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Volumn 50, Issue 35, 2011, Pages 7710-7717

2H kinetic isotope effects and pH dependence of catalysis as mechanistic probes of rat monoamine oxidase A: Comparisons with the human enzyme

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL MODEL; BENZYLAMINES; BINDING AFFINITIES; C-H BOND CLEAVAGE; DEUTERIUM KINETIC ISOTOPE EFFECT; DOMINANT CONTRIBUTIONS; ELECTRONIC SUBSTITUENT PARAMETERS; FLAVOENZYMES; FUNCTIONAL PROPERTIES; HUMAN ENZYMES; KINETIC ISOTOPE EFFECTS; MECHANISTIC PROBES; MEMBRANE-BOUND; MONOAMINE OXIDASE A; NUCLEOPHILIC MECHANISMS; PH DEPENDENCE; QUANTITATIVE STRUCTURE ACTIVITY RELATIONSHIP; RATE LIMITING; STRUCTURE-ACTIVITY; VAN DER WAALS VOLUME;

EID: 80052245133     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200951z     Document Type: Article
Times cited : (34)

References (34)
  • 4
    • 0032914318 scopus 로고    scopus 로고
    • Monoamine oxidase: From genes to behavior
    • DOI 10.1146/annurev.neuro.22.1.197
    • Shih, J. C., Chen, K., and Ridd, M. J. (1999) Monoamine oxidase: From genes to behavior Annu. Rev. Neurosci. 22, 197-217 (Pubitemid 29144886)
    • (1999) Annual Review of Neuroscience , vol.22 , pp. 197-217
    • Shih, J.C.1    Chen, K.2    Ridd, M.J.3
  • 5
    • 51249118269 scopus 로고    scopus 로고
    • Monoamine oxidase inactivation: From pathophysiology to therapeutics
    • Bortolato, M., Chen, K., and Shih, J. C. (2008) Monoamine oxidase inactivation: From pathophysiology to therapeutics Adv. Drug Delivery Rev. 60, 1527-1533
    • (2008) Adv. Drug Delivery Rev. , vol.60 , pp. 1527-1533
    • Bortolato, M.1    Chen, K.2    Shih, J.C.3
  • 6
    • 33644874936 scopus 로고    scopus 로고
    • Oxidative stress by monoamine oxidase mediates receptor-independent cardiomyocyte apoptosis by serotonin and postischemic myocardial injury
    • DOI 10.1161/CIRCULATIONAHA.104.528133, PII 0000301720051122000015
    • Bianchi, P., Kunduzova, O., Masini, E., Cambon, C., Bani, D., Raimondi, L., Seguelas, M. H., Nistri, S., Colucci, W., Leducq, N., and Parini, A. (2005) Oxidative stress by monoamine oxidase mediates receptor-independent cardiomyocyte apoptosis by serotonin and postischemic myocardial injury Circulation 112, 3297-3305 (Pubitemid 43739375)
    • (2005) Circulation , vol.112 , Issue.21 , pp. 3297-3305
    • Bianchi, P.1    Kunduzova, O.2    Masini, E.3    Cambon, C.4    Bani, D.5    Raimondi, L.6    Seguelas, M.-H.7    Nistri, S.8    Colucci, W.9    Leducq, N.10    Parini, A.11
  • 9
    • 1842474296 scopus 로고    scopus 로고
    • Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors
    • DOI 10.1016/j.jmb.2004.02.032, PII S0022283604001998
    • Ma, J., Yoshimura, M., Yamashita, E., Nakagawa, A., Ito, A., and Tsukihara, T. (2004) Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors J. Mol. Biol. 338, 103-114 (Pubitemid 38429789)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.1 , pp. 103-114
    • Ma, J.1    Yoshimura, M.2    Yamashita, E.3    Nakagawa, A.4    Ito, A.5    Tsukihara, T.6
  • 10
    • 38949096792 scopus 로고    scopus 로고
    • Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl β-D-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy
    • DOI 10.1021/bi7021377
    • Upadhyay, A. K., Borbat, P. P., Wang, J., Freed, J. H., and Edmondson, D. E. (2008) Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl β- d -glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy Biochemistry 47, 1554-1566 (Pubitemid 351231206)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1554-1566
    • Upadhyay, A.K.1    Borbat, P.P.2    Wang, J.3    Freed, J.H.4    Edmondson, D.E.5
  • 11
    • 34249940141 scopus 로고    scopus 로고
    • Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: Insights from molecular modeling studies
    • DOI 10.1016/j.bmc.2007.05.021, PII S0968089607004208
    • Fierro, A., Osorio-Olivares, M., Cassels, B. K., Edmondson, D. E., Sepulveda-Boza, S., and Reyes-Parada, M. (2007) Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: Insights from molecular modeling studies Bioorg. Med. Chem. 15, 5198-5206 (Pubitemid 46880373)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.15 , pp. 5198-5206
    • Fierro, A.1    Osorio-Olivares, M.2    Cassels, B.K.3    Edmondson, D.E.4    Sepulveda-Boza, S.5    Reyes-Parada, M.6
  • 12
    • 0033550070 scopus 로고    scopus 로고
    • Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A
