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Volumn 287, Issue 1, 2012, Pages 757-766

The ethylmalonyl-CoA pathway is used in place of the glyoxylate cycle by Methylobacterium extorquens AM1 during growth on acetate

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL-COA; ENTRY POINT; EXTORQUENS AM1; GLYOXYLATE; KEY ENZYMES; METABOLIC FLUX ANALYSIS; METABOLIC FLUX DISTRIBUTION; METHYLOBACTERIUM; PROTEOMIC ANALYSIS; REACTION SEQUENCES; TCA CYCLE;

EID: 84855258472     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.305219     Document Type: Article
Times cited : (70)

References (44)
  • 1
    • 0000581636 scopus 로고
    • Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle
    • Kornberg, H. L., and Krebs, H. A. (1957) Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle. Nature 179, 988-991
    • (1957) Nature , vol.179 , pp. 988-991
    • Kornberg, H.L.1    Krebs, H.A.2
  • 2
    • 0000396226 scopus 로고
    • Synthesis of C4-dicarboxylic acids from acetate by a glyoxylate bypass of the tricarboxylic acid cycle
    • Kornberg, H. L., and Madsen, N. B. (1957) Synthesis of C4-dicarboxylic acids from acetate by a glyoxylate bypass of the tricarboxylic acid cycle. Biochim. Biophys. Acta 24, 651-653
    • (1957) Biochim. Biophys. Acta , vol.24 , pp. 651-653
    • Kornberg, H.L.1    Madsen, N.B.2
  • 4
    • 0017151577 scopus 로고
    • Acetate metabolism in Rhodopseudomonas gelatinosa and several other Rhodospirillaceae
    • Albers, H., and Gottschalk, G. (1976) Acetate metabolism in Rhodopseudomonas gelatinosa and several other Rhodospirillaceae. Arch. Microbiol. 111, 45-49
    • (1976) Arch. Microbiol. , vol.111 , pp. 45-49
    • Albers, H.1    Gottschalk, G.2
  • 5
    • 0030754153 scopus 로고    scopus 로고
    • A novel alternate anaplerotic pathway to the glyoxylate cycle in streptomycetes
    • Han, L., and Reynolds, K. A. (1997) A novel alternate anaplerotic pathway to the glyoxylate cycle in streptomycetes. J. Bacteriol. 179, 5157-5164 (Pubitemid 27340551)
    • (1997) Journal of Bacteriology , vol.179 , Issue.16 , pp. 5157-5164
    • Han, L.1    Reynolds, K.A.2
  • 6
    • 0018927443 scopus 로고
    • Mixotrophic growth of Thiobacillus A2 on acetate and thiosulfate as growth limiting substrates in the chemostat
    • DOI 10.1007/BF00421888
    • Gottschal, J. C., and Kuenen, J. G. (1980) Mixotrophic growth of Thiobacillus-A2 on acetate and thiosulfate as growth limiting substrates in the chemostat. Arch. Microbiol. 126, 33-42 (Pubitemid 10020670)
    • (1980) Archives of Microbiology , vol.126 , Issue.1 , pp. 33-42
    • Gottschal, J.C.1    Kuenen, J.G.2
  • 7
    • 79959974762 scopus 로고    scopus 로고
    • How half a century of research was required to understand bacterial growth on C1 and C2 compounds: The story of the serine cycle and the ethylmalonyl-CoA pathway
    • Anthony, C. (2011) How half a century of research was required to understand bacterial growth on C1 and C2 compounds: the story of the serine cycle and the ethylmalonyl-CoA pathway. Sci. Prog. 94, 109-137
    • (2011) Sci. Prog. , vol.94 , pp. 109-137
    • Anthony, C.1
  • 9
    • 67049132524 scopus 로고    scopus 로고
    • Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase
    • Erb, T. J., Brecht, V., Fuchs, G., Müller, M., and Alber, B. E. (2009) Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase. Proc. Natl. Acad. Sci. U.S.A. 106, 8871-8876
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8871-8876
    • Erb, T.J.1    Brecht, V.2    Fuchs, G.3    Müller, M.4    Alber, B.E.5
  • 10
    • 77749279783 scopus 로고    scopus 로고
    • The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase
    • Erb, T. J., Frerichs-Revermann, L., Fuchs, G., and Alber, B. E. (2010) The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase. J. Bacteriol. 192, 1249-1258
    • (2010) J. Bacteriol. , vol.192 , pp. 1249-1258
    • Erb, T.J.1    Frerichs-Revermann, L.2    Fuchs, G.3    Alber, B.E.4
