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Volumn 159, Issue 2, 2011, Pages 78-83

Catalytic and inhibitor binding properties of zebrafish monoamine oxidase (zMAO): Comparisons with human MAO A and MAO B

Author keywords

Inhibitor binding; Monoamine oxidase; Substrate specificity; Zebrafish

Indexed keywords

1,4 DIPHENYL 1,3 BUTADIENE; 1,4 DIPHENYL 2 BUTENE; 8 (3 CHLOROSTYRYL)CAFFEINE; AMINE OXIDASE (FLAVIN CONTAINING); AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; BENZYLAMINE DERIVATIVE; DEXAMPHETAMINE; DOPAMINE; FARNESOL; HARMAN; METHYLENE BLUE; MONOAMINE OXIDASE A INHIBITOR; MONOAMINE OXIDASE B INHIBITOR; PIRLINDOLE; SAFINAMIDE; SEROTONIN; TETRINDOLE; TYRAMINE; UNCLASSIFIED DRUG;

EID: 79953314929     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2011.02.002     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 79953316001 scopus 로고
    • A new antidepressant tetrindole II. Experimental investigation of tetrindole tolerability
    • Andreeva N.I., Golovina S.M., Mashkovskii M.D. A new antidepressant tetrindole II. Experimental investigation of tetrindole tolerability. J. Med. Pharm. Chem. 1992, 26:11-12.
    • (1992) J. Med. Pharm. Chem. , vol.26 , pp. 11-12
    • Andreeva, N.I.1    Golovina, S.M.2    Mashkovskii, M.D.3
  • 2
    • 33748464391 scopus 로고    scopus 로고
    • Distinct structure and activity of monoamine oxidase in the brain of zebrafish (Danio rerio)
    • Anichtchik O., Sallinen V., Peitsaro N., Panula P. Distinct structure and activity of monoamine oxidase in the brain of zebrafish (Danio rerio). J. Comp. Neurol. 2006, 498:593-610.
    • (2006) J. Comp. Neurol. , vol.498 , pp. 593-610
    • Anichtchik, O.1    Sallinen, V.2    Peitsaro, N.3    Panula, P.4
  • 3
    • 76749114230 scopus 로고    scopus 로고
    • Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: purification and comparison with human MAO A and MAO B
    • Arslan B.K., Edmondson D.E. Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: purification and comparison with human MAO A and MAO B. Protein Expr. Purif. 2010, 70:290-297.
    • (2010) Protein Expr. Purif. , vol.70 , pp. 290-297
    • Arslan, B.K.1    Edmondson, D.E.2
  • 5
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    • Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A. Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat. Struct. Biol. 2002, 9:22-26.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubalek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 6
    • 0042693016 scopus 로고    scopus 로고
    • Insights into the mode of inhibiton of human mitochondrial monoamine oxidase B from high-resolution crystal structure
    • USA
    • Binda C., Li M., Hubalek F., Restelli B., Edmondson D.E., Mattevi A. Insights into the mode of inhibiton of human mitochondrial monoamine oxidase B from high-resolution crystal structure. Proc. Natl Acad. Sci. 2003, 100:9750-9755. USA.
    • (2003) Proc. Natl Acad. Sci. , vol.100 , pp. 9750-9755
    • Binda, C.1    Li, M.2    Hubalek, F.3    Restelli, B.4    Edmondson, D.E.5    Mattevi, A.6
  • 7
    • 36148955400 scopus 로고    scopus 로고
    • Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs
    • Binda C., Wang J., Pisani L., Caccia C., Carotti A., Salvati P., Edmondson D.E., Mattevi A. Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs. J. Med. Chem. 2007, 50:5848-5852.
    • (2007) J. Med. Chem. , vol.50 , pp. 5848-5852
    • Binda, C.1    Wang, J.2    Pisani, L.3    Caccia, C.4    Carotti, A.5    Salvati, P.6    Edmondson, D.E.7    Mattevi, A.8
  • 8
    • 20544433165 scopus 로고
    • Van der Waals volumes and radii
