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Volumn 48, Issue 7, 2009, Pages 1508-1516

pH dependence of a mammalian polyamine oxidase: Insights into substrate specificity and the role of lysine 315

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; ACTIVE SITES; AMINE OXIDATIONS; MONOAMINE OXIDASE; MUTANT PROTEINS; PH DEPENDENCES; PH DEPENDENTS; POLYAMINE; POLYAMINE OXIDASE; POSITIVELY CHARGED; PROTONATION STATE; SPERMIDINE; SUBSTRATE OXIDATIONS; SUBSTRATE SPECIFICITIES;

EID: 61749094173     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802227m     Document Type: Article
Times cited : (42)

References (49)
  • 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
    • 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
  • 4
    • 32944467076 scopus 로고    scopus 로고
    • Mammalian polyamine catabolism: A therapeutic target, a pathological problem, or both?
    • Wang, Y., and Casero, R. A., Jr. (2006) Mammalian polyamine catabolism: A therapeutic target, a pathological problem, or both? J. Biochem. 139, 17-25.
    • (2006) J. Biochem , vol.139 , pp. 17-25
    • Wang, Y.1    Casero Jr., R.A.2
  • 5
    • 0036846756 scopus 로고    scopus 로고
    • Identification and characterization of a novel flavincontaining spermine oxidase of mammalian cell origin
    • VujciC., S., Diegelman, P., Bacchi, C. J., Kramer, D. L., and Porter, C. W. (2002) Identification and characterization of a novel flavincontaining spermine oxidase of mammalian cell origin. Biochem. J. 367, 665-675.
    • (2002) Biochem. J , vol.367 , pp. 665-675
    • VujciC, S.1    Diegelman, P.2    Bacchi, C.J.3    Kramer, D.L.4    Porter, C.W.5
  • 7
    • 0038136943 scopus 로고    scopus 로고
    • Heterologous expression and characterization of mouse spermine oxidase
    • Cervelli, M., Polticelli, F., Federico, R., and Mariottini, P. (2003) Heterologous expression and characterization of mouse spermine oxidase. J. Biol. Chem. 278, 5271-5276.
    • (2003) J. Biol. Chem , vol.278 , pp. 5271-5276
    • Cervelli, M.1    Polticelli, F.2    Federico, R.3    Mariottini, P.4
  • 9
    • 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
  • 10
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 77956923521 scopus 로고
    • Flavoprotein oxidases
    • Boyer, P, Ed, 3rd ed, Academic Press, New York
    • Bright, H. J., and Porter, D. J. T. (1975) Flavoprotein oxidases. In The Enzymes (Boyer, P., Ed.) 3rd ed., Vol. XII, pp 421-505, Academic Press, New York.
    • (1975) The Enzymes , vol.12 , pp. 421-505
    • Bright, H.J.1    Porter, D.J.T.2
  • 15
    • 0034860788 scopus 로고    scopus 로고
    • Substrate dehydrogenation by flavoproteins
    • Fitzpatrick, P. F. (2001) Substrate dehydrogenation by flavoproteins. Acc. Chem. Res. 34, 299-307.
    • (2001) Acc. Chem. Res , vol.34 , pp. 299-307
    • Fitzpatrick, P.F.1
  • 16
    • 38349078616 scopus 로고    scopus 로고
    • Insights into the mechanisms of flavoprotein oxidases from kinetic isotope effects
    • Fitzpatrick, P. F. (2007) Insights into the mechanisms of flavoprotein oxidases from kinetic isotope effects. J. Labelled Compd. Radiopharm. 50, 1016-1025.
    • (2007) J. Labelled Compd. Radiopharm , vol.50 , pp. 1016-1025
    • Fitzpatrick, P.F.1
  • 17
    • 11144270176 scopus 로고    scopus 로고
    • Chemical aspects of amine oxidation by flavoprotein enzymes
    • Scrutton, N. S. (2004) Chemical aspects of amine oxidation by flavoprotein enzymes. Nat. Prod. Rep. 21, 722-730.
    • (2004) Nat. Prod. Rep , vol.21 , pp. 722-730
    • Scrutton, N.S.1
  • 18
    • 33646576258 scopus 로고    scopus 로고
    • Spectral and kinetic characterization of the Michaelis charge transfer complex in monomeric sarcosine oxidase
    • Zhao, G., and Jorns, M. S. (2006) Spectral and kinetic characterization of the Michaelis charge transfer complex in monomeric sarcosine oxidase. Biochemistry 45, 5985-5992.
    • (2006) Biochemistry , vol.45 , pp. 5985-5992
    • Zhao, G.1    Jorns, M.S.2
  • 19
    • 34547698945 scopus 로고    scopus 로고
    • Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B
    • 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. 264, 269-276.
    • (2007) Arch. Biochem. Biophys , vol.264 , pp. 269-276
    • Edmondson, D.E.1    Binda, C.2    Mattevi, A.3
  • 20
    • 0034722962 scopus 로고    scopus 로고
    • Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase
    • Kurtz, K. A., Rishavy, M. A., Cleland, W. W., and Fitzpatrick, P. F. (2000) Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase. J. Am. Chem. Soc. 122, 12896-12897.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 12896-12897
    • Kurtz, K.A.1    Rishavy, M.A.2    Cleland, W.W.3    Fitzpatrick, P.F.4
  • 21
    • 0035719831 scopus 로고    scopus 로고
    • pH and kinetic isotope effects in D-amino acid oxidase catalysis: Evidence for a concerted mechanism in substrate dehydrogenation via hydride transfer
    • Harris, C. M., Pollegioni, L., and Ghisla, S. (2001) pH and kinetic isotope effects in D-amino acid oxidase catalysis: Evidence for a concerted mechanism in substrate dehydrogenation via hydride transfer. Eur. J. Biochem. 268, 5504-5520.
    • (2001) Eur. J. Biochem , vol.268 , pp. 5504-5520
    • Harris, C.M.1    Pollegioni, L.2    Ghisla, S.3
  • 22
    • 0037031276 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: Role of histidine 269 in catalysis
    • Zhao, G., Song, H., Chen, Z., Mathews, S., and Jorns, M. S. (2002) Monomeric sarcosine oxidase: Role of histidine 269 in catalysis. Biochemistry 41, 9751-9764.
    • (2002) Biochemistry , vol.41 , pp. 9751-9764
    • Zhao, G.1    Song, H.2    Chen, Z.3    Mathews, S.4    Jorns, M.S.5
  • 23
    • 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
    • Jones, T. Z., 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.
    • (2007) J. Neural Transm , vol.114 , pp. 707-712
    • Jones, T.Z.1    Balsa, D.2    Unzeta, M.3    Ramsay, R.R.4
  • 24
    • 0034663814 scopus 로고    scopus 로고
    • The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
    • Pawelek, P. D., Cheah, J., Coulombe, R., Macheroux, P., Ghisla, S., and Vrielink, A. (2000) The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. EMBO J. 19, 4204-4215.
    • (2000) EMBO J , vol.19 , pp. 4204-4215
    • Pawelek, P.D.1    Cheah, J.2    Coulombe, R.3    Macheroux, P.4    Ghisla, S.5    Vrielink, A.6
  • 25
    • 0001390566 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: Structure of a covalently flavinylated amine oxidizing enzyme
    • Trickey, P., Wagner, M. A., Jorns, M. S., and Mathews, F. S. (1999) Monomeric sarcosine oxidase: Structure of a covalently flavinylated amine oxidizing enzyme. Structure 7, 331-345.
    • (1999) Structure , vol.7 , pp. 331-345
    • Trickey, P.1    Wagner, M.A.2    Jorns, M.S.3    Mathews, F.S.4
  • 26
    • 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
  • 27
    • 17444422874 scopus 로고    scopus 로고
    • Crystal structures of Fms1 and its complex with spermine reveal substrate specificity
    • Huang, Q., Liu, Q., and Hao, Q. (2005) Crystal structures of Fms1 and its complex with spermine reveal substrate specificity. J. Mol. Biol. 348, 951-959.
    • (2005) J. Mol. Biol , vol.348 , pp. 951-959
    • Huang, Q.1    Liu, Q.2    Hao, Q.3
  • 28
    • 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
  • 30
    • 1842474296 scopus 로고    scopus 로고
    • Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors
    • 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.
    • (2004) J. Mol. Biol , vol.338 , pp. 103-114
    • Ma, J.1    Yoshimura, M.2    Yamashita, E.3    Nakagawa, A.4    Ito, A.5    Tsukihara, T.6
  • 31
    • 34548782681 scopus 로고    scopus 로고
    • The synthesis of deuterium-labeled spermine, N1-acetylspermine and N1-acetyl-spermidine
    • Gawandi, V., and Fitzpatrick, P. F. (2007) The synthesis of deuterium-labeled spermine, N1-acetylspermine and N1-acetyl-spermidine. J. Labelled Compd. Radiopharm. 50, 666-670.
    • (2007) J. Labelled Compd. Radiopharm , vol.50 , pp. 666-670
    • Gawandi, V.1    Fitzpatrick, P.F.2
  • 32
    • 18244400100 scopus 로고    scopus 로고
    • Mechanistic studies of mouse polyamine oxidase with N1,N12-bisethylspermine as a substrate
    • Royo, M., and Fitzpatrick, P. F. (2005) Mechanistic studies of mouse polyamine oxidase with N1,N12-bisethylspermine as a substrate. Biochemistry 44, 7079-7084.
    • (2005) Biochemistry , vol.44 , pp. 7079-7084
    • Royo, M.1    Fitzpatrick, P.F.2
  • 34
    • 0011786864 scopus 로고
    • Prediction of the strengths of organic bases
    • Clark, J., and Perrin, D. D. (1964) Prediction of the strengths of organic bases. Q. ReV. Chem. Soc. 18, 295-320.
    • (1964) Q. ReV. Chem. Soc , vol.18 , pp. 295-320
    • Clark, J.1    Perrin, D.D.2
  • 35
