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Volumn 289, Issue 19, 2014, Pages 13066-13078

Mycobacterium tuberculosis phosphoenolpyruvate carboxykinase is regulated by redox mechanisms and interaction with thioredoxin

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; GENE EXPRESSION; METABOLISM; REACTION KINETICS;

EID: 84900459867     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.536748     Document Type: Article
Times cited : (26)

References (35)
  • 1
    • 84878560475 scopus 로고    scopus 로고
    • World Health Organization, World Health Organization, Geneva
    • World Health Organization (2013) Global Tuberculosis Report 2013, World Health Organization, Geneva
    • (2013) Global Tuberculosis Report 2013
  • 2
    • 35848943478 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis invasion of macrophages: Linking bacterial gene expression to environmental cues
    • Rohde, K. H., Abramovitch, R. B., and Russell, D. G. (2007) Mycobacterium tuberculosis invasion of macrophages: linking bacterial gene expression to environmental cues. Cell Host Microbe 2, 352-364
    • (2007) Cell Host Microbe , vol.2 , pp. 352-364
    • Rohde, K.H.1    Abramovitch, R.B.2    Russell, D.G.3
  • 3
    • 34248638498 scopus 로고    scopus 로고
    • Microarray analysis of whole genome expression of intracellular Mycobacterium tuberculosis
    • Waddell, S. J., and Butcher, P. D. (2007) Microarray analysis of whole genome expression of intracellular Mycobacterium tuberculosis. Curr. Mol. Med. 7, 287-296
    • (2007) Curr. Mol. Med. , vol.7 , pp. 287-296
    • Waddell, S.J.1    Butcher, P.D.2
  • 4
    • 77649141318 scopus 로고    scopus 로고
    • Unique flexibility in energy metabolism allows mycobacteria to combat starvation and hypoxia
    • Berney, M., and Cook, G. M. (2010) Unique flexibility in energy metabolism allows mycobacteria to combat starvation and hypoxia. PLoS One 5, e8614
    • (2010) PLoS One , vol.5
    • Berney, M.1    Cook, G.M.2
  • 6
    • 84864044868 scopus 로고    scopus 로고
    • Linking the transcriptional profiles and the physiological states of Mycobacterium tuberculosis during an extended intracellular infection
    • Rohde, K. H., Veiga, D. F., Caldwell, S., Balázsi, G., and Russell, D. G. (2012) Linking the transcriptional profiles and the physiological states of Mycobacterium tuberculosis during an extended intracellular infection. PLoS Pathog. 8, e1002769
    • (2012) PLoS Pathog. , vol.8
    • Rohde, K.H.1    Veiga, D.F.2    Caldwell, S.3    Balázsi, G.4    Russell, D.G.5
  • 8
    • 33644915024 scopus 로고    scopus 로고
    • Ancient genes in contemporary persistent microbial pathogens
    • Srinivasan, V., and Morowitz, H. J. (2006) Ancient genes in contemporary persistent microbial pathogens. Biol. Bull. 210, 1-9
    • (2006) Biol. Bull. , vol.210 , pp. 1-9
    • Srinivasan, V.1    Morowitz, H.J.2
  • 9
    • 80055079575 scopus 로고    scopus 로고
    • Fumarate reductase activity maintains an energized membrane in anaerobic Mycobacterium tuberculosis
    • Watanabe, S., Zimmermann, M., Goodwin, M. B., Sauer, U., Barry, C. E., 3rd, and Boshoff, H. I. (2011) Fumarate reductase activity maintains an energized membrane in anaerobic Mycobacterium tuberculosis. PLoS Pathog. 7, e1002287
    • (2011) PLoS Pathog. , vol.7
    • Watanabe, S.1    Zimmermann, M.2    Goodwin, M.B.3    Sauer, U.4    Barry III, C.E.5    Boshoff, H.I.6
  • 11
    • 17644375240 scopus 로고    scopus 로고
    • The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria
    • Sauer, U., and Eikmanns, B. J. (2005) The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria. FEMS Microbiol. Rev. 29, 765-794
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 765-794
    • Sauer, U.1    Eikmanns, B.J.2
  • 12
