메뉴 건너뛰기




Volumn 44, Issue 18, 2005, Pages 7079-7084

Mechanistic studies of mouse polyamine oxidase with N1,N12-bisethylspermine as a substrate

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; LIVING SYSTEMS STUDIES; NITROGEN; OXIDATION; OXYGEN; POLYMERS; SUBSTRATES;

EID: 18244400100     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050347k     Document Type: Article
Times cited : (24)

References (35)
  • 2
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton, L. J., and Pegg, A. E. (1995) Polyamines as targets for therapeutic intervention, Annu. Rev. Pharmacol. Toxicol. 35, 55-91.
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 3
    • 0345688128 scopus 로고    scopus 로고
    • A perspective of polyamine metabolism
    • Wallace, H. M., Fraser, A. V., and Hughes, A. (2003) A perspective of polyamine metabolism, Biochem. J. 376, 1-14.
    • (2003) Biochem. J. , vol.376 , pp. 1-14
    • Wallace, H.M.1    Fraser, A.V.2    Hughes, A.3
  • 4
  • 6
    • 0035804314 scopus 로고    scopus 로고
    • Terminally alkylated polyamine analogues as chemotherapeutic agents
    • Casero, R. A., Jr., and Woster, P. M. (2001) Terminally alkylated polyamine analogues as chemotherapeutic agents, J. Med. Chem. 44, 1-26.
    • (2001) J. Med. Chem. , vol.44 , pp. 1-26
    • Casero Jr., R.A.1    Woster, P.M.2
  • 7
    • 0036098409 scopus 로고    scopus 로고
    • Detoxification of the polyamine analogue N1-ethyl-N11-[(cycloheptyl) methy]-4,8-diazaundecane (CHENSpm) by polyamine oxidase
    • Lawson, K. R., Marek, S., Linehan, J. A., Woster, P. M., Casero, R. A., Jr., Payne, C. M., and Gerner, E. W. (2002) Detoxification of the polyamine analogue N1-ethyl-N11-[(cycloheptyl)methy]-4,8-diazaundecane (CHENSpm) by polyamine oxidase, Clin. Cancer Res. 8, 1241-1247.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1241-1247
    • Lawson, K.R.1    Marek, S.2    Linehan, J.A.3    Woster, P.M.4    Casero Jr., R.A.5    Payne, C.M.6    Gerner, E.W.7
  • 8
    • 0346734280 scopus 로고    scopus 로고
    • A Phase II study of the polyamine analog N1,N11-diethylnorspermine (DENSpm) daily for five days every 21 days in patients with previously treated metastatic breast cancer
    • Wolff, A. C., Armstrong, D. K., Fetting, J. H., Carducci, M. K., Riley, C. D., Bender, J. F., Casero, R. A., Jr., and Davidson, N. E. (2003) A Phase II study of the polyamine analog N1,N11-diethylnorspermine (DENSpm) daily for five days every 21 days in patients with previously treated metastatic breast cancer, Clin. Cancer Res. 9, 5922-5928.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 5922-5928
    • Wolff, A.C.1    Armstrong, D.K.2    Fetting, J.H.3    Carducci, M.K.4    Riley, C.D.5    Bender, J.F.6    Casero Jr., R.A.7    Davidson, N.E.8
  • 9
    • 0037396450 scopus 로고    scopus 로고
    • The biological activities of new polyamine derivatives as potential therapeutic agents
    • Lin, P. K. T., Dance, A. M., Bestwick, C., and Milne, L. (2003) The biological activities of new polyamine derivatives as potential therapeutic agents, Biochem. Soc. Trans. 31, 407-410.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 407-410
    • Lin, P.K.T.1    Dance, A.M.2    Bestwick, C.3    Milne, L.4
  • 10
    • 0038419788 scopus 로고    scopus 로고
    • Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase
    • Wu, T., Yankovskaya, V., and McIntire, W. S. (2003) Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase, J. Biol. Chem. 278, 20514-20525.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20514-20525
    • Wu, T.1    Yankovskaya, V.2    McIntire, W.S.3