    • Bondi A. Van der Waals volumes and radii. J. Phys. Chem. 1964, 68:441-451.
    • (1964) J. Phys. Chem. , vol.68 , pp. 441-451
    • Bondi, A.1
  • 9
    • 0028559727 scopus 로고
    • Cloning of a novel monoamine oxidase cDNA from trout liver
    • Chen K., Wu H.F., Grimsby J., Shih J.C. Cloning of a novel monoamine oxidase cDNA from trout liver. Mol. Pharmacol. 1994, 46:1226-1233.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 1226-1233
    • Chen, K.1    Wu, H.F.2    Grimsby, J.3    Shih, J.C.4
  • 10
    • 24644437716 scopus 로고    scopus 로고
    • Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B
    • USA
    • De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., Mattevi A. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc. Natl Acad. Sci. 2005, 102:12684-12689. USA.
    • (2005) Proc. Natl Acad. Sci. , vol.102 , pp. 12684-12689
    • De Colibus, L.1    Li, M.2    Binda, C.3    Lustig, A.4    Edmondson, D.E.5    Mattevi, A.6
  • 11
    • 34547698945 scopus 로고    scopus 로고
    • Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B
    • Edmondson D.E., Binda C., Mattevi A. Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B. Arch. Biochem. Biophys. 2007, 464:269-276.
    • (2007) Arch. Biochem. Biophys. , vol.464 , pp. 269-276
    • Edmondson, D.E.1    Binda, C.2    Mattevi, A.3
  • 12
    • 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., Mattevi A. Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases. Biochemistry 2009, 48:4230-4430.
    • (2009) Biochemistry , vol.48 , pp. 4230-4430
    • Edmondson, D.E.1    Binda, C.2    Wang, J.3    Upadhyay, A.4    Mattevi, A.5
  • 13
    • 0033578302 scopus 로고    scopus 로고
    • Cation-Π Interactions in Structural Biology
    • USA
    • Gallivan J.P., Dougherty D.A. Cation-Π Interactions in Structural Biology. Proc. Natl. Acad. Sci. 1999, 96:9459-9464. USA.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 9459-9464
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 14
    • 0019191223 scopus 로고
    • P-methoxyamphetamine, a potent reversible inhibitor of type-A monoamine oxidase in vitro and in vivo
    • Green A.L., El Hait M.A. p-methoxyamphetamine, a potent reversible inhibitor of type-A monoamine oxidase in vitro and in vivo. J. Pharm. Pharmacol. 1980, 32:262-266.
    • (1980) J. Pharm. Pharmacol. , vol.32 , pp. 262-266
    • Green, A.L.1    El Hait, M.A.2
  • 16
    • 18144423424 scopus 로고    scopus 로고
    • Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors
    • Hubálek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N., Edmondson D.E. Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors. J. Biol. Chem. 2005, 280:15761-15766.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15761-15766
    • Hubálek, F.1    Binda, C.2    Khalil, A.3    Li, M.4    Mattevi, A.5    Castagnoli, N.6    Edmondson, D.E.7
  • 17
    • 0001222320 scopus 로고
    • Calculation of substrate dissociation-constants from steady-state isotope effects in enzyme-catalyzed reactions
    • Klinman J.P., Matthews R.G. Calculation of substrate dissociation-constants from steady-state isotope effects in enzyme-catalyzed reactions. J. Am. Chem. Soc. 1985, 107:1058-1060.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 1058-1060
    • Klinman, J.P.1    Matthews, R.G.2
  • 19
    • 79953320027 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Emory University.
    • Li, M. 2006. Ph.D. Dissertation, Emory University.
    • (2006)
    • Li, M.1
  • 20
    • 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
    • Li M., Hubálek F., Newton-Vinson P., Edmondson D.E. High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr. Purif. 2002, 24:152-162.