  • 11
    • 70350165195 scopus 로고    scopus 로고
    • (2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
    • Erb, T. J., Fuchs, G., and Alber, B. E. (2009) (2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. Mol. Microbiol. 73, 992-1008
    • (2009) Mol. Microbiol. , vol.73 , pp. 992-1008
    • Erb, T.J.1    Fuchs, G.2    Alber, B.E.3
  • 12
    • 33748494471 scopus 로고    scopus 로고
    • Study of an alternate glyoxylate cycle for acetate assimilation by Rhodobacter sphaeroides
    • DOI 10.1111/j.1365-2958.2006.05238.x
    • Alber, B. E., Spanheimer, R., Ebenau-Jehle, C., and Fuchs, G. (2006) Study of an alternate glyoxylate cycle for acetate assimilation by Rhodobacter sphaeroides. Mol. Microbiol. 61, 297-309 (Pubitemid 44356564)
    • (2006) Molecular Microbiology , vol.61 , Issue.2 , pp. 297-309
    • Alber, B.E.1    Spanheimer, R.2    Ebenau-Jehle, C.3    Fuchs, G.4
  • 14
    • 80755159333 scopus 로고    scopus 로고
    • Genome-scale reconstruction and system level investigation of the metabolic network of Methylobacterium extorquens AM1
    • Peyraud, R., Schneider, K., Kiefer, P., Massou, S., Vorholt, J. A., and Portais, J. C. (2011) Genome-scale reconstruction and system level investigation of the metabolic network of Methylobacterium extorquens AM1. BMC Syst. Biol. 5, 189
    • (2011) BMC Syst. Biol. , vol.5 , pp. 189
    • Peyraud, R.1    Schneider, K.2    Kiefer, P.3    Massou, S.4    Vorholt, J.A.5    Portais, J.C.6
  • 15
    • 0030463296 scopus 로고    scopus 로고
    • Flux analysis and control of the central metabolic pathways in Escherichia coli
    • Holms, H. (1996) Flux analysis and control of the central metabolic pathways in Escherichia coli. FEMS Microbiol. Rev. 19, 85-116
    • (1996) FEMS Microbiol. Rev. , vol.19 , pp. 85-116
    • Holms, H.1
  • 16
    • 0037066717 scopus 로고    scopus 로고
    • Global expression profiling of acetate-grown Escherichia coli
    • DOI 10.1074/jbc.M110809200
    • Oh, M. K., Rohlin, L., Kao, K. C., and Liao, J. C. (2002) Global expression profiling of acetate-grown Escherichia coli. J. Biol. Chem. 277, 13175-13183 (Pubitemid 34952688)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13175-13183
    • Oh, M.-K.1    Rohlin, L.2    Kao, K.C.3    Liao, J.C.4
  • 17
    • 0021149774 scopus 로고
    • Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt
    • Walsh, K., and Koshland, D. E., Jr. (1984) Determination of flux through the branch point of two metabolic cycles: the tricarboxylic acid cycle and the glyoxylate shunt. J. Biol. Chem. 259, 9646-9654 (Pubitemid 14060533)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.15 , pp. 9646-9654
    • Walsh, K.1    Koshland Jr., D.E.2
  • 18
    • 0037422210 scopus 로고    scopus 로고
    • 13C-labeled acetate and glucose using GC-MS and powerful flux calculation method
    • DOI 10.1016/S0168-1656(02)00316-4, PII S0168165602003164
    • Zhao, J., and Shimizu, K. (2003) Metabolic flux analysis of Escherichia coli K12 grown on 13C-labeled acetate and glucose using GC-MS and powerful flux calculation method. J. Biotechnol. 101, 101-117 (Pubitemid 36144197)
    • (2003) Journal of Biotechnology , vol.101 , Issue.2 , pp. 101-117
    • Zhao, J.1    Shimizu, K.2
  • 19
    • 0037391699 scopus 로고    scopus 로고
    • Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement
    • Peng, L., and Shimizu, K. (2003) Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement. Appl. Microbiol. Biotechnol. 61, 163-178 (Pubitemid 36470198)
    • (2003) Applied Microbiology and Biotechnology , vol.61 , Issue.2 , pp. 163-178
    • Peng, L.1    Shimizu, K.2
  • 21
    • 0034115397 scopus 로고    scopus 로고
    • Quantitative determination of metabolic fluxes during coutilization of two carbon sources: Comparative analyses with Corynebacterium glutamicum during growth on acetate and/or glucose
    • DOI 10.1128/JB.182.11.3088-3096.2000
