    Ouzzine, M.7
  • 13
    • 0031033883 scopus 로고    scopus 로고
    • Expression and functional domains of rabbit liver UDP- Glucuronosyltransferase 2B16 and 2B13
    • DOI 10.1074/jbc.272.6.3272
    • Li Q, Lou X, Peyronneau MA, Straub PO, and Tukey RH (1997) Expression and functional domains of rabbit liver UDP-glucuronosyltransferase 2B16 and 2B13. J Biol Chem 272:3272-3279. (Pubitemid 27066819)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , pp. 3272-3279
    • Li, Q.1    Lou, X.2    Peyronneau, M.-A.3    Straub, P.O.4    Tukey, R.H.5
  • 14
    • 33847027327 scopus 로고    scopus 로고
    • Comparative modelling of the human UDP-glucuronosyltransferases: Insights into structure and mechanism
    • DOI 10.1080/00498250601129109, PII 770494291
    • Locuson CW and Tracy TS (2007) Comparative modeling of the human UDP-glucuronosyltransferases: insights into structure and mechanism. Xenobiotica 37:155-168. (Pubitemid 46269618)
    • (2007) Xenobiotica , vol.37 , Issue.2 , pp. 155-168
    • Locuson, C.W.1    Tracy, T.S.2
  • 15
    • 0025236448 scopus 로고
    • Expression of chimeric cDNAs in cell culture defines a region of UDP-glucuronosyltransferase involved in substrate selection
    • Mackenzie PI (1990) Expression of chimeric cDNAs in cell culture defines a region of UDP-glucuronosyltransferase involved in substrate selection. J Biol Chem 265:3232-3235.
    • (1990) J Biol Chem , vol.265 , pp. 3232-3235
    • Mackenzie, P.I.1
  • 17
    • 1842536798 scopus 로고    scopus 로고
    • Amino acid residue ILE211 is essential for the enzymatic activity of human UDP-glucuronosyltransferase 1A10 (UGT1A10)
    • DOI 10.1124/dmd.32.4.455
    • Martineau I, Tchernof A, and Bélanger A (2004) Amino acid residue Ile211 is essential for the enzymatic activity of human UDP- glucuronosyltransferase 1A10 (UGT1A10). Drug Metab Dispos 32:455-459. (Pubitemid 38420281)
    • (2004) Drug Metabolism and Disposition , vol.32 , Issue.4 , pp. 455-459
    • Martineau, I.1    Tchernof, A.2    Belanger, A.3
  • 18
    • 34247618754 scopus 로고    scopus 로고
    • Crystal Structure of the Cofactor-Binding Domain of the Human Phase II Drug-Metabolism Enzyme UDP-Glucuronosyltransferase 2B7
    • DOI 10.1016/j.jmb.2007.03.066, PII S0022283607004329
    • Miley MJ, Zielinska AK, Keenan JE, Bratton SM, Radominska-Pandya A, and Redinbo MR (2007) Crystal structure of the cofactor binding domain of the human phase II drug metabolism enzyme UDP-glucuronosyltransferase 2B7. J Mol Biol 369:498-511. (Pubitemid 46678060)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.2 , pp. 498-511
    • Miley, M.J.1    Zielinska, A.K.2    Keenan, J.E.3    Bratton, S.M.4    Radominska-Pandya, A.5    Redinbo, M.R.6
  • 19
  • 20
    • 33646077674 scopus 로고    scopus 로고
    • In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: Pitfalls and promises
    • Miners JO, Knights KM, Houston JB, and Mackenzie PI (2006) In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: pitfalls and promises. Biochem Pharmacol 71:1531-1539.
    • (2006) Biochem Pharmacol , vol.71 , pp. 1531-1539
    • Miners, J.O.1    Knights, K.M.2    Houston, J.B.3    Mackenzie, P.I.4
  • 21
    • 0344610168 scopus 로고    scopus 로고
    • Predicting human drug glucuronidation parameters: Application of in vitro and in silico modeling approaches
    • Miners JO, Smith PA, Sorich MJ, McKinnon RA, and Mackenzie PI (2004) Predicting human drug glucuronidation parameters: application of in vitro and in silico modeling approaches. Annu Rev Pharmacol Toxicol 44:1-25.
