메뉴 건너뛰기




Volumn 51, Issue 10, 2012, Pages 2157-2168

Mechanism of inhibition for N6022, a first-in-class drug targeting S-nitrosoglutathione reductase

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL MODEL; CHRONIC OBSTRUCTIVE PULMONARY DISEASE; CLINICAL STUDY; COFACTORS; DRUG-TARGETING; INFLAMMATORY BOWEL DISEASE; INHIBITORY ACTIVITY; KINETIC ASSAY; OXIDATION AND REDUCTION; RELATED COMPOUNDS; S-NITROSOGLUTATHIONE; SUBSTRATE BINDING; TIGHT BINDING;

EID: 84863237651     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201785u     Document Type: Article
Times cited : (69)

References (49)
  • 1
    • 0021757678 scopus 로고
    • Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: π-ADH
    • Wagner, F. W., Parés, X., Holmquist, B., and Vallee, B. L. (1984) Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: π-ADH Biochemistry 23, 2193-2199
    • (1984) Biochemistry , vol.23 , pp. 2193-2199
    • Wagner, F.W.1    Parés, X.2    Holmquist, B.3    Vallee, B.L.4
  • 2
    • 0023517566 scopus 로고
    • Mammalian alcohol dehydrogenase: Characteristics of class III isoenzymes
    • Juliá, P., Boleda, M. D., Farrés, J., and Parés, X. (1987) Mammalian alcohol dehydrogenase: Characteristics of class III isoenzymes Alcohol Suppl. 1) 169-173
    • (1987) Alcohol , Issue.SUPPL. 1 , pp. 169-173
    • Juliá, P.1    Boleda, M.D.2    Farrés, J.3    Parés, X.4
  • 3
    • 0024422072 scopus 로고
    • Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase
    • DOI 10.1016/0014-5793(89)81797-1
    • Koivusalo, M., Baumann, M., and Uotila, L. (1989) Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase FEBS Lett. 257, 105-109 (Pubitemid 19261773)
    • (1989) FEBS Letters , vol.257 , Issue.1 , pp. 105-109
    • Koivusalo, M.1    Baumann, M.2    Uotila, L.3
  • 4
    • 0026076043 scopus 로고
    • Human liver class III alcohol and glutathione dependent formaldehyde dehydrogenase are the same enzyme
    • Holmquist, B. and Vallee, B. L. (1991) Human liver class III alcohol and glutathione dependent formaldehyde dehydrogenase are the same enzyme Biochem. Biophys. Res. Commun. 178, 1371-1377
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 1371-1377
    • Holmquist, B.1    Vallee, B.L.2
  • 5
    • 58149141583 scopus 로고    scopus 로고
    • Dual functions of alcohol dehydrogenase 3: Implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities
    • Staab, C. A., Hellgren, M., and Höög, J. O. (2008) Dual functions of alcohol dehydrogenase 3: Implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities Cell. Mol. Life Sci. 65, 3950-3960
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3950-3960
    • Staab, C.A.1    Hellgren, M.2    Höög, J.O.3
  • 6
    • 0026778829 scopus 로고
    • "enzymogenesis": Classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line
    • Danielsson, O. and Jörnvall, H. (1992) "Enzymogenesis": Classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line Proc. Natl. Acad. Sci. U.S.A. 89, 9247-9251
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9247-9251
    • Danielsson, O.1    Jörnvall, H.2
  • 7
    • 0035139107 scopus 로고    scopus 로고
    • Mammalian alcohol dehydrogenase - Functional and structural implications
    • DOI 10.1159/000054015
    • Höög, J. O., Hedberg, J. J., Strömberg, P., and Svensson, S. (2001) Mammalian alcohol dehydrogenase: Functional and structural implications J. Biomed. Sci. 8, 71-76 (Pubitemid 32098487)
    • (2001) Journal of Biomedical Science , vol.8 , Issue.1 , pp. 71-76
    • Hoog, J.-O.1    Hedberg, J.J.2    Stromberg, P.3    Svensson, S.4
  • 8
    • 29244479504 scopus 로고    scopus 로고
    • Merging protein, gene and genomic data: The evolution of the MDR-ADH family
    • DOI 10.1038/sj.hdy.6800723, PII 6800723
    • Gonzàlez-Duarte, R. and Albalat, R. (2005) Merging protein, gene and genomic data: The evolution of the MDR-ADH family Heredity 95, 184-197 (Pubitemid 43102279)
    • (2005) Heredity , vol.95 , Issue.3 , pp. 184-197
    • Gonzalez-Duarte, R.1    Albalat, R.2
  • 10
    • 0030592763 scopus 로고    scopus 로고
    • Alcohol dehydrogenase in human tissues: Localisation of transcripts coding for five classes of the enzyme
    • DOI 10.1016/S0014-5793(96)01204-5, PII S0014579396012045