    • Wendisch, V. F., de Graaf, A. A., Sahm, H., and Eikmanns, B. J. (2000) Quantitative determination of metabolic fluxes during coutilization of two carbon sources: comparative analyses with Corynebacterium glutamicum during growth on acetate and/or glucose. J. Bacteriol. 182, 3088-3096 (Pubitemid 30326922)
    • (2000) Journal of Bacteriology , vol.182 , Issue.11 , pp. 3088-3096
    • Wendisch, V.F.1    De Graaf, A.A.2    Sahm, H.3    Eikmanns, B.J.4
  • 22
    • 58849109320 scopus 로고    scopus 로고
    • Methanol-based industrial biotechnology: Current status and future perspectives of methylotrophic bacteria
    • Schrader, J., Schilling, M., Holtmann, D., Sell, D., Filho, M. V., Marx, A., and Vorholt, J. A. (2009) Methanol-based industrial biotechnology: current status and future perspectives of methylotrophic bacteria. Trends Biotechnol. 27, 107-115
    • (2009) Trends Biotechnol. , vol.27 , pp. 107-115
    • Schrader, J.1    Schilling, M.2    Holtmann, D.3    Sell, D.4    Filho, M.V.5    Marx, A.6    Vorholt, J.A.7
  • 23
    • 70649098331 scopus 로고    scopus 로고
    • Metabolite profiling uncovers plasmid-induced cobalt limitation under methylotrophic growth conditions
    • Kiefer, P., Buchhaupt, M., Christen, P., Kaup, B., Schrader, J., and Vorholt, J. A. (2009) Metabolite profiling uncovers plasmid-induced cobalt limitation under methylotrophic growth conditions. PLoS One 4, e7831
    • (2009) PLoS One , vol.4
    • Kiefer, P.1    Buchhaupt, M.2    Christen, P.3    Kaup, B.4    Schrader, J.5    Vorholt, J.A.6
  • 26
    • 77949519484 scopus 로고    scopus 로고
    • On the beta-binomial model for analysis of spectral count data in label-free tandem mass spectrometry-based proteomics
    • Pham, T. V., Piersma, S. R., Warmoes, M., and Jimenez, C. R. (2010) On the beta-binomial model for analysis of spectral count data in label-free tandem mass spectrometry-based proteomics. Bioinformatics 26, 363-369
    • (2010) Bioinformatics , vol.26 , pp. 363-369
    • Pham, T.V.1    Piersma, S.R.2    Warmoes, M.3    Jimenez, C.R.4
  • 28
    • 52249087130 scopus 로고    scopus 로고
    • Quantitative metabolome analysis using liquid chromatography-high- resolution mass spectrometry
    • Kiefer, P., Portais, J. C., and Vorholt, J. A. (2008) Quantitative metabolome analysis using liquid chromatography-high-resolution mass spectrometry. Anal. Biochem. 382, 94-100
    • (2008) Anal. Biochem. , vol.382 , pp. 94-100
    • Kiefer, P.1    Portais, J.C.2    Vorholt, J.A.3
  • 29
    • 34547779987 scopus 로고    scopus 로고
    • NMR-based fluxomics: Quantitative 2D NMR methods for isotopomers analysis
    • DOI 10.1016/j.phytochem.2007.03.011, PII S0031942207001689
    • Massou, S., Nicolas, C., Letisse, F., and Portais, J. C. (2007) NMR-based fluxomics: quantitative 2D NMR methods for isotopomers analysis. Phytochemistry 68, 2330-2340 (Pubitemid 47224957)
    • (2007) Phytochemistry , vol.68 , Issue.16-18 , pp. 2330-2340
    • Massou, S.1    Nicolas, C.2    Letisse, F.3    Portais, J.-C.4
  • 30
    • 34249744402 scopus 로고    scopus 로고
    • 13C-labeled metabolites
    • DOI 10.1016/j.ymben.2007.03.001, PII S1096717607000158
    • Massou, S., Nicolas, C., Letisse, F., and Portais, J. C. (2007) Application of 2D-TOCSY NMR to the measurement of specific 13C-enrichments in complex mixtures of 13C-labeled metabolites. Metab. Eng. 9, 252-257 (Pubitemid 46823904)
    • (2007) Metabolic Engineering , vol.9 , Issue.3 , pp. 252-257
    • Massou, S.1    Nicolas, C.2    Letisse, F.3    Portais, J.-C.4
  • 31
    • 26244452731 scopus 로고    scopus 로고
    • 13C-label distribution of the non-oxidative branch of the pentose phosphate pathway based upon kinetic and genetic evidence
    • DOI 10.1111/j.1742-4658.2005.04907.x
    • Kleijn, R. J., van Winden, W. A., van Gulik, W. M., and Heijnen, J. J. (2005) Revisiting the 13C-label distribution of the non-oxidative branch of the pentose phosphate pathway based upon kinetic and genetic evidence. FEBS J. 272, 4970-4982 (Pubitemid 41415120)