    • 77953105101 scopus 로고    scopus 로고
    • Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection
    • Marrero, J., Rhee, K. Y., Schnappinger, D., Pethe, K., and Ehrt, S. (2010) Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection. Proc. Natl. Acad. Sci. U. S. A. 107, 9819-9824
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9819-9824
    • Marrero, J.1    Rhee, K.Y.2    Schnappinger, D.3    Pethe, K.4    Ehrt, S.5
  • 13
    • 0038148638 scopus 로고    scopus 로고
    • Pcka-deficient Mycobacterium bovis BCG shows attenuated virulence in mice and in macrophages
    • Liu, K., Yu, J., and Russell, D. G. (2003) pckA-deficient Mycobacterium bovis BCG shows attenuated virulence in mice and in macrophages. Microbiology 149, 1829-1835
    • (2003) Microbiology , vol.149 , pp. 1829-1835
    • Liu, K.1    Yu, J.2    Russell, D.G.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0036683828 scopus 로고    scopus 로고
    • Role of cysteine 306 in the catalytic mechanism of Ascaris suum phosphoenolpyruvate carboxykinase
    • Riós, S. E., and Nowak, T. (2002) Role of cysteine 306 in the catalytic mechanism of Ascaris suum phosphoenolpyruvate carboxykinase. Arch. Biochem. Biophys. 404, 25-37
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 25-37
    • Riós, S.E.1    Nowak, T.2
  • 18
    • 0014894202 scopus 로고
    • Kinetic studies with cytosol and mitochondrial phosphoenolpyruvate carboxykinases
    • Ballard, F. J. (1970) Kinetic studies with cytosol and mitochondrial phosphoenolpyruvate carboxykinases. Biochem. J. 120, 809-814
    • (1970) Biochem. J. , vol.120 , pp. 809-814
    • Ballard, F.J.1
  • 19
    • 55949103773 scopus 로고    scopus 로고
    • 235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion-quadrupole interaction with phosphoenolpyruvate carboxylate
    • 235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion-quadrupole interaction with phosphoenolpyruvate carboxylate. FEBS J. 275, 5810-5819
    • (2008) FEBS J. , vol.275 , pp. 5810-5819
    • Dharmarajan, L.1    Case, C.L.2    Dunten, P.3    Mukhopadhyay, B.4
  • 20
    • 77952985821 scopus 로고    scopus 로고
    • Ultrahigh performance liquid chromatography-tandem mass spectrometry method for fast and robust quantification of anionic and aromatic metabolites
    • Buescher, J. M., Moco, S., Sauer, U., and Zamboni, N. (2010) Ultrahigh performance liquid chromatography-tandem mass spectrometry method for fast and robust quantification of anionic and aromatic metabolites. Anal. Chem. 82, 4403-4412
    • (2010) Anal. Chem. , vol.82 , pp. 4403-4412
    • Buescher, J.M.1    Moco, S.2    Sauer, U.3    Zamboni, N.4
  • 21
    • 0024314836 scopus 로고
    • A reactive cysteine in avian liver phosphoenolpyruvate carboxykinase
    • Makinen, A. L., and Nowak, T. (1989) A reactive cysteine in avian liver phosphoenolpyruvate carboxykinase. J. Biol. Chem. 264, 12148-12157
    • (1989) J. Biol. Chem. , vol.264 , pp. 12148-12157
    • Makinen, A.L.1    Nowak, T.2
  • 22
    • 33847608289 scopus 로고    scopus 로고
    • Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC
    • Li, M. Z., and Elledge, S. J. (2007) Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC. Nat. Methods 4, 251-256
    • (2007) Nat. Methods , vol.4 , pp. 251-256
    • Li, M.Z.1    Elledge, S.J.2
  • 23
    • 84899713549 scopus 로고    scopus 로고
    • Identification of protein partners in Mycobacteria using a single step affinity purification method
    • Plocinski P., Laubitz D., Cysewski D., Stodus K., Kowalskaand K., and Dziembowski A. (2014) Identification of protein partners in Mycobacteria using a single step affinity purification method. PLoS One 9, e91380
    • (2014) PLoS One , vol.9
    • Plocinski, P.1    Laubitz, D.2    Cysewski, D.3    Stodus, K.4    Kowalskaand, K.5    Dziembowski, A.6