    • Estonius, M., Svensson, S., and Höög, J. O. (1996) Alcohol dehydrogenase in human tissues: Localisation of transcripts coding for five classes of the enzyme FEBS Lett. 397, 338-342 (Pubitemid 26414045)
    • (1996) FEBS Letters , vol.397 , Issue.2-3 , pp. 338-342
    • Estonius, M.1    Svensson, S.2    Hoog, J.-O.3
  • 11
    • 34147141506 scopus 로고    scopus 로고
    • Tissue-specific mRNA expression profiles of human phase i metabolizing enzymes except for cytochrome P450 and phase II metabolizing enzymes
    • Nishimura, M. and Naito, S. (2006) Tissue-specific mRNA expression profiles of human phase I metabolizing enzymes except for cytochrome P450 and phase II metabolizing enzymes Drug Metab. Pharmacokinet. 21, 357-374
    • (2006) Drug Metab. Pharmacokinet. , vol.21 , pp. 357-374
    • Nishimura, M.1    Naito, S.2
  • 12
  • 13
    • 0032522535 scopus 로고    scopus 로고
    • S-nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
    • Jensen, D. E., Belka, G. K., and Du Bois, G. C. (1998) S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme Biochem. J. 331, 659-668 (Pubitemid 28182185)
    • (1998) Biochemical Journal , vol.331 , Issue.2 , pp. 659-668
    • Jensen, D.E.1    Belka, G.K.2    Du Bois, G.C.3
  • 14
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • DOI 10.1038/35068596
    • Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J., and Stamler, J. S. (2001) A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans Nature 410, 490-494 (Pubitemid 32240051)
    • (2001) Nature , vol.410 , Issue.6827 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 15
    • 0038136867 scopus 로고    scopus 로고
    • S-nitrosylation in health and disease
    • DOI 10.1016/S1471-4914(03)00028-5
    • Foster, M. W., McMahon, T. J., and Stamler, J. S. (2003) S-nitrosylation in health and disease Trends Mol. Med. 9, 160-168 (Pubitemid 36626705)
    • (2003) Trends in Molecular Medicine , vol.9 , Issue.4 , pp. 160-168
    • Foster, M.W.1    McMahon, T.J.2    Stamler, J.S.3
  • 16
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • Foster, M. W., Hess, D. T., and Stamler, J. S. (2009) Protein S-nitrosylation in health and disease: A current perspective Trends Mol. Med. 9, 391-404
    • (2009) Trends Mol. Med. , vol.9 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 17
  • 18
    • 0031046328 scopus 로고    scopus 로고
    • Structure of human χχ alcohol dehydrogenase: A glutathione-dependent formaldehyde dehydrogenase
    • DOI 10.1006/jmbi.1996.0731
    • Yang, Z. N., Bosron, W. F., and Hurley, T. D. (1997) Structure of human chi chi alcohol dehydrogenase: A glutathione-dependent formaldehyde dehydrogenase J. Mol. Biol. 265, 330-343 (Pubitemid 27110689)
    • (1997) Journal of Molecular Biology , vol.265 , Issue.3 , pp. 330-343
    • Yang, Z.-N.1    Bosron, W.F.2    Hurley, T.D.3
  • 19
    • 0037015156 scopus 로고    scopus 로고
    • Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes
    • DOI 10.1021/bi0257639
    • Sanghani, P. C., Robinson, H., Bosron, W. F., and Hurley, T. D. (2002) Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes Biochemistry 41, 10778-10786 (Pubitemid 34971054)
    • (2002) Biochemistry , vol.41 , Issue.35 , pp. 10778-10786
    • Sanghani, P.C.1    Robinson, H.2    Bosron, W.F.3    Hurley, T.D.4
  • 20
    • 0037168478 scopus 로고    scopus 로고
    • Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation
    • DOI 10.1021/bi026705q
    • Sanghani, P. C., Bosron, W. F., and Hurley, T. D. (2002) Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation Biochemistry 41, 15189-15194 (Pubitemid 36008127)
    • (2002) Biochemistry , vol.41 , Issue.51 , pp. 15189-15194
    • Sanghani, P.C.1    Bosron, W.F.2    Hurley, T.D.3
  • 21
    • 0344643061 scopus 로고    scopus 로고
    • Structure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase)
    • DOI 10.1016/S0009-2797(02)00203-X, PII S000927970200203X
    • Sanghani, P. C., Robinson, H., Bennett-Lovsey, R., Hurley, T. D., and Bosron, W. F. (2003) Structure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase) Chem.-Biol. Interact. 143-144, 195-200 (Pubitemid 36246441)
    • (2003) Chemico-Biological Interactions , vol.143-144 , pp. 195-200
