메뉴 건너뛰기




Volumn 287, Issue 44, 2012, Pages 37057-37065

Specific function of the Met-Tyr-Trp adduct radical and residues Arg-418 and Asp-137 in the atypical catalase reaction of catalase-peroxidase KatG

Author keywords

[No Author keywords available]

Indexed keywords

ADDUCT RADICALS; CATALASE ACTIVITY; CATALASE-PEROXIDASE; RADICAL INTERACTIONS;

EID: 84868221466     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.401208     Document Type: Article
Times cited : (21)

References (36)
  • 1
    • 2942538880 scopus 로고    scopus 로고
    • Role of KatG catalase-peroxidase in mycobacterial pathogenesis: Countering the phagocyte oxidative burst
    • Ng, V. H., Cox, J. S., Sousa, A. O., MacMicking, J. D., and McKinney, J. D. (2004) Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst. Mol. Microbiol. 52, 1291-1302
    • (2004) Mol. Microbiol. , vol.52 , pp. 1291-1302
    • Ng, V.H.1    Cox, J.S.2    Sousa, A.O.3    MacMicking, J.D.4    McKinney, J.D.5
  • 2
    • 0028905846 scopus 로고
    • Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis
    • Wilson, T. M., de Lisle, G. W., and Collins, D. M. (1995) Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis. Mol. Microbiol. 15, 1009-1015
    • (1995) Mol. Microbiol. , vol.15 , pp. 1009-1015
    • Wilson, T.M.1    De Lisle, G.W.2    Collins, D.M.3
  • 3
    • 72249100848 scopus 로고    scopus 로고
    • The catalase-peroxidase KatG is required for virulence of Xanthomonas campestris pv. campestris in a host plant by providing protection against low levels of H2O2
    • Jittawuttipoka, T., Buranajitpakorn, S., Vattanaviboon, P., and Mongkolsuk, S. (2009) The catalase-peroxidase KatG is required for virulence of Xanthomonas campestris pv. campestris in a host plant by providing protection against low levels of H2O2. J. Bacteriol. 191, 7372-7377
    • (2009) J. Bacteriol. , vol.191 , pp. 7372-7377
    • Jittawuttipoka, T.1    Buranajitpakorn, S.2    Vattanaviboon, P.3    Mongkolsuk, S.4
  • 4
    • 0036707543 scopus 로고    scopus 로고
    • The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui
    • Yamada, Y., Fujiwara, T., Sato, T., Igarashi, N., and Tanaka, N. (2002) The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui. Nat. Struct. Biol. 9, 691-695
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 691-695
    • Yamada, Y.1    Fujiwara, T.2    Sato, T.3    Igarashi, N.4    Tanaka, N.5
  • 7
    • 33645551821 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant
    • Zhao, X., Yu, H., Yu, S., Wang, F., Sacchettini, J. C., and Magliozzo, R. S. (2006) Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant. Biochemistry 45, 4131-4140
    • (2006) Biochemistry , vol.45 , pp. 4131-4140
    • Zhao, X.1    Yu, H.2    Yu, S.3    Wang, F.4    Sacchettini, J.C.5    Magliozzo, R.S.6
  • 8
    • 0037827700 scopus 로고    scopus 로고
    • Total conversion of bifunctional catalase-peroxidase (KatG) to monofunctional peroxidase by exchange of a conserved distal side tyrosine
    • Jakopitsch, C., Auer, M., Ivancich, A., Rüker, F., Furtmüller, P. G., and Obinger, C. (2003) Total conversion of bifunctional catalase-peroxidase (KatG) to monofunctional peroxidase by exchange of a conserved distal side tyrosine. J. Biol. Chem. 278, 20185-20191
    • (2003) J. Biol. Chem. , vol.278 , pp. 20185-20191
    • Jakopitsch, C.1    Auer, M.2    Ivancich, A.3    Rüker, F.4    Furtmüller, P.G.5    Obinger, C.6
  • 9
    • 8544265364 scopus 로고    scopus 로고
    • Influence of the unusual covalent adduct on the kinetics and formation of radical intermediates in synechocystis catalase peroxidase: A stopped-flow and EPR characterization of the MET275, TYR249, and ARG439 variants
    • Jakopitsch, C., Ivancich, A., Schmuckenschlager, F., Wanasinghe, A., Pöltl, G., Furtmüller, P. G., Rüker, F., and Obinger, C. (2004) Influence of the unusual covalent adduct on the kinetics and formation of radical intermediates in synechocystis catalase peroxidase: a stopped-flow and EPR characterization of the MET275, TYR249, and ARG439 variants. J. Biol. Chem. 279, 46082-46095
