메뉴 건너뛰기




Volumn 72, Issue 2, 2006, Pages 1040-1044

Biodegradation of 3-nitrotyrosine by Burkholderia sp. strain JS165 and Variovorax paradoxus JS171

Author keywords

[No Author keywords available]

Indexed keywords

BIODEGRADATION; CARBON; ECOSYSTEMS; ENERGY RESOURCES; LIPIDS; METABOLISM; MICROORGANISMS; NITROGEN; NITROGEN OXIDES; NUCLEIC ACIDS; PROTEINS; STOICHIOMETRY;

EID: 33144476159     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.72.2.1040-1044.2006     Document Type: Article
Times cited : (35)

References (32)
  • 1
    • 0000998679 scopus 로고
    • Metabolism of p-hydroxyphenylacetic acid in Pseudomonas avails
    • Adachi, K., Y. Takeda, S. Senoh, and H. Kita. 1964. Metabolism of p-hydroxyphenylacetic acid in Pseudomonas avails. Biochim. Biophys. Acta 93:483-493.
    • (1964) Biochim. Biophys. Acta , vol.93 , pp. 483-493
    • Adachi, K.1    Takeda, Y.2    Senoh, S.3    Kita, H.4
  • 2
    • 3242813728 scopus 로고    scopus 로고
    • The homogentisate pathway: A central catabolic pathway involved in the degradation of L-phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in Pseudomonas putida
    • Arias-Barrau, E., E. R. Olivera, J. M. Luengo, C. Fernandez, B. Galan, J. L. Garcia, E. Diaz, and B. Minambres. 2004. The homogentisate pathway: a central catabolic pathway involved in the degradation of L-phenylalanine, L-tyrosine, and 3-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 186:5062-5077.
    • (2004) J. Bacteriol. , vol.186 , pp. 5062-5077
    • Arias-Barrau, E.1    Olivera, E.R.2    Luengo, J.M.3    Fernandez, C.4    Galan, B.5    Garcia, J.L.6    Diaz, E.7    Minambres, B.8
  • 3
    • 0027065530 scopus 로고
    • p-Hydroxyphenyl-acetate-3-hydroxylase. A two-protein component enzyme
    • Arunachalam, U., V. Massey, and C. Vaidyanathan. 1992. p-Hydroxyphenyl-acetate-3-hydroxylase. A two-protein component enzyme. J. Biol. Chem. 267:25848-25855.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25848-25855
    • Arunachalam, U.1    Massey, V.2    Vaidyanathan, C.3
  • 4
    • 0023119482 scopus 로고
    • Nitrosubstituted aromatic compounds as nitrogen source for bacteria
    • Bruhn, C., H. Lenke, and H.-J. Knackmuss. 1987. Nitrosubstituted aromatic compounds as nitrogen source for bacteria. Appl. Environ. Microbiol. S3: 208-210.
    • (1987) Appl. Environ. Microbiol. , vol.S3 , pp. 208-210
    • Bruhn, C.1    Lenke, H.2    Knackmuss, H.-J.3
  • 5
    • 0003807799 scopus 로고
    • Purification studies of tyrosine-alpha-ketoglutaric acid transaminase
    • Canellakis, Z. N., and P. P. Cohen. 1956. Purification studies of tyrosine-alpha-ketoglutaric acid transaminase. J. Biol. Chem. 222:53-62.
    • (1956) J. Biol. Chem. , vol.222 , pp. 53-62
    • Canellakis, Z.N.1    Cohen, P.P.2
  • 8
    • 0034928756 scopus 로고    scopus 로고
    • NO, nitrotyrosine, and cyclic GMP in signal transduction
    • Hanafy, K. A., J. A. Krumenacker, and F. Murad. 2001. NO, nitrotyrosine, and cyclic GMP in signal transduction. Med. Sci. Monit. 7:801-819.
    • (2001) Med. Sci. Monit. , vol.7 , pp. 801-819
    • Hanafy, K.A.1    Krumenacker, J.A.2    Murad, F.3
  • 9
    • 19944374808 scopus 로고    scopus 로고
    • 2/nitrite systems in human saliva and characterization of an oxidation product of quercetin formed during the inhibition
    • 2/nitrite systems in human saliva and characterization of an oxidation product of quercetin formed during the inhibition. J. Agric. Food Chem. 53:3265-3272.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 3265-3272
    • Hirota, S.1    Takahama, U.2    Ly, T.N.3    Yamauchi, R.4
  • 10
    • 0037948843 scopus 로고    scopus 로고
    • Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins
    • Irie, Y., M. Saeki, Y. Kamisaki, E. Martin, and F. Murad. 2003. Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins. Proc. Natl. Acad. Sci. USA 100:5634-5639.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5634-5639
    • Irie, Y.1    Saeki, M.2    Kamisaki, Y.3    Martin, E.4    Murad, F.5
  • 11
    • 0038731081 scopus 로고    scopus 로고
    • Biological selectivity and functional aspects of protein tyrosine nitration
    • Ischiropoulos, H. 2003. Biological selectivity and functional aspects of protein tyrosine nitration. Biochem. Biophys. Res. Commun. 305:776-783.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 776-783
    • Ischiropoulos, H.1
  • 12
    • 20144388475 scopus 로고    scopus 로고
    • Abundance of cellular material and proteins in the atmosphere
    • Jaenicke, R. 2005. Abundance of cellular material and proteins in the atmosphere. Science 308:73.
    • (2005) Science , vol.308 , pp. 73
    • Jaenicke, R.1
  • 13
    • 0017597937 scopus 로고
    • Purification and properties of homoprotocatechuate 2,3-dioxygenase from Bacillus stearothermophilus
    • Jamaluddin, M. P. 1977. Purification and properties of homoprotocatechuate 2,3-dioxygenase from Bacillus stearothermophilus. J. Bacteriol. 129:690-697.
    • (1977) J. Bacteriol. , vol.129 , pp. 690-697
    • Jamaluddin, M.P.1
  • 16
    • 0037105336 scopus 로고    scopus 로고
    • Signal transduction by protein tyrosine nitration: Competition or cooperation with tyrosine phosphorylation-dependent signaling events?
    • Monteiro, H. P. 2002. Signal transduction by protein tyrosine nitration: competition or cooperation with tyrosine phosphorylation-dependent signaling events? Free Radic. Biol. Med. 33:765-773.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 765-773
    • Monteiro, H.P.1
  • 17
    • 20444411648 scopus 로고    scopus 로고
    • The moving frontier in nitric oxide-dependent signaling
    • Nathan, C. 2004. The moving frontier in nitric oxide-dependent signaling. Sci. STKE 2004:pe52.
    • (2004) Sci. STKE , vol.2004
    • Nathan, C.1
  • 18
    • 0034061462 scopus 로고    scopus 로고
    • Aerobic degradation of dinitrotoluenes and pathway for bacterial degradation of 2,6-dinitrotoluene
    • Nishino, S. F., G. Paoli, and J. C. Spain. 2000. Aerobic degradation of dinitrotoluenes and pathway for bacterial degradation of 2,6-dinitrotoluene. Appl. Environ. Microbiol. 66:2139-2147.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2139-2147
    • Nishino, S.F.1    Paoli, G.2    Spain, J.C.3
  • 19
    • 11144281909 scopus 로고    scopus 로고
    • Catabolism of nitroaromatic compounds
    • J.-L. Ramos (ed.), Kluwer Academic/Plenum Publishers, New York, N.Y.
    • Nishino, S. F., and J. C. Spain. 2004. Catabolism of nitroaromatic compounds, p. 575-608. In J.-L. Ramos (ed.), Pseudomonas, vol. 3. Kluwer Academic/Plenum Publishers, New York, N.Y.
    • (2004) Pseudomonas , vol.3 , pp. 575-608
    • Nishino, S.F.1    Spain, J.C.2
  • 20
    • 0025612247 scopus 로고
    • Nitrotyrosine as a new marker for endogenous nitrosation and nitration of proteins
    • Ohshima, H., M. Friesen, I. Brouet, and H. Bartsch. 1990. Nitrotyrosine as a new marker for endogenous nitrosation and nitration of proteins. Food Chem. Toxicol. 28:647-652.
    • (1990) Food Chem. Toxicol. , vol.28 , pp. 647-652
    • Ohshima, H.1    Friesen, M.2    Brouet, I.3    Bartsch, H.4
  • 21
    • 0033372542 scopus 로고    scopus 로고
    • Nitrite- and peroxide-dependent oxidation pathways of dopamine: 6-Nitrodopamine and 6-hydroxydopamine formation as potential contributory mechanisms of oxidative stress- and nitric oxide-induced neurotoxicity in neuronal degeneration