    • (2004) Annu Rev Pharmacol Toxicol , vol.44 , pp. 1-25
    • Miners, J.O.1    Smith, P.A.2    Sorich, M.J.3    McKinnon, R.A.4    Mackenzie, P.I.5
  • 22
    • 49749116380 scopus 로고    scopus 로고
    • Mutation analysis in UGT1A9 suggests a relationship between substrate and catalytic residues in UDP-glucuronosyltransferases
    • Patana AS, Kurkela M, Finel M, and Goldman A (2008) Mutation analysis in UGT1A9 suggests a relationship between substrate and catalytic residues in UDP-glucuronosyltransferases. Protein Eng Des Sel 21:537-543.
    • (2008) Protein Eng des Sel , vol.21 , pp. 537-543
    • Patana, A.S.1    Kurkela, M.2    Finel, M.3    Goldman, A.4
  • 23
    • 34548356391 scopus 로고    scopus 로고
    • The human UDP-glucuronosyltransferase: Identification of key residues within the nucleotide-sugar binding site
    • DOI 10.1124/mol.107.036871
    • Patana AS, Kurkela M, Goldman A, and Finel M (2007) The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide sugar binding site. Mol Pharmacol 72:604-611. (Pubitemid 47347295)
    • (2007) Molecular Pharmacology , vol.72 , Issue.3 , pp. 604-611
    • Patana, A.-S.1    Kurkela, M.2    Goldman, A.3    Finel, M.4
  • 25
    • 0026591504 scopus 로고
    • Two human liver cDNAs encode UDP-glucuronosyltransferases with 2 log differences in activity toward parallel substrates including hyodeoxycholic acid and certain estrogen derivatives
    • Ritter JK, Chen F, Sheen YY, Lubet RA, and Owens IS (1993) Two human liver cDNAs encode UDP-glucuronosyltransferases with 2 log differences in activity toward parallel substrates including hyodeoxycholic acid and certain estrogen derivatives. Biochemistry 31:3409-3414.
    • (1993) Biochemistry , vol.31 , pp. 3409-3414
    • Ritter, J.K.1    Chen, F.2    Sheen, Y.Y.3    Lubet, R.A.4    Owens, I.S.5
  • 26
    • 0026701911 scopus 로고
    • A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini
    • Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, and Owens IS (1992) A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem 267:3257-3261.
    • (1992) J Biol Chem , vol.267 , pp. 3257-3261
    • Ritter, J.K.1    Chen, F.2    Sheen, Y.Y.3    Tran, H.M.4    Kimura, S.5    Yeatman, M.T.6    Owens, I.S.7
  • 29
    • 33845767068 scopus 로고    scopus 로고
    • The importance of local chemical structure for chemical metabolism by uridine 5′-diphosphate glucuronosyltransferase
    • Sorich MJ, McKinnon RA, Miners JO, and Smith PA (2006) The importance of local chemical structure for chemical metabolism by uridine 5′-diphosphate glucuronosyltransferase. J Chem Inf Model 46:2692-2697.