  • 11
    • 0037442525 scopus 로고    scopus 로고
    • Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion
    • Vujcic, S., Liang, P., Diegelman, P., Kramer, D. L., and Porter, C. W. (2003) Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion, Biochem. J. 370, 19-28.
    • (2003) Biochem. J. , vol.370 , pp. 19-28
    • Vujcic, S.1    Liang, P.2    Diegelman, P.3    Kramer, D.L.4    Porter, C.W.5
  • 12
    • 0035878846 scopus 로고    scopus 로고
    • Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
    • Wang, Y., Devereux, W., Woster, P. M., Stewart, T. M., Hacker, A., and Casero, R. A., Jr. (2001) Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure, Cancer Res. 61, 5370-5373.
    • (2001) Cancer Res. , vol.61 , pp. 5370-5373
    • Wang, Y.1    Devereux, W.2    Woster, P.M.3    Stewart, T.M.4    Hacker, A.5    Casero Jr., R.A.6
  • 13
    • 0035814939 scopus 로고    scopus 로고
    • Structural bases for inhibitor binding and catalysis in polyamine oxidase
    • Binda, C., Angelini, R., Federico, R., Ascenzi, P., and Mattevi, A. (2001) Structural bases for inhibitor binding and catalysis in polyamine oxidase, Biochemistry 40, 2766-2776.
    • (2001) Biochemistry , vol.40 , pp. 2766-2776
    • Binda, C.1    Angelini, R.2    Federico, R.3    Ascenzi, P.4    Mattevi, A.5
  • 14
    • 34548519907 scopus 로고    scopus 로고
    • A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • Binda, C., Coda, A., Angelini, R., Federico, R., Ascenzi, P., and Mattevi, A. (1999) A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase, Structure 7, 265-276.
    • (1999) Structure , vol.7 , pp. 265-276
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 16
    • 0035808250 scopus 로고    scopus 로고
    • FAD-containing polyamine oxidases: A timely challenge for researchers in biochemistry and physiology of plants
    • Sebela, M., Radová, A., Angelini, R., Tavladoraki, P., Frébort, I., and Pec, P. (2001) FAD-containing polyamine oxidases: A timely challenge for researchers in biochemistry and physiology of plants, Plant Sci. 160, 197-207.
    • (2001) Plant Sci. , vol.160 , pp. 197-207
    • Sebela, M.1    Radová, A.2    Angelini, R.3    Tavladoraki, P.4    Frébort, I.5    Pec, P.6
  • 17
    • 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
  • 18
    • 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., and Edmondson, D. E. (2002) Structure-function relationships in flavoenzyme dependent amine oxidations. A comparison of polyamine oxidase and monoamine oxidase, J. Biol. Chem. 277, 23973-23976.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23973-23976
    • Binda, C.1    Mattevi, A.2    Edmondson, D.E.3
  • 19
    • 0001319451 scopus 로고
    • Radical ideas about monoamine oxidase
    • Silverman, R. B. (1995) Radical ideas about monoamine oxidase, Acc. Chem. Res. 28, 335-342.
    • (1995) Acc. Chem. Res. , vol.28 , pp. 335-342
    • Silverman, R.B.1
  • 21
    • 0037432631 scopus 로고    scopus 로고
    • Yeast Fms1 is a FAD-utilizing polyamine oxidase
    • Landry, J., and Sternglanz, R. (2003) Yeast Fms1 is a FAD-utilizing polyamine oxidase, Biochem. Biophys. Res. Commun. 303, 771-776.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 771-776
    • Landry, J.1    Sternglanz, R.2
  • 22
    • 0002458523 scopus 로고
    • Mechanisms of flavoprotein catalysis
    • Singer, T. P., Ed. John Wiley and Sons, New York
    • Palmer, G., and Massey, V. (1968) Mechanisms of flavoprotein catalysis, in Biological Oxidation (Singer, T. P., Ed.) pp 263-300, John Wiley and Sons, New York.
    • (1968) Biological Oxidation , pp. 263-300