    • (2004) J. Biol. Chem. , vol.279 , pp. 46082-46095
    • Jakopitsch, C.1    Ivancich, A.2    Schmuckenschlager, F.3    Wanasinghe, A.4    Pöltl, G.5    Furtmüller, P.G.6    Rüker, F.7    Obinger, C.8
  • 10
    • 0242497993 scopus 로고    scopus 로고
    • Rapid formation of compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function
    • Yu, S., Girotto, S., Zhao, X., and Magliozzo, R. S. (2003) Rapid formation of compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function. J. Biol. Chem. 278, 44121-44127
    • (2003) J. Biol. Chem. , vol.278 , pp. 44121-44127
    • Yu, S.1    Girotto, S.2    Zhao, X.3    Magliozzo, R.S.4
  • 11
    • 27944490007 scopus 로고    scopus 로고
    • Role of the Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG) as revealed by KatG(M255I
    • Ghiladi, R. A., Medzihradszky, K. F., and Ortiz de Montellano, P. R. (2005) Role of the Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG) as revealed by KatG(M255I). Biochemistry 44, 15093-15105
    • (2005) Biochemistry , vol.44 , pp. 15093-15105
    • Ghiladi, R.A.1    Medzihradszky, K.F.2    Ortiz De Montellano, P.R.3
  • 12
    • 20744456284 scopus 로고    scopus 로고
    • The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG)
    • Ghiladi, R. A., Knudsen, G. M., Medzihradszky, K. F., and Ortiz de Montellano, P. R. (2005) The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG). J. Biol. Chem. 280, 22651-22663
    • (2005) J. Biol. Chem. , vol.280 , pp. 22651-22663
    • Ghiladi, R.A.1    Knudsen, G.M.2    Medzihradszky, K.F.3    Ortiz De Montellano, P.R.4
  • 13
    • 65449149104 scopus 로고    scopus 로고
    • An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalaseperoxidase (KatG)
    • Suarez, J., Ranguelova, K., Jarzecki, A. A., Manzerova, J., Krymov, V., Zhao, X., Yu, S., Metlitsky, L., Gerfen, G. J., and Magliozzo, R. S. (2009) An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalaseperoxidase (KatG). J. Biol. Chem. 284, 7017-7029
    • (2009) J. Biol. Chem. , vol.284 , pp. 7017-7029
    • Suarez, J.1    Ranguelova, K.2    Jarzecki, A.A.3    Manzerova, J.4    Krymov, V.5    Zhao, X.6    Yu, S.7    Metlitsky, L.8    Gerfen, G.J.9    Magliozzo, R.S.10
  • 14
    • 65449180743 scopus 로고    scopus 로고
    • Role of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant
    • Zhao, X., Yu, S., Ranguelova, K., Suarez, J., Metlitsky, L., Schelvis, J. P., and Magliozzo, R. S. (2009) Role of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant. J. Biol. Chem. 284, 7030-7037
    • (2009) J. Biol. Chem. , vol.284 , pp. 7030-7037
    • Zhao, X.1    Yu, S.2    Ranguelova, K.3    Suarez, J.4    Metlitsky, L.5    Schelvis, J.P.6    Magliozzo, R.S.7
  • 15
    • 77953648254 scopus 로고    scopus 로고
    • A radical on the Met-Tyr-Trp modification required for catalase activity in catalase-peroxidase is established by isotopic labeling and sitedirected mutagenesis
    • Zhao, X., Suarez, J., Khajo, A., Yu, S., Metlitsky, L., and Magliozzo, R. S. (2010) A radical on the Met-Tyr-Trp modification required for catalase activity in catalase-peroxidase is established by isotopic labeling and sitedirected mutagenesis. J. Am. Chem. Soc. 132, 8268-8269
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 8268-8269
    • Zhao, X.1    Suarez, J.2    Khajo, A.3    Yu, S.4    Metlitsky, L.5    Magliozzo, R.S.6
  • 16
    • 33846805916 scopus 로고    scopus 로고
    • Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium tuberculosis
    • Jakopitsch, C., Vlasits, J., Wiseman, B., Loewen, P. C., and Obinger, C. (2007) Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium tuberculosis. Biochemistry 46, 1183-1193
    • (2007) Biochemistry , vol.46 , pp. 1183-1193
    • Jakopitsch, C.1    Vlasits, J.2    Wiseman, B.3    Loewen, P.C.4    Obinger, C.5