    • (2006) J Chem Inf Model , vol.46 , pp. 2692-2697
    • Sorich, M.J.1    McKinnon, R.A.2    Miners, J.O.3    Smith, P.A.4
  • 30
    • 0042679455 scopus 로고    scopus 로고
    • Isoform selectivity and kinetics of morphine 3- And 6-glucuronidation by human UDP-glucuronosyltransferases: Evidence for atypical glucuronidation kinetics by UGT2B7
    • DOI 10.1124/dmd.31.9.1086
    • Stone AN, Mackenzie PI, Galetin A, Houston JB, and Miners JO (2003) Isoform selectivity and kinetics of morphine 3- and 6-glucuronidation by human UDP-glucuronosyltransferases; evidence for atypical glucuronidation kinetics by UGT2B7. Drug Metab Dispos 31:1086-1089. (Pubitemid 37048278)
    • (2003) Drug Metabolism and Disposition , vol.31 , Issue.9 , pp. 1086-1089
    • Stone, A.N.1    Mackenzie, P.I.2    Galetin, A.3    Houston, J.B.4    Miners, J.O.5
  • 31
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression, and disease
    • DOI 10.1146/annurev.pharmtox.40.1.581
    • Tukey RH and Strassburg CP (2000) Human UDP-glucuronosyltransferases: metabolism, expression and disease. Annu Rev Pharmacol Toxicol 40:581-616. (Pubitemid 30340694)
    • (2000) Annual Review of Pharmacology and Toxicology , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 32
    • 0142074253 scopus 로고    scopus 로고
    • Glucuronidation of arachidonic and linoleic acid metabolites by human UDP-glucuronosyltransferases
    • DOI 10.1194/jlr.M300010-JLR200
    • Turgeon D, Chouinard S, Belanger P, Picard S, Labbe JF, Borgeat P, and Belanger A (2003) Glucuronidation of arachidonic acid and linoleic acid metabolites by human UDP-glucuronosyltransferases. J Lipid Res 44:1182-1191. (Pubitemid 37279636)
    • (2003) Journal of Lipid Research , vol.44 , Issue.6 , pp. 1182-1191
    • Turgeon, D.1    Chouinard, S.2    Belanger, P.3    Picard, S.4    Labbe, J.-F.5    Borgeat, P.6    Belanger, A.7
  • 33
    • 33344473930 scopus 로고    scopus 로고
    • Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine and sulfinpyrazone) 'probes' for human UDP-glucuronosyltransferases
    • Uchaipichat V, Mackenzie PI, Elliot DJ, and Miners JO (2006) Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine and sulfinpyrazone) 'probes' for human UDP-glucuronosyltransferases. Drug Metab Dispos 34:449-456.
    • (2006) Drug Metab Dispos , vol.34 , pp. 449-456
    • Uchaipichat, V.1    Mackenzie, P.I.2    Elliot, D.J.3    Miners, J.O.4
  • 34
    • 1842536833 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid
    • DOI 10.1124/dmd.32.4.413
    • Uchaipichat V, Mackenzie PI, Guo XH, Gardner-Stephen D, Galetin A, Houston JB, and Miners JO (2004) Human UDP-glucuronosyltransferases: isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid. Drug Metab Dispos 32:413-423. (Pubitemid 38420275)
    • (2004) Drug Metabolism and Disposition , vol.32 , Issue.4 , pp. 413-423
    • Uchaipichat, V.1    Mackenzie, P.I.2    Guo, X.-H.3    Gardner-Stephen, D.4    Galetin, A.5    Houston, J.B.6    Miners, J.O.7
  • 35
    • 34748822655 scopus 로고    scopus 로고
    • Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A substrates
    • DOI 10.1097/FPC.0b013e328256b1b6, PII 0121301120071200000002
    • Udomuksorn W, Elliot DJ, Lewis BC, Mackenzie PI, Yoovathaworn K, and Miners JO (2007) Influence of mutations associated with Gilbert and Crigler Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A (UGT1A) substrates. Pharmacogenet Genomics 17:1017-1029. (Pubitemid 351339486)
    • (2007) Pharmacogenetics and Genomics , vol.17 , Issue.12 , pp. 1017-1029
    • Udomuksorn, W.1    Elliot, D.J.2    Lewis, B.C.3    Mackenzie, P.I.4    Yoovathaworn, K.5    Miners, J.O.6
  • 36
    • 33144483681 scopus 로고    scopus 로고
    • Phenylalanine 90 and 93 are localized within the phenol binding site of human UDP-glucuronosyltransferase 1A10 as determined by photoaffinity labeling, mass spectrometry, and site-directed mutagenesis
    • DOI 10.1021/bi0519001
    • Xiong Y, Bernardi D, Bratton S, Ward MD, Battaglia E, Finel M, Drake RR, and Radominska- Pandya A (2006) Phenylalanine 90 and 93 are localized within the phenol binding site of human UDP-glucuronosyltransferase 1A10 as determined by photoaffinity labeling, mass spectrometry, and site-directed mutagenesis. Biochemistry 45:2322-2332. (Pubitemid 43271332)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2322-2332
    • Xiong, Y.1    Bernardi, D.2    Bratton, S.3    Ward, M.D.4    Battaglia, E.5    Finel, M.6    Drake, R.R.7    Radominska-Pandya, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.