    • (2002) Protein Expr. Purif. , vol.24 , pp. 152-162
    • Li, M.1    Hubálek, F.2    Newton-Vinson, P.3    Edmondson, D.E.4
  • 21
    • 0014430090 scopus 로고
    • Human liver mitochondrial monoamine oxidase I. Kinetic studies of model interactions
    • McEwen C.M., Sasaki G., Jones D.C. Human liver mitochondrial monoamine oxidase I. Kinetic studies of model interactions. J. Biol. Chem. 1968, 243:5217-5225.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5217-5225
    • McEwen, C.M.1    Sasaki, G.2    Jones, D.C.3
  • 22
    • 0014594785 scopus 로고
    • Human liver mitochondrial monoamine oxidase II. Determinants of substrate and inhibitor specificities
    • McEwen C.M., Sasaki G., Jones D.C. Human liver mitochondrial monoamine oxidase II. Determinants of substrate and inhibitor specificities. Biochemistry 1969, 8:3952-3962.
    • (1969) Biochemistry , vol.8 , pp. 3952-3962
    • McEwen, C.M.1    Sasaki, G.2    Jones, D.C.3
  • 23
    • 79953302196 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Emory University.
    • Milczek, E.M. 2010 Ph.D. Dissertation, Emory University.
    • (2010)
    • Milczek, E.M.1
  • 24
    • 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., Edmondson D.E. Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A. Biochemistry 1999, 38:13670-13683.
    • (1999) Biochemistry , vol.38 , pp. 13670-13683
    • Miller, J.R.1    Edmondson, D.E.2
  • 25
    • 0014454095 scopus 로고
    • Kinetics of reversible inhibition of enzyme catalyzed reactions by tight binding inhibitors
    • Morrison J.F. Kinetics of reversible inhibition of enzyme catalyzed reactions by tight binding inhibitors. Biochim. Biophys. Acta 1968, 185:269-286.
    • (1968) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 26
    • 0034642217 scopus 로고    scopus 로고
    • Structure-activity relations in the oxidation of phenethylamine analogues by recombinant human liver monoamine oxidase A
    • Nandigama R.K., Edmondson D.E. Structure-activity relations in the oxidation of phenethylamine analogues by recombinant human liver monoamine oxidase A. Biochemistry 2000, 39:15258-15265.
    • (2000) Biochemistry , vol.39 , pp. 15258-15265
    • Nandigama, R.K.1    Edmondson, D.E.2
  • 27
    • 0033773601 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase B in Pichia pastoris
    • Newton-Vinson P., Hubálek F., Edmondson D.E. High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr. Purif. 2000, 20:334-345.
    • (2000) Protein Expr. Purif. , vol.20 , pp. 334-345
    • Newton-Vinson, P.1    Hubálek, F.2    Edmondson, D.E.3
  • 28
    • 0022262460 scopus 로고
    • Human brain monoamine oxidase type B: mechanism of deamination as probed by steady state methods
    • Pearce L.B., Roth J.A. Human brain monoamine oxidase type B: mechanism of deamination as probed by steady state methods. Biochemistry 1985, 24:1821-1826.
    • (1985) Biochemistry , vol.24 , pp. 1821-1826
    • Pearce, L.B.1    Roth, J.A.2
  • 29
    • 36048982476 scopus 로고    scopus 로고
    • Methylene blue and serotonin toxicity: inhibition of monoamine oxidase A (MAO A) confirms a theoretical prediction
    • Ramsay R.R., Dunford C., Gillman P.K. Methylene blue and serotonin toxicity: inhibition of monoamine oxidase A (MAO A) confirms a theoretical prediction. Br. J. Pharmacol. 2007, 152:946-951.
    • (2007) Br. J. Pharmacol. , vol.152 , pp. 946-951
    • Ramsay, R.R.1    Dunford, C.2    Gillman, P.K.3
  • 33
    • 11144299596 scopus 로고    scopus 로고
    • Molecular characterization of monoamine oxidase in zebrafish (Danio rerio)
