메뉴 건너뛰기




Volumn 21, Issue 4, 2007, Pages 206-215

Functional activity of the mouse flavin-containing monooxygenase forms 1, 3, and 5

Author keywords

Expression and purification; mFMO1; mFMO3; mFMO5; Mouse flavin containing monooxygenase; pH profile; Substrate specificity; Thermal stability

Indexed keywords

DIMETHYLANILINE MONOOXYGENASE; ESONARIMOD; HYBRID PROTEIN; IMIDAZOLE DERIVATIVE; ISOENZYME; MALTOSE BINDING PROTEIN; PHENOTHIAZINE DERIVATIVE; TRIMETHYLAMINE; CARRIER PROTEIN; DIMETHYLANILINE MONOOXYGENASE (N-OXIDE FORMING); MALTOSE-BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXYGENASE; UNCLASSIFIED DRUG;

EID: 36048983802     PISSN: 10956670     EISSN: 10990461     Source Type: Journal    
DOI: 10.1002/jbt.20176     Document Type: Conference Paper
Times cited : (28)

References (28)
  • 1
    • 19444375492 scopus 로고    scopus 로고
    • Mammalian flavin-containing monooxygenases: Structure/function, genetic polymorphisms and role in drug metabolism
    • Krueger SK, Williams DE. Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism. Pharmacol Ther 2005;106(3):357-387.
    • (2005) Pharmacol Ther , vol.106 , Issue.3 , pp. 357-387
    • Krueger, S.K.1    Williams, D.E.2
  • 3
    • 0036076899 scopus 로고    scopus 로고
    • Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase
    • Hines RN, Hopp KA, Franco J, Saeian K, Begun FP. Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase. Mol Pharmacol 2002;62(2):320-325.
    • (2002) Mol Pharmacol , vol.62 , Issue.2 , pp. 320-325
    • Hines, R.N.1    Hopp, K.A.2    Franco, J.3    Saeian, K.4    Begun, F.P.5
  • 4
    • 1342309263 scopus 로고    scopus 로고
    • Organization and evolution of the flavin-containing monooxygenase genes of human and mouse: Identification of novel gene and pseudogene clusters
    • 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(2):117-130.
    • (2004) Pharmacogenetics , vol.14 , Issue.2 , pp. 117-130
    • Hernandez, D.1    Janmohamed, A.2    Chandan, P.3    Phillips, I.R.4    Shephard, E.A.5
  • 5
    • 2942596156 scopus 로고    scopus 로고
    • Cell-, tissue-, sex- and developmental stage-specific expression of mouse flavin-containing monooxygenases (FMOs)
    • Janmohamed A, Hernandez D, Phillips IR, Shephard EA. Cell-, tissue-, sex- and developmental stage-specific expression of mouse flavin-containing monooxygenases (FMOs). Biochem Pharmacol 2004;68(1):73-83.
    • (2004) Biochem Pharmacol , vol.68 , Issue.1 , pp. 73-83
    • Janmohamed, A.1    Hernandez, D.2    Phillips, I.R.3    Shephard, E.A.4
  • 6
    • 29944437885 scopus 로고    scopus 로고
    • Quantitative analysis of FMO gene mRNA levels in human tissues
    • Zhang J, Cashman JR. Quantitative analysis of FMO gene mRNA levels in human tissues. Drug Metab Dispos 2006;34(1):19-26.
    • (2006) Drug Metab Dispos , vol.34 , Issue.1 , pp. 19-26
    • Zhang, J.1    Cashman, J.R.2
  • 7
    • 0029310470 scopus 로고
    • Gender differences in hepatic expression of flavin-containing monooxygenase isoforms (FMO1, FMO3, and FMO5) in mice
    • Falls JG, Blake BL, Cao Y, Levi PE, Hodgson E. Gender differences in hepatic expression of flavin-containing monooxygenase isoforms (FMO1, FMO3, and FMO5) in mice. J Biochem Toxicol 1995;10(3):171-177.
    • (1995) J Biochem Toxicol , vol.10 , Issue.3 , pp. 171-177
    • Falls, J.G.1    Blake, B.L.2    Cao, Y.3    Levi, P.E.4    Hodgson, E.5
  • 8
    • 0036157094 scopus 로고    scopus 로고
    • Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression
    • Koukouritaki SB, Simpson P, Yeung CK, Rettie AE, Hines RN. Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression. Pediatr Res 2002;51(2):236-243.
    • (2002) Pediatr Res , vol.51 , Issue.2 , pp. 236-243
    • Koukouritaki, S.B.1    Simpson, P.2    Yeung, C.K.3    Rettie, A.E.4    Hines, R.N.5
  • 9
    • 0031878122 scopus 로고    scopus 로고
    • Physiological factors affecting protein expression of flavin-containing monooxygenases 1, 3 and 5
    • 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(7):673-682.
    • (1998) Xenobiotica , vol.28 , Issue.7 , pp. 673-682
    • Cherrington, N.J.1    Cao, Y.2    Cherrington, J.W.3    Rose, R.L.4    Hodgson, E.5
  • 10
    • 0031282528 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): Comparison with the human isoform