  • 17
    • 33645996688 scopus 로고    scopus 로고
    • Roles for Arg-426 and Trp-111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes
    • Carpena, X., Wiseman, B., Deemagarn, T., Herguedas, B., Ivancich, A., Singh, R., Loewen, P. C., and Fita, I. (2006) Roles for Arg-426 and Trp-111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes. Biochemistry 45, 5171-5179
    • (2006) Biochemistry , vol.45 , pp. 5171-5179
    • Carpena, X.1    Wiseman, B.2    Deemagarn, T.3    Herguedas, B.4    Ivancich, A.5    Singh, R.6    Loewen, P.C.7    Fita, I.8
  • 18
    • 77249107909 scopus 로고    scopus 로고
    • Isoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: Catalase, peroxidase, and INH-NADH adduct formation activities
    • Cade, C. E., Dlouhy, A. C., Medzihradszky, K. F., Salas-Castillo, S. P., and Ghiladi, R. A. (2010) Isoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: catalase, peroxidase, and INH-NADH adduct formation activities. Protein Sci. 19, 458-474
    • (2010) Protein Sci. , vol.19 , pp. 458-474
    • Cade, C.E.1    Dlouhy, A.C.2    Medzihradszky, K.F.3    Salas-Castillo, S.P.4    Ghiladi, R.A.5
  • 20
    • 0034673985 scopus 로고    scopus 로고
    • Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis
    • Hillar, A., Peters, B., Pauls, R., Loboda, A., Zhang, H., Mauk, A. G., and Loewen, P. C. (2000) Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis. Biochemistry 39, 5868-5875
    • (2000) Biochemistry , vol.39 , pp. 5868-5875
    • Hillar, A.1    Peters, B.2    Pauls, R.3    Loboda, A.4    Zhang, H.5    Mauk, A.G.6    Loewen, P.C.7
  • 21
    • 33846223322 scopus 로고    scopus 로고
    • Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism
    • Vlasits, J., Jakopitsch, C., Schwanninger, M., Holubar, P., and Obinger, C. (2007) Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism. FEBS Lett. 581, 320-324
    • (2007) FEBS Lett. , vol.581 , pp. 320-324
    • Vlasits, J.1    Jakopitsch, C.2    Schwanninger, M.3    Holubar, P.4    Obinger, C.5
  • 22
    • 0014216132 scopus 로고
    • Studies on the equilibria and kinetics of the reactions of peroxidase with ligands. II. The reaction of ferroperoxidase with oxygen
    • Wittenberg, J. B., Noble, R. W., Wittenberg, B. A., Antonini, E., Brunori, M., and Wyman, J. (1967) Studies on the equilibria and kinetics of the reactions of peroxidase with ligands. II. The reaction of ferroperoxidase with oxygen. J. Biol. Chem. 242, 626-634
    • (1967) J. Biol. Chem. , vol.242 , pp. 626-634
    • Wittenberg, J.B.1    Noble, R.W.2    Wittenberg, B.A.3    Antonini, E.4    Brunori, M.5    Wyman, J.6
  • 23
    • 0034663910 scopus 로고    scopus 로고
    • Catalase-peroxidase (Mycobacterium tuberculosis KatG) catalysis and isoniazid activation
    • Chouchane, S., Lippai, I., and Magliozzo, R. S. (2000) Catalase-peroxidase (Mycobacterium tuberculosis KatG) catalysis and isoniazid activation. Biochemistry 39, 9975-9983
    • (2000) Biochemistry , vol.39 , pp. 9975-9983
    • Chouchane, S.1    Lippai, I.2    Magliozzo, R.S.3
  • 24
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 25
    • 0037044789 scopus 로고    scopus 로고
    • Identification and characterization of tyrosyl radical formation in Mycobacterium tuberculosis catalase-peroxidase (KatG)
    • Chouchane, S., Girotto, S., Yu, S., and Magliozzo, R. S. (2002) Identification and characterization of tyrosyl radical formation in Mycobacterium tuberculosis catalase-peroxidase (KatG). J. Biol. Chem. 277, 42633-42638
    • (2002) J. Biol. Chem. , vol.277 , pp. 42633-42638
    • Chouchane, S.1    Girotto, S.2    Yu, S.3    Magliozzo, R.S.4
  • 26
    • 0033622071 scopus 로고    scopus 로고
    • Quantitative electron paramagnetic resonance and spectrophotometric determination of the free radical 4-hydroxy-2,2,6,6-tetramethylpiperidinyloxy