    • Palmer, G.1    Massey, V.2
  • 23
    • 77956923521 scopus 로고
    • Flavoprotein oxidases
    • Boyer, P., Ed. Academic Press, New York
    • Bright, H. J., and Porter, D. J. T. (1975) Flavoprotein oxidases, in The Enzymes, 3rd ed. (Boyer, P., Ed.) Vol. XII, pp 421-505, Academic Press, New York.
    • (1975) The Enzymes, 3rd Ed. , vol.12 , pp. 421-505
    • Bright, H.J.1    Porter, D.J.T.2
  • 24
    • 0020453403 scopus 로고
    • The use of pH studies to determine chemical mechanisms of enzyme-catalyzed reactions
    • Cleland, W. W. (1982) The use of pH studies to determine chemical mechanisms of enzyme-catalyzed reactions, Methods Enzymol. 87, 390-405.
    • (1982) Methods Enzymol. , vol.87 , pp. 390-405
    • Cleland, W.W.1
  • 26
    • 4143049044 scopus 로고    scopus 로고
    • Inhibitors of polyamine metabolism: Review article
    • Wallace, H. M., and Fraser, A. V. (2004) Inhibitors of polyamine metabolism: Review article, Amino Acids 26, 353-365.
    • (2004) Amino Acids , vol.26 , pp. 353-365
    • Wallace, H.M.1    Fraser, A.V.2
  • 27
    • 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., and Mattevi, A. (2002) Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders, Nat. Struct. Biol. 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
  • 29
    • 0001409925 scopus 로고
    • Role of charge-transfer interactions in flavoprotein catalysis
    • Massey, V., and Ghisla, S. (1974) Role of charge-transfer interactions in flavoprotein catalysis, Ann. N.Y. Acad. 227, 446-465.
    • (1974) Ann. N.Y. Acad. , vol.227 , pp. 446-465
    • Massey, V.1    Ghisla, S.2
  • 31
    • 0002869575 scopus 로고
    • On the reaction of reduced flavins with molecular oxygen
    • King, T. E., Mason, H. S., and Morrison, M., Eds. University Park Press, Baltimore
    • Massey, V., Palmer, G., and Ballou, D. (1973) On the reaction of reduced flavins with molecular oxygen, in Oxidases and related redox systems (King, T. E., Mason, H. S., and Morrison, M., Eds.) pp 25-49, University Park Press, Baltimore.
    • (1973) Oxidases and Related Redox Systems , pp. 25-49
    • Massey, V.1    Palmer, G.2    Ballou, D.3
  • 33
    • 0001826757 scopus 로고
    • Free flavins: Syntheses, chemical and physical properties
    • Muller, F., Ed. CRC Press, Boca Raton, FL
    • Muller, F. (1991) Free flavins: Syntheses, chemical and physical properties, in Chemistry and Biochemistry of Flavoenzymes (Muller, F., Ed.) Vol. I, pp 1-71, CRC Press, Boca Raton, FL.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.1 , pp. 1-71
    • Muller, F.1
  • 34
    • 0028877810 scopus 로고
    • Mechanistic probes of monoamine oxidase B catalysis: Rapid-scan stopped flow and magnetic field independence of the reductive half-reaction
    • Miller, J. R., Edmondson, D. E., and Grissom, C. B. (1995) Mechanistic probes of monoamine oxidase B catalysis: Rapid-scan stopped flow and magnetic field independence of the reductive half-reaction, J. Am. Chem. Soc. 117, 7830-7831.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7830-7831
    • Miller, J.R.1    Edmondson, D.E.2    Grissom, C.B.3
  • 35
    • 0035846625 scopus 로고    scopus 로고
    • Loss of serotonin oxidatin as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAOA
    • Nandigama, R. K., Miller, J. R., and Edmondson, D. (2001) Loss of serotonin oxidatin as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAOA, Biochemistry 40, 14839-14846.
    • (2001) Biochemistry , vol.40 , pp. 14839-14846
    • Nandigama, R.K.1    Miller, J.R.2    Edmondson, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.