    • Sanghani, P.C.1    Robinson, H.2    Bennett-Lovsey, R.3    Hurley, T.D.4    Bosron, W.F.5
  • 22
    • 0034609526 scopus 로고    scopus 로고
    • Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase
    • Sanghani, P. C., Stone, C. L., Ray, B. D., Pindel, E. V., Hurley, T. D., and Bosron, W. F. (2000) Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase Biochemistry 39, 10720-10729
    • (2000) Biochemistry , vol.39 , pp. 10720-10729
    • Sanghani, P.C.1    Stone, C.L.2    Ray, B.D.3    Pindel, E.V.4    Hurley, T.D.5    Bosron, W.F.6
  • 23
    • 0037351726 scopus 로고    scopus 로고
    • Reduction of S-nitrosoglutathione by human alcohol dehydrogenase 3 is an irreversible reaction as analysed by electrospray mass spectrometry
    • DOI 10.1046/j.1432-1033.2003.03486.x
    • Hedberg, J. J., Griffiths, W. J., Nilsson, S. J., and Höög, J. O. (2003) Reduction of S-nitrosoglutathione by human alcohol dehydrogenase 3 is an irreversible reaction as analysed by electrospray mass spectrometry Eur. J. Biochem. 270, 1249-1256 (Pubitemid 36388743)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1249-1256
    • Hedberg, J.J.1    Griffiths, W.J.2    Nilsson, S.J.F.3    Hoog, J.-O.4
  • 25
    • 67349222284 scopus 로고    scopus 로고
    • Medium-chain fatty acids and glutathione derivatives as inhibitors of S-nitrosoglutathione reduction mediated by alcohol dehydrogenase 3
    • Staab, C. A., Hellgren, M., Grafström, R. C., and Höög, J. O. (2009) Medium-chain fatty acids and glutathione derivatives as inhibitors of S-nitrosoglutathione reduction mediated by alcohol dehydrogenase 3 Chem.-Biol. Interact. 180, 113-118
    • (2009) Chem.-Biol. Interact. , vol.180 , pp. 113-118
    • Staab, C.A.1    Hellgren, M.2    Grafström, R.C.3    Höög, J.O.4
  • 26
    • 48249147530 scopus 로고    scopus 로고
    • Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate alcohols via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors
    • Staab, C. A., Ålander, J., Brandt, M., Lengqvist, J., Morgenstern, R., Grafström, R. C., and Höög, J. O. (2008) Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate alcohols via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors Biochem. J. 413, 493-504
    • (2008) Biochem. J. , vol.413 , pp. 493-504
    • Staab, C.A.1    Ålander, J.2    Brandt, M.3    Lengqvist, J.4    Morgenstern, R.5    Grafström, R.C.6    Höög, J.O.7
  • 27
    • 20444410779 scopus 로고    scopus 로고
    • Biomedicine: Protection from experimental asthma by an endogenous bronchodilator
    • DOI 10.1126/science.1108228
    • Que, L. G., Liu, L., Yan, Y., Whitehead, G. S., Gavett, S. H., Schwartz, D. A., and Stamler, J. S. (2005) Protection from experimental asthma by an endogenous bronchodilator Science 308, 1618-1621 (Pubitemid 40807509)
    • (2005) Science , vol.308 , Issue.5728 , pp. 1618-1621
    • Que, L.G.1    Liu, L.2    Yan, Y.3    Whitehead, G.S.4    Gavett, S.H.5    Schwartz, D.A.6    Stamler, J.S.7
  • 30
    • 0032947628 scopus 로고    scopus 로고
    • S-Nitrosoglutathione enhances neutrophil DNA fragmentation and cell death
    • Fortenberry, J. D., Owens, M. L., and Brown, L. A. (1999) S-Nitrosoglutathione enhances neutrophil DNA fragmentation and cell death Am. J. Physiol. 276, L435-L442
    • (1999) Am. J. Physiol. , vol.276
    • Fortenberry, J.D.1    Owens, M.L.2    Brown, L.A.3
  • 36
    • 84855503316 scopus 로고    scopus 로고
    • A nonclinical safety and pharmacokinetic evaluation of N6022: A first-in-class S-nitrosoglutathione reductase inhibitor for the treatment of asthma
    • Colagiovanni, D. B., Drolet, D. W., Langlois-Forget, E., Piché, M. P., Looker, D., and Rosenthal, G. J. (2012) A nonclinical safety and pharmacokinetic evaluation of N6022: A first-in-class S-nitrosoglutathione reductase inhibitor for the treatment of asthma Regul. Toxicol. Pharmacol. 62, 115-124
    • (2012) Regul. Toxicol. Pharmacol. , vol.62 , pp. 115-124
    • Colagiovanni, D.B.1    Drolet, D.W.2    Langlois-Forget, E.3    Piché, M.P.4    Looker, D.5    Rosenthal, G.J.6
  • 38
    • 37149050839 scopus 로고    scopus 로고
    • Reversible Modes of Inhibitor Interactions with Enzymes
    • In, pp, John Wiley & Sons, Inc. Hoboken, NJ.