    • Falls JG, Cherrington NJ, Clements KM, Philpot RM, Levi PE, Rose RL, Hodgson E. Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): comparison with the human isoform. Arch Biochem Biophys 1997;347(1):9-18.
    • (1997) Arch Biochem Biophys , vol.347 , Issue.1 , pp. 9-18
    • Falls, J.G.1    Cherrington, N.J.2    Clements, K.M.3    Philpot, R.M.4    Levi, P.E.5    Rose, R.L.6    Hodgson, E.7
  • 12
    • 0035195097 scopus 로고    scopus 로고
    • Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse
    • Karoly ED, Rose RL. Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse. J Biochem Mol Toxicol 2001;15(6): 300-308.
    • (2001) J Biochem Mol Toxicol , vol.15 , Issue.6 , pp. 300-308
    • Karoly, E.D.1    Rose, R.L.2
  • 13
    • 0036782999 scopus 로고    scopus 로고
    • A practical procedure for the synthesis of esonarimod, (R,S)-2-acetylthiomethyl-4-(4-methylphenyl)- 4-oxobutanoic acid, an antirheumatic agent (Part 1)
    • Noguchi T, Onodera A, Tomisawa K, Yokomori S. A practical procedure for the synthesis of esonarimod, (R,S)-2-acetylthiomethyl-4-(4-methylphenyl)- 4-oxobutanoic acid, an antirheumatic agent (Part 1). Chem Pharm Bull (Tokyo) 2002;50:1407-1412.
    • (2002) Chem Pharm Bull (Tokyo) , vol.50 , pp. 1407-1412
    • Noguchi, T.1    Onodera, A.2    Tomisawa, K.3    Yokomori, S.4
  • 14
    • 0027185830 scopus 로고
    • Expression in Escherichia coli of the flavin-containing monooxygenase D (form II) from adult human liver: Determination of a distinct tertiary amine substrate specificity
    • Lomri N, Yang Z, Cashman JR. Expression in Escherichia coli of the flavin-containing monooxygenase D (form II) from adult human liver: determination of a distinct tertiary amine substrate specificity. Chem Res Toxicol 1993;6(4):425-429.
    • (1993) Chem Res Toxicol , vol.6 , Issue.4 , pp. 425-429
    • Lomri, N.1    Yang, Z.2    Cashman, J.R.3
  • 15
    • 0025151081 scopus 로고
    • Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: Differences due to substrate size
    • Nagata T, Williams DE, Ziegler DM. Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: differences due to substrate size. Chem Res Toxicol 1990;3(4):372-376.
    • (1990) Chem Res Toxicol , vol.3 , Issue.4 , pp. 372-376
    • Nagata, T.1    Williams, D.E.2    Ziegler, D.M.3
  • 16
    • 0030803384 scopus 로고    scopus 로고
    • Characterization of two human flavin-containing monooxygenase (form 3) enzymes expressed in Escherichia coli as maltose binding protein fusions
    • Brunelle A, Bi YA, Lin J, Russell B, Luy L, Berkman C, Cashman J. Characterization of two human flavin-containing monooxygenase (form 3) enzymes expressed in Escherichia coli as maltose binding protein fusions. Drug Metab Dispos 1997;25(8):1001-1007.
    • (1997) Drug Metab Dispos , vol.25 , Issue.8 , pp. 1001-1007
    • Brunelle, A.1    Bi, Y.A.2    Lin, J.3    Russell, B.4    Luy, L.5    Berkman, C.6    Cashman, J.7
  • 17
    • 0037974644 scopus 로고    scopus 로고
    • Two new polymorphisms of the FMO3 gene in Caucasian and African-American populations: Comparative genetic and functional studies
    • Lattard V, Zhang J, Tran Q, Furnes B, Schlenk D, Cashman JR. Two new polymorphisms of the FMO3 gene in Caucasian and African-American populations: comparative genetic and functional studies. Drug Metab Dispos 2003;31(7):854-860.
    • (2003) Drug Metab Dispos , vol.31 , Issue.7 , pp. 854-860
    • Lattard, V.1    Zhang, J.2    Tran, Q.3    Furnes, B.4    Schlenk, D.5    Cashman, J.R.6
  • 18
    • 1642498339 scopus 로고    scopus 로고
    • S-oxidation of S-methyl-esonarimod by flavin-containing monooxygenases in human liver microsomes
    • Ohmi N, Yoshida H, Endo H, Hasegawa M, Akimoto M, Higuchi S. S-oxidation of S-methyl-esonarimod by flavin-containing monooxygenases in human liver microsomes. Xenobiotica 2003;33(12):1221-1231.
    • (2003) Xenobiotica , vol.33 , Issue.12 , pp. 1221-1231
    • Ohmi, N.1    Yoshida, H.2    Endo, H.3    Hasegawa, M.4    Akimoto, M.5    Higuchi, S.6
  • 19
    • 0027494529 scopus 로고
    • Regio- and stereoselective oxygenations by adult human liver flavin-containing monooxygenase 3. Comparison with forms 1 and 2