    • Palumbo, A, A. Napolitano, P. Barone, and M. d'Ischia. 1999. Nitrite- and peroxide-dependent oxidation pathways of dopamine: 6-nitrodopamine and 6-hydroxydopamine formation as potential contributory mechanisms of oxidative stress- and nitric oxide-induced neurotoxicity in neuronal degeneration. Chem. Res. Toxicol. 12:1213-1222.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 1213-1222
    • Palumbo, A.1    Napolitano, A.2    Barone, P.3    D'Ischia, M.4
  • 22
    • 1642570319 scopus 로고    scopus 로고
    • Nitric oxide, oxidants, and protein tyrosine nitration
    • Radi, R. 2004. Nitric oxide, oxidants, and protein tyrosine nitration. Proc. Natl. Acad. Sci. USA 101:4003-4008.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4003-4008
    • Radi, R.1
  • 24
    • 0000612080 scopus 로고
    • Phenotypic characterization
    • P. Gerhardt, R. G. E. Murray, W. A. Wood, and N. R. Krieg (ed.), ASM Press, Washington, D.C.
    • Smibert, R. M., and N. R. Krieg. 1994. Phenotypic characterization, p. 607-654. In P. Gerhardt, R. G. E. Murray, W. A. Wood, and N. R. Krieg (ed.), Methods for general and molecular bacteriology. ASM Press, Washington, D.C.
    • (1994) Methods for General and Molecular Bacteriology , pp. 607-654
    • Smibert, R.M.1    Krieg, N.R.2
  • 26
    • 0032950583 scopus 로고    scopus 로고
    • In vivo disposition of 3-nitro-L-tyrosine in rats: Implications on tracking systemic peroxynitrite exposure
    • Tabrizi-Fard, M. A., T. S. Maurer, and H.-L. Fung. 1999. In vivo disposition of 3-nitro-L-tyrosine in rats: implications on tracking systemic peroxynitrite exposure. Drug Metab. Dispos. 27:429-431.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 429-431
    • Tabrizi-Fard, M.A.1    Maurer, T.S.2    Fung, H.-L.3
  • 27
    • 0037127253 scopus 로고    scopus 로고
    • The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates
    • Vaillancourt, F. H., G. Labbe, N. M. Drouin, P. D. Fortin, and L. D. Eltis. 2002. The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates. J. Biol. Chem. 277:2019-2027.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2019-2027
    • Vaillancourt, F.H.1    Labbe, G.2    Drouin, N.M.3    Fortin, P.D.4    Eltis, L.D.5
  • 28
    • 17644419814 scopus 로고    scopus 로고
    • Ring-cleavage dioxygenases
    • J.-L. Ramos (ed.), Kluwer Academic/Plenum Publishers, New York, N.Y.
    • Vaillancourt, F. H., J. T. Bolin, and L. D. Eltis. 2004. Ring-cleavage dioxygenases, p. 359-395. in J.-L. Ramos (ed.), Pseudomonas, vol. 3. Kluwer Academic/Plenum Publishers, New York, N.Y.
    • (2004) Pseudomonas , vol.3 , pp. 359-395
    • Vaillancourt, F.H.1    Bolin, J.T.2    Eltis, L.D.3
  • 29
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity
    • van der Vliet, A., J. P. Eiserich, B. Halliwell, and C. E. Cross. 1997. Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J. Biol. Chem. 272:7617-7625.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7617-7625
    • Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 31
    • 0035209452 scopus 로고    scopus 로고
    • Nitric oxide: Comparative synthesis and signaling in animal and plant cells
    • Wendehenne, D., A. Pugin, D. F. Klessig, and J. Durner. 2001. Nitric oxide: comparative synthesis and signaling in animal and plant cells. Trends Plant Sci. 6:177-183.
    • (2001) Trends Plant Sci. , vol.6 , pp. 177-183
    • Wendehenne, D.1    Pugin, A.2    Klessig, D.F.3    Durner, J.4
  • 32
    • 0023896389 scopus 로고
    • Purification and characterization of a bacterial nitrophenol oxygenase which converts ortho-nitrophenol to catechol and nitrite
    • Zeyer, J., and H. P. Kocher. 1988. Purification and characterization of a bacterial nitrophenol oxygenase which converts ortho-nitrophenol to catechol and nitrite. J. Bacteriol. 70:1789-1794.
    • (1988) J. Bacteriol. , vol.70 , pp. 1789-1794
    • Zeyer, J.1    Kocher, H.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.