    • Copeland, R. A. (2005) Reversible Modes of Inhibitor Interactions with Enzymes. In Evaluation of Enzyme Inhibitors in Drug Discovery, pp 48-81, John Wiley & Sons, Inc., Hoboken, NJ.
    • (2005) Evaluation of Enzyme Inhibitors in Drug Discovery , pp. 48-81
    • Copeland, R.A.1
  • 41
    • 58149103872 scopus 로고    scopus 로고
    • Human carbonyl reductase 1 is an S-nitrosoglutathione reductase
    • Bateman, R. L., Rauh, D., Tavshanjian, B., and Shokat, K. M. (2008) Human carbonyl reductase 1 is an S-nitrosoglutathione reductase J. Biol. Chem. 283, 35756-35762
    • (2008) J. Biol. Chem. , vol.283 , pp. 35756-35762
    • Bateman, R.L.1    Rauh, D.2    Tavshanjian, B.3    Shokat, K.M.4
  • 42
    • 58149105437 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: Three-dimensional structures of MDR alcohol dehydrogenases
    • Eklund, H. and Ramaswamy, S. (2008) Medium- and short-chain dehydrogenase/reductase gene and protein families: Three-dimensional structures of MDR alcohol dehydrogenases Cell. Mol. Life Sci. 65, 3907-3917
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3907-3917
    • Eklund, H.1    Ramaswamy, S.2
  • 43
    • 0030877359 scopus 로고    scopus 로고
    • X-ray structure of human class IV σσ alcohol dehydrogenase. Structural basis for substrate specificity
    • DOI 10.1074/jbc.272.30.18558
    • Xie, P., Parsons, S. H., Speckhard, D. C., Bosron, W. F., and Hurley, T. D. (1997) X-ray structure of human class IV sigma sigma alcohol dehydrogenase. Structural basis for substrate specificity J. Biol. Chem. 272, 18558-18563 (Pubitemid 27318194)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18558-18563
    • Xie, P.1    Parsons, S.H.2    Speckhard, D.C.3    Bosron, W.F.4    Hurley, T.D.5
  • 44
    • 0032974743 scopus 로고    scopus 로고
    • Impaired retinol utilization in Adh4 alcohol dehydrogenase mutant mice
    • DOI 10.1002/(SICI)1520-6408(1999)25:1<1::AID-DVG1>3.0.CO;2-W
    • Deltour, L., Foglio, M. H., and Duester, G. (1999) Impaired retinol utilization in Adh4 alcohol dehydrogenase mutant mice Dev. Genet. 25, 1-10 (Pubitemid 29305102)
    • (1999) Developmental Genetics , vol.25 , Issue.1 , pp. 1-10
    • Deltour, L.1    Foglio, M.H.2    Duester, G.3
  • 45
    • 84863247738 scopus 로고    scopus 로고
    • Lead Optimization and Structure-Activity Relationships for Reversible Inhibitors
    • In, pp, John Wiley & Sons, Inc. Hoboken, NJ.
    • Copeland, R. A. (2005) Lead Optimization and Structure-Activity Relationships for Reversible Inhibitors. In Evalation of Enzyme Inhibitors in Drug Discovery, pp 111-140, John Wiley & Sons, Inc., Hoboken, NJ.
    • (2005) Evalation of Enzyme Inhibitors in Drug Discovery , pp. 111-140
    • Copeland, R.A.1
  • 46
    • 4544381198 scopus 로고    scopus 로고
    • Biochemical mechanisms of drug action: What does it take for success?
    • DOI 10.1038/nrd1500
    • Swinney, D. C. (2004) Biochemical mechanisms of drug action: What does it take for success? Nat. Rev. Drug Discovery 3, 801-808 (Pubitemid 39242832)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.9 , pp. 801-808
    • Swinney, D.C.1
  • 47
    • 58449131873 scopus 로고    scopus 로고
    • The role of binding kinetics in therapeutically useful drug action
    • Swinney, D. C. (2009) The role of binding kinetics in therapeutically useful drug action Curr. Opin. Drug Discovery Dev. 12, 31-39
    • (2009) Curr. Opin. Drug Discovery Dev. , vol.12 , pp. 31-39
    • Swinney, D.C.1
  • 48
    • 0029981211 scopus 로고    scopus 로고
    • Enzyme inhibition in open systems. Superiority of uncompetitive agents
    • Westley, A. M. and Westley, J. (1996) Enzyme inhibition in open systems. Superiority of uncompetitive agents J. Biol. Chem. 271, 5347-5352
    • (1996) J. Biol. Chem. , vol.271 , pp. 5347-5352
    • Westley, A.M.1    Westley, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.