    • Yordanov, N. D., and Ranguelova, K. (2000) Quantitative electron paramagnetic resonance and spectrophotometric determination of the free radical 4-hydroxy-2,2,6,6-tetramethylpiperidinyloxy. Spectrochim. Acta A Mol. Biomol. Spectrosc. 56A, 373-378
    • (2000) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.56 A , pp. 373-378
    • Yordanov, N.D.1    Ranguelova, K.2
  • 27
    • 0015621197 scopus 로고
    • Studies on horseradish peroxidase. 13. The kinetic effect of cyanide on the oxidationreduction cycle
    • Cotton, M. L., Dunford, H. B., and Raycheba, J. M. (1973) Studies on horseradish peroxidase. 13. The kinetic effect of cyanide on the oxidationreduction cycle. Can. J. Biochem. 51, 627-631
    • (1973) Can. J. Biochem. , vol.51 , pp. 627-631
    • Cotton, M.L.1    Dunford, H.B.2    Raycheba, J.M.3
  • 30
    • 0037424380 scopus 로고    scopus 로고
    • Analysis of heme structural heterogeneity in Mycobacterium tuberculosis catalase-peroxidase (KatG)
    • Chouchane, S., Girotto, S., Kapetanaki, S., Schelvis, J. P., Yu, S., and Magliozzo, R. S. (2003) Analysis of heme structural heterogeneity in Mycobacterium tuberculosis catalase-peroxidase (KatG). J. Biol. Chem. 278, 8154-8162
    • (2003) J. Biol. Chem. , vol.278 , pp. 8154-8162
    • Chouchane, S.1    Girotto, S.2    Kapetanaki, S.3    Schelvis, J.P.4    Yu, S.5    Magliozzo, R.S.6
  • 31
    • 0002204018 scopus 로고
    • Purification of horseradish peroxidase and comparison of its properties with those of catalase and methaemoglobin
    • Keilin, D., and Hartree, E. F. (1951) Purification of horseradish peroxidase and comparison of its properties with those of catalase and methaemoglobin. Biochem. J. 49, 88-104
    • (1951) Biochem. J. , vol.49 , pp. 88-104
    • Keilin, D.1    Hartree, E.F.2
  • 32
    • 54849429128 scopus 로고    scopus 로고
    • Spin trapping investigation of peroxide- and isoniazid-induced radicals in Mycobacterium tuberculosis Catalase-Peroxidase
    • Ranguelova, K., Suarez, J., Magliozzo, R. S., and Mason, R. P. (2008) Spin trapping investigation of peroxide- and isoniazid-induced radicals in Mycobacterium tuberculosis Catalase-Peroxidase. Biochemistry 47, 11377-11385
    • (2008) Biochemistry , vol.47 , pp. 11377-11385
    • Ranguelova, K.1    Suarez, J.2    Magliozzo, R.S.3    Mason, R.P.4
  • 33
    • 15744370277 scopus 로고    scopus 로고
    • Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: Proposal for the catalatic mechanism
    • Jakopitsch, C., Wanasinghe, A., Jantschko, W., Furtmüller, P. G., and Obinger, C. (2005) Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism. J. Biol. Chem. 280, 9037-9042
    • (2005) J. Biol. Chem. , vol.280 , pp. 9037-9042
    • Jakopitsch, C.1    Wanasinghe, A.2    Jantschko, W.3    Furtmüller, P.G.4    Obinger, C.5
  • 34
    • 0024806963 scopus 로고
    • Kinetics of the reaction of compound II of horseradish peroxidase with hydrogen peroxide to form compound III
    • Adediran, S. A., and Lambeir, A.-M. (1989) Kinetics of the reaction of compound II of horseradish peroxidase with hydrogen peroxide to form compound III. Eur. J. Biochem. 186, 571-576
    • (1989) Eur. J. Biochem. , vol.186 , pp. 571-576
    • Adediran, S.A.1    Lambeir, A.-M.2
  • 35
    • 0023664038 scopus 로고
    • The mechanism of oxyperoxidase formation from ferryl peroxidase and hydrogen peroxide
    • Nakajima, R., and Yamazaki, I. (1987) The mechanism of oxyperoxidase formation from ferryl peroxidase and hydrogen peroxide. J. Biol. Chem. 262, 2576-2581
    • (1987) J. Biol. Chem. , vol.262 , pp. 2576-2581
    • Nakajima, R.1    Yamazaki, I.2
  • 36
    • 0031029149 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis
    • Johnsson, K., Froland, W. A., and Schultz, P. G. (1997) Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis. J. Biol. Chem. 272, 2834-2840
    • (1997) J. Biol. Chem. , vol.272 , pp. 2834-2840
    • Johnsson, K.1    Froland, W.A.2    Schultz, P.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.