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Volumn 1672, Issue 1, 2004, Pages 60-66

Conformational changes in monoamine oxidase A in response to ligand binding or reduction

Author keywords

Aromatic amino acid; CD; Circular dichroism; Covalent modification; Difference spectra; Flavin reduction; MAO; Monoamine oxidase; Monoamine oxidase A

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AROMATIC AMINO ACID; CLORGYLINE; DEXAMPHETAMINE; LIGAND; PIRLINDOLE; QUERCETIN; TRYPTOPHAN; TYROSINE;

EID: 1642587783     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.02.011     Document Type: Article
Times cited : (27)

References (18)
  • 1
    • 0024534967 scopus 로고
    • Interactions of monoamine oxidase with substrates and inhibitors
    • Dostert P.L., Strolin Benedetti M., Tipton K.F. Interactions of monoamine oxidase with substrates and inhibitors. Med. Res. Rev. 9:1989;45-89.
    • (1989) Med. Res. Rev. , vol.9 , pp. 45-89
    • Dostert, P.L.1    Strolin Benedetti, M.2    Tipton, K.F.3
  • 2
    • 85063482229 scopus 로고
    • Monoamine oxidases
    • Müller F. Boca Raton, FL: CRC Press
    • Singer T.P. Monoamine oxidases. Müller F. Chemistry and Biochemistry of Flavoenzymes. vol. 2:1991;437-470 CRC Press, Boca Raton, FL.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.2 , pp. 437-470
    • Singer, T.P.1
  • 3
    • 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. 9:2002;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
  • 4
    • 0042693016 scopus 로고    scopus 로고
    • Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
    • Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A. Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc. Natl. Acad. Sci. U. S. A. 100:2003;9750-9755.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9750-9755
    • Binda, C.1    Li, M.2    Hubalek, F.3    Restelli, N.4    Edmondson, D.E.5    Mattevi, A.6
  • 5
    • 0031898408 scopus 로고    scopus 로고
    • Structural aspects of monoamine oxidase and its reversible inhibition
    • Wouters J. Structural aspects of monoamine oxidase and its reversible inhibition. Curr. Med. Chem. 5:1998;137-162.
    • (1998) Curr. Med. Chem. , vol.5 , pp. 137-162
    • Wouters, J.1
  • 6
    • 0037025299 scopus 로고    scopus 로고
    • Structure-function relationships in flavoenzyme-dependent amine oxidations: A comparison of polyamine oxidase and monoamine oxidase
    • Binda C., Mattevi A., Edmondson D.E. Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase. J. Biol. Chem. 277:2002;23973-23976.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23973-23976
    • Binda, C.1    Mattevi, A.2    Edmondson, D.E.3
  • 7
    • 0037053312 scopus 로고    scopus 로고
    • Analysis of conserved active site residues in monoamine oxidase a and B and their three-dimensional molecular modeling
    • Geha R.M., Chen K., Wouters J., Ooms F., Shih J.C. Analysis of conserved active site residues in monoamine oxidase A and B and their three-dimensional molecular modeling. J. Biol. Chem. 277:2002;17209-17216.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17209-17216
    • Geha, R.M.1    Chen, K.2    Wouters, J.3    Ooms, F.4    Shih, J.C.5
  • 8
    • 0037121460 scopus 로고    scopus 로고
    • Inhibitors alter the spectrum and redox properties of monoamine oxidase a
    • Ramsay R.R., Hunter D.J.B. Inhibitors alter the spectrum and redox properties of monoamine oxidase A. BBA-Proteins Proteomics. 1601:2002;178-184.
    • (2002) BBA-Proteins Proteomics , vol.1601 , pp. 178-184
    • Ramsay, R.R.1    Hunter, D.J.B.2
  • 9
    • 0037716398 scopus 로고    scopus 로고
    • Monoamine oxidase a inhibitory potency and flavin perturbation are influenced by different aspects of pirlindole inhibitor structure
    • Hynson R.M.G., Wouters J., Ramsay R.R. Monoamine oxidase A inhibitory potency and flavin perturbation are influenced by different aspects of pirlindole inhibitor structure. Biochem. Pharmacol. 65:2003;1867-1874.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1867-1874
    • Hynson, R.M.G.1    Wouters, J.2    Ramsay, R.R.3
  • 10
    • 0028806711 scopus 로고
    • A reversible monoamine oxidase inhibitor toloxatone - Comparison of its physicochemical properties with those of other inhibitors including brofaromine, harmine, R40519 and moclobemide
    • Moureau F., Wouters J., Depas M., Vercauteren D.P., Durant F., Ducrey F., Koenig J.J., Jarreau F.X. A reversible monoamine oxidase inhibitor toloxatone - comparison of its physicochemical properties with those of other inhibitors including brofaromine, harmine, R40519 and moclobemide. Eur. J. Med. Chem. 30:1995;823-838.
    • (1995) Eur. J. Med. Chem. , vol.30 , pp. 823-838
    • Moureau, F.1    Wouters, J.2    Depas, M.3    Vercauteren, D.P.4    Durant, F.5    Ducrey, F.6    Koenig, J.J.7    Jarreau, F.X.8
  • 11
    • 0025871857 scopus 로고
    • Kinetic mechanism of monoamine oxidase a
    • Ramsay R.R. Kinetic mechanism of monoamine oxidase A. Biochemistry. 30:1991;4624-4629.
    • (1991) Biochemistry , vol.30 , pp. 4624-4629
    • Ramsay, R.R.1
  • 12
    • 0022400583 scopus 로고
    • Purification and properties of mitochondrial monoamine-oxidase type-A from human-placenta
    • Weyler W., Salach J.I. Purification and properties of mitochondrial monoamine-oxidase type-A from human-placenta. J. Biol. Chem. 260:1985;3199-3207.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3199-3207
    • Weyler, W.1    Salach, J.I.2
  • 13
    • 0020473204 scopus 로고
    • Kinetic studies on the catalytic mechanism of liver monoamine oxidase
    • Husain M., Edmondson D.E., Singer T.P. Kinetic studies on the catalytic mechanism of liver monoamine oxidase. Biochemistry. 21:1982;595-600.
    • (1982) Biochemistry , vol.21 , pp. 595-600
    • Husain, M.1    Edmondson, D.E.2    Singer, T.P.3
  • 14
    • 0029565151 scopus 로고
    • Redox properties of the flavin co-factor of monoamine oxidases a and B and their relationship to the kinetic mechanism
    • Ramsay R.R., Sablin S.O., Singer T.P. Redox properties of the flavin co-factor of monoamine oxidases A and B and their relationship to the kinetic mechanism. Prog. Brain Res. 106:1995;33-39.
    • (1995) Prog. Brain Res. , vol.106 , pp. 33-39
    • Ramsay, R.R.1    Sablin, S.O.2    Singer, T.P.3
  • 15
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • Strickland E.H. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 2:1974;113-175.
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 16
    • 0018339835 scopus 로고
    • The interpretation of near-ultraviolet circular dichroism
    • Kahn P.C. The interpretation of near-ultraviolet circular dichroism. Methods Enzymol. 61:1979;339-376.
    • (1979) Methods Enzymol. , vol.61 , pp. 339-376
    • Kahn, P.C.1
  • 18
    • 0014314486 scopus 로고
    • Some observations upon a new inhibitor of monoamine oxidase in brain tissue
    • Johnston J.P. Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem. Pharmacol. 17:1968;1285-1297.
    • (1968) Biochem. Pharmacol. , vol.17 , pp. 1285-1297
    • Johnston, J.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.