    • Setini A., Pierucci F., Senatori O., Nicotra A. Molecular characterization of monoamine oxidase in zebrafish (Danio rerio). Comp. Biochem. Physiol. B 2005, 140:153-161.
    • (2005) Comp. Biochem. Physiol. B , vol.140 , pp. 153-161
    • Setini, A.1    Pierucci, F.2    Senatori, O.3    Nicotra, A.4
  • 34
    • 44449117421 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase a at 2.2-Å resolution: the control of opening the entry for substrates/inhibitors
    • USA
    • Son S.-Y., Ma Jichun, Youhei Kondou, Masato Yoshimura, Eiki Yamashita, Tomitake Tsukihara Structure of human monoamine oxidase a at 2.2-Å resolution: the control of opening the entry for substrates/inhibitors. Proc. Natl Acad. Sci. 2008, 105:5739-5744. USA.
    • (2008) Proc. Natl Acad. Sci. , vol.105 , pp. 5739-5744
    • Son, S.-Y.1    Ma, J.2    Youhei, K.3    Masato, Y.4    Eiki, Y.5    Tomitake, T.6
  • 35
    • 4444268426 scopus 로고    scopus 로고
    • Monoamine oxidase inhibitors, their structural analogues, and neuroprotection
    • Sowa B.N., Holt A., Todd K.G., Baker G.B. Monoamine oxidase inhibitors, their structural analogues, and neuroprotection. Indian J. Exp. Biol. 2004, 42:851-857.
    • (2004) Indian J. Exp. Biol. , vol.42 , pp. 851-857
    • Sowa, B.N.1    Holt, A.2    Todd, K.G.3    Baker, G.B.4
  • 36
    • 42749094798 scopus 로고    scopus 로고
    • Characterization of detergent purified recombinant rat liver monoamine oxidase B expressed in Pichia pastoris
    • Upadhyay A.K., Edmondson D.E. Characterization of detergent purified recombinant rat liver monoamine oxidase B expressed in Pichia pastoris. Protein Expr. Purif. 2008, 59:349-356.
    • (2008) Protein Expr. Purif. , vol.59 , pp. 349-356
    • Upadhyay, A.K.1    Edmondson, D.E.2
  • 37
    • 17444368018 scopus 로고    scopus 로고
    • Mutation of surface cysteine 374 to alanine in monoamine oxidase A alters substrate turnover and inactivation by cyclopropylamines
    • Vintén A.P.B., Price N.T., Silverman R.B., Ramsay R.R. Mutation of surface cysteine 374 to alanine in monoamine oxidase A alters substrate turnover and inactivation by cyclopropylamines. Bioorg. Med. Chem. 2005, 13:3487-3495.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3487-3495
    • Vintén, A.P.B.1    Price, N.T.2    Silverman, R.B.3    Ramsay, R.R.4
  • 38
    • 0028278443 scopus 로고
    • Structure-activity relationships in the oxidation of benzylamine analogs by bovine liver mitochondrial monoamine oxidase B
    • Walker M.C., Edmondson D.E. Structure-activity relationships in the oxidation of benzylamine analogs by bovine liver mitochondrial monoamine oxidase B. Biochemistry 1994, 33:7088-7098.
    • (1994) Biochemistry , vol.33 , pp. 7088-7098
    • Walker, M.C.1    Edmondson, D.E.2
  • 39
    • 76749104256 scopus 로고    scopus 로고
    • High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: comparisons to human MAO A
    • Wang J., Edmondson D.E. High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: comparisons to human MAO A. Protein Expr. Purif. 2009, 70:211-217.
    • (2009) Protein Expr. Purif. , vol.70 , pp. 211-217
    • Wang, J.1    Edmondson, D.E.2
  • 40
    • 68749107344 scopus 로고    scopus 로고
    • Mutagenic probes of the role of serine 209 on the cavity shaping loop of human monoamine oxidase A
    • Wang J., Harris J., Mousseau D.D., Edmondson D.E. Mutagenic probes of the role of serine 209 on the cavity shaping loop of human monoamine oxidase A. FEBS J. 2009, 276:4569-4581.
    • (2009) FEBS J. , vol.276 , pp. 4569-4581
    • Wang, J.1    Harris, J.2    Mousseau, D.D.3    Edmondson, D.E.4
  • 41


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