    • Miller, J. R. and Edmondson, D. E. (1999) Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A Biochemistry 38, 13670-13683
    • (1999) Biochemistry , vol.38 , pp. 13670-13683
    • Miller, J.R.1    Edmondson, D.E.2
  • 13
    • 47249152398 scopus 로고    scopus 로고
    • The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzyme-substrate complex
    • DOI 10.1111/j.1742-4658.2008.06532.x
    • Dunn, R. V., Marshall, K. R., Munro, A. W., and Scrutton, N. S. (2008) The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzyme-substrate complex FEBS J. 275, 3850-3858 (Pubitemid 351990950)
    • (2008) FEBS Journal , vol.275 , Issue.15 , pp. 3850-3858
    • Dunn, R.V.1    Marshall, K.R.2    Munro, A.W.3    Scrutton, N.S.4
  • 14
    • 76749104256 scopus 로고    scopus 로고
    • High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: Comparison with human MAO A
    • Wang, J. and Edmondson, D. E. (2010) High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: Comparison with human MAO A Protein Expression Purif. 70, 211-217
    • (2010) Protein Expression Purif. , vol.70 , pp. 211-217
    • Wang, J.1    Edmondson, D.E.2
  • 15
    • 0028278443 scopus 로고
    • Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B
    • DOI 10.1021/bi00189a011
    • Walker, M. C. and Edmondson, D. E. (1994) Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B Biochemistry 33, 7088-7098 (Pubitemid 24208745)
    • (1994) Biochemistry , vol.33 , Issue.23 , pp. 7088-7098
    • Walker, M.C.1    Edmondson, D.E.2
  • 16
    • 0014454095 scopus 로고
    • Kinetics of reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison, J. F. (1969) Kinetics of reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors Biochim. Biophys. Acta 185, 269-286
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 18
    • 20544433165 scopus 로고
    • Van der waals volumes and radii
    • Bondi, A. (1964) Van der waals volumes and radii J. Phys. Chem. 68, 441-451
    • (1964) J. Phys. Chem. , vol.68 , pp. 441-451
    • Bondi, A.1
  • 19
    • 0001222320 scopus 로고
    • Calculation of substrate dissociation-constants from steady-state isotope effects in enzyme-catalyzed reactions
    • Klinman, J. P. and Matthews, R. G. (1985) Calculation of substrate dissociation-constants from steady-state isotope effects in enzyme-catalyzed reactions J. Am. Chem. Soc. 107, 1058-1060
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 1058-1060
    • Klinman, J.P.1    Matthews, R.G.2
  • 20
    • 73149102982 scopus 로고    scopus 로고
    • Mechanistic studies of para-substituted N,N′-dibenzyl-1,4- diaminobutanes as substrates for a mammalian polyamine oxidase
    • Pozzi, M. H., Gawandi, V., and Fitzpatrick, P. F. (2009) Mechanistic studies of para-substituted N,N′-dibenzyl-1,4-diaminobutanes as substrates for a mammalian polyamine oxidase Biochemistry 48, 12305-12313
    • (2009) Biochemistry , vol.48 , pp. 12305-12313
    • Pozzi, M.H.1    Gawandi, V.2    Fitzpatrick, P.F.3
  • 21
    • 0036467588 scopus 로고    scopus 로고
    • Kinetics and mechanism of the oxidation of substituted benzylamines by hexamethylenetetramine-bromine
    • DOI 10.1002/poc.456
    • Dubey, R., Kothari, S., and Banerji, K. K. (2002) Kinetics and mechanism of the oxidation of substituted benzylamines by hexamethylenetetramine-bromine J. Phys. Org. Chem. 15, 103-107 (Pubitemid 34104732)
    • (2002) Journal of Physical Organic Chemistry , vol.15 , Issue.2 , pp. 103-107
    • Dubey, R.1    Kothari, S.2    Banerji, K.K.3
  • 22
    • 17744364487 scopus 로고    scopus 로고
    • Kinetics and mechanism of the oxidation of substituted benzylamines by cetyltrimethylammonium permanganate
    • Shukla, R., Sharma, P. K., Kotai, L., and Banerji, K. (2003) Kinetics and mechanism of the oxidation of substituted benzylamines by cetyltrimethylammonium permanganate Proc.-Indian Acad. Sci., Chem. Sci. 115, 129-134 (Pubitemid 40574211)
    • (2003) Journal of Chemical Sciences , vol.115 , Issue.2 , pp. 129-134
    • Shukla, R.1    Sharma, P.K.2    Kotai, L.3    Banerji, K.K.4
  • 23
    • 80051596304 scopus 로고    scopus 로고
    • 2)Benzylamine. Nitrogen Rehybridization and CH Bond Cleavage are Not Concerted
    • 2)Benzylamine. Nitrogen Rehybridization and CH Bond Cleavage are Not Concerted J. Am. Chem. Soc. 133, 12319-12321
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 12319-12321
    • MacMillar, S.1    Edmondson, D.E.2    Matsson, O.3
  • 24
    • 0014594785 scopus 로고