    • Lomri N, Yang Z, Cashman JR, Regio- and stereoselective oxygenations by adult human liver flavin-containing monooxygenase 3. Comparison with forms 1 and 2. Chem Res Toxicol 1993;6(6):800-807.
    • (1993) Chem Res Toxicol , vol.6 , Issue.6 , pp. 800-807
    • Lomri, N.1    Yang, Z.2    Cashman, J.R.3
  • 20
    • 0028930879 scopus 로고
    • Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: Evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog
    • Overby LH, Buckpitt AR, Lawton MP, Atta-Asafo-Adjei E, Schulze J, Philpot RM. Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Arch Biochem Biophys 1995;317(1):275-284.
    • (1995) Arch Biochem Biophys , vol.317 , Issue.1 , pp. 275-284
    • Overby, L.H.1    Buckpitt, A.R.2    Lawton, M.P.3    Atta-Asafo-Adjei, E.4    Schulze, J.5    Philpot, R.M.6
  • 21
    • 0030833164 scopus 로고    scopus 로고
    • Quantitation and kinetic properties of hepatic microsomal and recombinant flavin-containing monooxygenases 3 and 5 from humans
    • Overby LH, Carver GC, Philpot RM. Quantitation and kinetic properties of hepatic microsomal and recombinant flavin-containing monooxygenases 3 and 5 from humans. Chem Biol Interact 1997;106(1):29-45.
    • (1997) Chem Biol Interact , vol.106 , Issue.1 , pp. 29-45
    • Overby, L.H.1    Carver, G.C.2    Philpot, R.M.3
  • 22
    • 0034241811 scopus 로고    scopus 로고
    • Size limits of thiocarbamides accepted as substrates by human flavin-containing monooxygenase 1
    • Kim YM, Ziegler DM. Size limits of thiocarbamides accepted as substrates by human flavin-containing monooxygenase 1. Drug Metab Dispos 2000;28(8):1003-1006.
    • (2000) Drug Metab Dispos , vol.28 , Issue.8 , pp. 1003-1006
    • Kim, Y.M.1    Ziegler, D.M.2
  • 23
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenases: Catalytic mechanism and substrate specificities
    • Ziegler DM. Flavin-containing monooxygenases: catalytic mechanism and substrate specificities. Drug Metab Rev 1988;19(1):1-32.
    • (1988) Drug Metab Rev , vol.19 , Issue.1 , pp. 1-32
    • Ziegler, D.M.1
  • 24
    • 0036036854 scopus 로고    scopus 로고
    • An overview of the mechanism, substrate specificities, and structure of FMOs
    • Ziegler DM. An overview of the mechanism, substrate specificities, and structure of FMOs. Drug Metab Rev 2002;34(3):503-511.
    • (2002) Drug Metab Rev , vol.34 , Issue.3 , pp. 503-511
    • Ziegler, D.M.1
  • 25
    • 0024974962 scopus 로고
    • Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution. Analysis of the enzyme-substrate and enzyme-product complexes
    • Schreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, Drenth J. Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution. Analysis of the enzyme-substrate and enzyme-product complexes. J Mol Biol 1989;208(4):679-696.
    • (1989) J Mol Biol , vol.208 , Issue.4 , pp. 679-696
    • Schreuder, H.A.1    Prick, P.A.2    Wierenga, R.K.3    Vriend, G.4    Wilson, K.S.5    Hol, W.G.6    Drenth, J.7
  • 26
    • 26444508868 scopus 로고    scopus 로고
    • Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase
    • Frederick KK, Palfey BA. Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase. Biochemistry 2005;44(40):13304-13314.
    • (2005) Biochemistry , vol.44 , Issue.40 , pp. 13304-13314
    • Frederick, K.K.1    Palfey, B.A.2
  • 27
    • 27544432463 scopus 로고    scopus 로고
    • Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases
    • Ballou DP, Entsch B, Cole LJ. Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases. Biochem Bio Phys Res Commun 2005;338(1):590-598.
    • (2005) Biochem Bio Phys Res Commun , vol.338 , Issue.1 , pp. 590-598
    • Ballou, D.P.1    Entsch, B.2    Cole, L.J.3
  • 28
    • 0033770639 scopus 로고    scopus 로고
    • In vitro evaluation of potential in vivo probes for human flavin-containing monooxygenase (FMO): Metabolism of benzydamine and caffeine by FMO and P450 isoforms
    • Lang DH, Rettie AE. In vitro evaluation of potential in vivo probes for human flavin-containing monooxygenase (FMO): metabolism of benzydamine and caffeine by FMO and P450 isoforms. Br J Clin Pharmacol 2000;50(4):311-314.
    • (2000) Br J Clin Pharmacol , vol.50 , Issue.4 , pp. 311-314
    • Lang, D.H.1    Rettie, A.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.