    • 0028869173 scopus 로고
    • Nuclear magnetic resonance as a tool for determining protonation constants of natural polyprotic bases in solution
    • Frassineti, C., Ghelli, S., Gans, P., Sabatini, A., Moruzzi, M. S., and Vacca, A. (1995) Nuclear magnetic resonance as a tool for determining protonation constants of natural polyprotic bases in solution. Anal. Biochem. 231, 374-382.
    • (1995) Anal. Biochem , vol.231 , pp. 374-382
    • Frassineti, C.1    Ghelli, S.2    Gans, P.3    Sabatini, A.4    Moruzzi, M.S.5    Vacca, A.6
  • 36
    • 0000709449 scopus 로고
    • a values and total proton distribution pattern of spermidine by carbon-13 nuclear magnetic resonance titrations
    • a values and total proton distribution pattern of spermidine by carbon-13 nuclear magnetic resonance titrations. Anal. Chem. 53, 789-793.
    • (1981) Anal. Chem , vol.53 , pp. 789-793
    • Kimberly, M.1    Goldstein, J.H.2
  • 37
    • 0030586985 scopus 로고    scopus 로고
    • Copper(II) ions as a factor interfering in the interaction between bioligands in systems with adenosine and polyamines
    • Lomozik, L., Gasowska, A., and Bolewski, L. (1996) Copper(II) ions as a factor interfering in the interaction between bioligands in systems with adenosine and polyamines. J. Inorg. Biochem. 63, 191-206.
    • (1996) J. Inorg. Biochem , vol.63 , pp. 191-206
    • Lomozik, L.1    Gasowska, A.2    Bolewski, L.3
  • 40
    • 0028212977 scopus 로고
    • Intrinsic primary, secondary, and solvent kinetic isotope effects on the reductive halfreaction of D-amino acid oxidase: Evidence against a concerted mechanism
    • Denu, J. M., and Fitzpatrick, P. F. (1994) Intrinsic primary, secondary, and solvent kinetic isotope effects on the reductive halfreaction of D-amino acid oxidase: Evidence against a concerted mechanism. Biochemistry 33, 4001-4007.
    • (1994) Biochemistry , vol.33 , pp. 4001-4007
    • Denu, J.M.1    Fitzpatrick, P.F.2
  • 41
    • 29344450649 scopus 로고    scopus 로고
    • Ionization of zwitterionic amine substrates bound to monomeric sarcosine oxidase
    • Zhao, G., and Jorns, M. S. (2005) Ionization of zwitterionic amine substrates bound to monomeric sarcosine oxidase. Biochemistry 44, 16866-16874.
    • (2005) Biochemistry , vol.44 , pp. 16866-16874
    • Zhao, G.1    Jorns, M.S.2
  • 42
    • 47249152398 scopus 로고    scopus 로고
    • The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzymesubstrate complex
    • 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 enzymesubstrate complex. FEBS J. 275, 3850-3858.
    • (2008) FEBS J , vol.275 , pp. 3850-3858
    • Dunn, R.V.1    Marshall, K.R.2    Munro, A.W.3    Scrutton, N.S.4
  • 45
    • 34250852848 scopus 로고    scopus 로고
    • Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase
    • Ralph, E. C., Hirschi, J. S., Anderson, M. A., Cleland, W. W., Singleton, D. A., and Fitzpatrick, P. F. (2007) Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase. Biochemistry 46, 7655-7664.
    • (2007) Biochemistry , vol.46 , pp. 7655-7664
    • Ralph, E.C.1    Hirschi, J.S.2    Anderson, M.A.3    Cleland, W.W.4    Singleton, D.A.5    Fitzpatrick, P.F.6
  • 46
    • 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
  • 47
    • 85063536463 scopus 로고
    • L-Lactate oxidase
    • Muller, F, Ed, CRC Press, Boca Raton, FL
    • Ghisla, S., and Massey, V. (1991) L-Lactate oxidase. In Chemistry and Biochemistry of FlaVoenzymes (Muller, F., Ed.) Vol. II, pp 243-289, CRC Press, Boca Raton, FL.
    • (1991) Chemistry and Biochemistry of FlaVoenzymes , vol.2 , pp. 243-289
    • Ghisla, S.1    Massey, V.2
  • 48
    • 0028902047 scopus 로고
    • Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 1. Kinetic mechanism
    • Emanuele, J. J., Jr., and Fitzpatrick, P. F. (1995) Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 1. Kinetic mechanism. Biochemistry 34, 3710-3715.
    • (1995) Biochemistry , vol.34 , pp. 3710-3715
    • Emanuele Jr., J.J.1    Fitzpatrick, P.F.2
  • 49
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone3 lysine4 demethylation
    • Lee, M. B., Winder, C., Cooch, H, and Shiekhattar, R. (2005) An essential role for CoREST in nucleosomal histone3 lysine4 demethylation. Nature 437, 432-435.
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.B.1    Winder, C.2    Cooch, H.3    Shiekhattar, R.4


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