    • Human liver mitochondrial monoamine oxidase. II. Determinants of substrate and inhibitor specificities
    • McEwen, C. M., Sasaki, G., and Jones, D. C. (1969) Human liver mitochondrial monoamine oxidase. II. Determinants of substrate and inhibitor specificities Biochemistry 8, 3952-3962
    • (1969) Biochemistry , vol.8 , pp. 3952-3962
    • McEwen, C.M.1    Sasaki, G.2    Jones, D.C.3
  • 25
    • 0014430090 scopus 로고
    • Human liver mitochondrial monoamine oxidase. I. Kinetic studies of model interactions
    • McEwen, C. M., Sasaki, G., and Lenz, W. R. (1968) Human liver mitochondrial monoamine oxidase. I. Kinetic studies of model interactions J. Biol. Chem. 243, 5217-5225
    • (1968) J. Biol. Chem. , vol.243 , pp. 5217-5225
    • McEwen, C.M.1    Sasaki, G.2    Lenz, W.R.3
  • 28
    • 38849116342 scopus 로고    scopus 로고
    • Comparison of the structural properties of the active site cavities of human and rat monoamine oxidase A and B in their soluble and membrane-bound forms
    • DOI 10.1021/bi7019707
    • Upadhyay, A. K., Wang, J., and Edmondson, D. E. (2008) Comparison of the structural properties of the active site cavities of human and rat monoamine oxidase A and B in their soluble and membrane-bound forms Biochemistry 47, 526-536 (Pubitemid 351195425)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 526-536
    • Upadhyay, A.K.1    Wang, J.2    Edmondson, D.E.3
  • 29
    • 0035996741 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase A in Pichia pastoris: Comparison with the enzyme expressed in Saccharomyces cerevisiae
    • DOI 10.1006/prep.2001.1546
    • Li, M., Hubalek, F., Newton-Vinson, P., and Edmondson, D. E. (2002) High-level expression of human liver monoamine oxidase A in Pichia pastoris: Comparison with the enzyme expressed in Saccharomyces cerevisiae Protein Expression Purif. 24, 152-162 (Pubitemid 34805422)
    • (2002) Protein Expression and Purification , vol.24 , Issue.1 , pp. 152-162
    • Li, M.1    Hubalek, F.2    Newton-Vinson, P.3    Edmondson, D.E.4
  • 30
    • 34250811635 scopus 로고    scopus 로고
    • Variations in activity and inhibition with pH: The protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better
    • DOI 10.1007/s00702-007-0675-y, Amine Oxidases from bench to bedside
    • Jones, T. Z. E., Balsa, D., Unzeta, M., and Ramsay, R. R. (2007) Variations in activity and inhibition with pH: The protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better J. Neural Transm. 114, 707-712 (Pubitemid 46980472)
    • (2007) Journal of Neural Transmission , vol.114 , Issue.6 , pp. 707-712
    • Jones, T.Z.E.1    Balsa, D.2    Unzeta, M.3    Ramsay, R.R.4
  • 31
    • 72049099611 scopus 로고    scopus 로고
    • Oxidation of amines by flavoproteins
    • Fitzpatrick, P. F. (2010) Oxidation of amines by flavoproteins Arch. Biochem. Biophys. 493, 13-25
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 13-25
    • Fitzpatrick, P.F.1
  • 32
    • 66149173641 scopus 로고    scopus 로고
    • Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases
    • Edmondson, D. E., Binda, C., Wang, J., Upadhyay, A. K., and Mattevi, A. (2009) Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases Biochemistry 48, 4220-4230
    • (2009) Biochemistry , vol.48 , pp. 4220-4230
    • Edmondson, D.E.1    Binda, C.2    Wang, J.3    Upadhyay, A.K.4    Mattevi, A.5
  • 33
    • 34547698945 scopus 로고    scopus 로고
    • Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B
    • DOI 10.1016/j.abb.2007.05.006, PII S0003986107002524
    • Edmondson, D. E., Binda, C., and Mattevi, A. (2007) Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B Arch. Biochem. Biophys. 464, 269-276 (Pubitemid 47210935)
    • (2007) Archives of Biochemistry and Biophysics , vol.464 , Issue.2 , pp. 269-276
    • Edmondson, D.E.1    Binda, C.2    Mattevi, A.3
  • 34
    • 36048982476 scopus 로고    scopus 로고
    • Methylene blue and serotonin toxicity: Inhibition of monoamine oxidase A (MAO A) confirms a theoretical prediction
    • DOI 10.1038/sj.bjp.0707430, PII 0707430
    • Ramsay, R. R., Dunford, C., and Gillman, P. K. (2007) Methylene blue and serotonin toxicity: Inhibition of monoamine oxidase A (MAO A) confirms a theoretical prediction Br. J. Pharmacol. 152, 946-951 (Pubitemid 350100489)
    • (2007) British Journal of Pharmacology , vol.152 , Issue.6 , pp. 946-951
    • Ramsay, R.R.1    Dunford, C.2    Gillman, P.K.3


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