  • 25
    • 0035844298 scopus 로고    scopus 로고
    • A GTP-dependent vertebrate-type phosphoenolpyruvate carboxykinase from Mycobacterium smegmatis
    • Mukhopadhyay, B., Concar, E. M., and Wolfe, R. S. (2001) A GTP-dependent vertebrate-type phosphoenolpyruvate carboxykinase from Mycobacterium smegmatis. J. Biol. Chem. 276, 16137-16145
    • (2001) J. Biol. Chem. , vol.276 , pp. 16137-16145
    • Mukhopadhyay, B.1    Concar, E.M.2    Wolfe, R.S.3
  • 26
    • 6044240910 scopus 로고    scopus 로고
    • The phosphoenolpyruvate carboxykinase also catalyzes C3 carboxylation at the interface of glycolysis and the TCA cycle of Bacillus subtilis
    • Zamboni, N., Maaheimo, H., Szyperski, T., Hohmann, H. P., and Sauer, U. (2004) The phosphoenolpyruvate carboxykinase also catalyzes C3 carboxylation at the interface of glycolysis and the TCA cycle of Bacillus subtilis. Metab. Eng. 6, 277-284
    • (2004) Metab. Eng. , vol.6 , pp. 277-284
    • Zamboni, N.1    Maaheimo, H.2    Szyperski, T.3    Hohmann, H.P.4    Sauer, U.5
  • 27
    • 0014690175 scopus 로고
    • Inhibitory effect of physiological bicarbonate ion levels on the activities of glucose 6-phosphate phosphohydrolase
    • Dyson, J. E., Anderson, W. B., and Nordlie, R. C. (1969) Inhibitory effect of physiological bicarbonate ion levels on the activities of glucose 6-phosphate phosphohydrolase. J. Biol. Chem. 244, 560-566
    • (1969) J. Biol. Chem. , vol.244 , pp. 560-566
    • Dyson, J.E.1    Anderson, W.B.2    Nordlie, R.C.3
  • 28
    • 33745814413 scopus 로고    scopus 로고
    • Structural insights into the mechanism of PEPCK catalysis
    • Holyoak, T., Sullivan, S. M., and Nowak, T. (2006) Structural insights into the mechanism of PEPCK catalysis. Biochemistry 45, 8254-8263
    • (2006) Biochemistry , vol.45 , pp. 8254-8263
    • Holyoak, T.1    Sullivan, S.M.2    Nowak, T.3
  • 30
    • 1042278885 scopus 로고    scopus 로고
    • Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
    • Jaeger, T., Budde, H., Flohé, L., Menge, U., Singh, M., Trujillo, M., and Radi, R. (2004) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophys. 423, 182-191
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 182-191
    • Jaeger, T.1    Budde, H.2    Flohé, L.3    Menge, U.4    Singh, M.5    Trujillo, M.6    Radi, R.7
  • 31
    • 79955031171 scopus 로고    scopus 로고
    • Aprabc: A Mycobacterium tuberculosis complex-specific locus that modulates pH-driven adaptation to the macrophage phagosome
    • Abramovitch, R. B., Rohde, K. H., Hsu, F. F., and Russell, D. G. (2011) aprABC: a Mycobacterium tuberculosis complex-specific locus that modulates pH-driven adaptation to the macrophage phagosome. Mol. Microbiol. 80, 678-694
    • (2011) Mol. Microbiol. , vol.80 , pp. 678-694
    • Abramovitch, R.B.1    Rohde, K.H.2    Hsu, F.F.3    Russell, D.G.4
  • 32
    • 84870165873 scopus 로고    scopus 로고
    • The -loop lid domain of phosphoenolpyruvate carboxykinase is essential for catalytic function
    • Johnson, T. A., and Holyoak, T. (2012) The -loop lid domain of phosphoenolpyruvate carboxykinase is essential for catalytic function. Biochemistry 51, 9547-9559
    • (2012) Biochemistry , vol.51 , pp. 9547-9559
    • Johnson, T.A.1    Holyoak, T.2
  • 34
    • 55749110937 scopus 로고    scopus 로고
    • Functional studies of multiple thioredoxins from Mycobacterium tuberculosis
    • Akif, M., Khare, G., Tyagi, A. K., Mande, S. C., and Sardesai, A. A. (2008) Functional studies of multiple thioredoxins from Mycobacterium tuberculosis. J. Bacteriol. 190, 7087-7095
    • (2008) J. Bacteriol. , vol.190 , pp. 7087-7095
    • Akif, M.1    Khare, G.2    Tyagi, A.K.3    Mande, S.C.4    Sardesai, A.A.5


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