    • (2005) FEBS Journal , vol.272 , Issue.19 , pp. 4970-4982
    • Kleijn, R.J.1    Van Winden, W.A.2    Van Gulik, W.M.3    Heijnen, J.J.4
  • 33
    • 0037967152 scopus 로고    scopus 로고
    • Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of view
    • DOI 10.1128/JB.185.10.2980-2987.2003
    • Chistoserdova, L., Chen, S. W., Lapidus, A., and Lidstrom, M. E. (2003) Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of view. J. Bacteriol. 185, 2980-2987 (Pubitemid 36539093)
    • (2003) Journal of Bacteriology , vol.185 , Issue.10 , pp. 2980-2987
    • Chistoserdova, L.1    Chen, S.-W.2    Lapidus, A.3    Lidstrom, M.E.4
  • 34
    • 2442471747 scopus 로고    scopus 로고
    • Comparison of the proteome of Methylobacterium extorquens AM1 grown under methylotrophic and nonmethylotrophic conditions
    • DOI 10.1002/pmic.200300713
    • Laukel, M., Rossignol, M., Borderies, G., Völker, U., and Vorholt, J. A. (2004) Comparison of the proteome of Methylobacterium extorquens AM1 grown under methylotrophic and nonmethylotrophic conditions. Proteomics 4, 1247-1264 (Pubitemid 38648014)
    • (2004) Proteomics , vol.4 , Issue.5 , pp. 1247-1264
    • Laukel, M.1    Rossignol, M.2    Borderies, G.3    Volker, U.4    Vorholt, J.A.5
  • 35
    • 52649161315 scopus 로고    scopus 로고
    • Comprehensive proteomics of Methylobacterium extorquens AM1 metabolism under single carbon and nonmethylotrophic conditions
    • Bosch, G., Skovran, E., Xia, Q., Wang, T., Taub, F., Miller, J. A., Lidstrom, M. E., and Hackett, M. (2008) Comprehensive proteomics of Methylobacterium extorquens AM1 metabolism under single carbon and nonmethylotrophic conditions. Proteomics 8, 3494-3505
    • (2008) Proteomics , vol.8 , pp. 3494-3505
    • Bosch, G.1    Skovran, E.2    Xia, Q.3    Wang, T.4    Taub, F.5    Miller, J.A.6    Lidstrom, M.E.7    Hackett, M.8
  • 36
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: A critical review
    • DOI 10.1007/s00216-007-1486-6, Proteomics/Molecular Imaging
    • Bantscheff, M., Schirle, M., Sweetman, G., Rick, J., and Kuster, B. (2007) Quantitative mass spectrometry in proteomics: a critical review. Anal. Bioanal. Chem. 389, 1017-1031 (Pubitemid 47482251)
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , Issue.4 , pp. 1017-1031
    • Bantscheff, M.1    Schirle, M.2    Sweetman, G.3    Rick, J.4    Kuster, B.5
  • 37
    • 0031679835 scopus 로고    scopus 로고
    • The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AM1
    • Vorholt, J. A., Chistoserdova, L., Lidstrom, M. E., and Thauer, R. K. (1998) The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AM1. J. Bacteriol. 180, 5351-5356 (Pubitemid 28471531)
    • (1998) Journal of Bacteriology , vol.180 , Issue.20 , pp. 5351-5356
    • Vorholt, J.A.1    Chistoserdova, L.2    Lidstrom, M.E.3    Thauer, R.K.4
  • 38
    • 0033947589 scopus 로고    scopus 로고
    • Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1
    • DOI 10.1046/j.1432-1327.2000.01413.x
    • Hagemeier, C. H., Chistoserdova, L., Lidstrom, M. E., Thauer, R. K., and Vorholt, J. A. (2000) Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1. Eur. J. Biochem. 267, 3762-3769 (Pubitemid 30423039)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.12 , pp. 3762-3769
    • Hagemeier, C.H.1    Chistoserdova, L.2    Lidstrom, M.E.3    Thauer, R.K.4    Vorholt, J.A.5
  • 39
    • 0346361864 scopus 로고    scopus 로고
    • Multiple Formate Dehydrogenase Enzymes in the Facultative Methylotroph Methylobacterium extorquens AM1 Are Dispensable for Growth on Methanol
    • DOI 10.1128/JB.186.1.22-28.2004
    • Chistoserdova, L., Laukel, M., Portais, J. C., Vorholt, J. A., and Lidstrom, M. E. (2004) Multiple formate dehydrogenase enzymes in the facultative methylotroph Methylobacterium extorquens AM1 are dispensable for growth on methanol. J. Bacteriol. 186, 22-28 (Pubitemid 38020282)
    • (2004) Journal of Bacteriology , vol.186 , Issue.1 , pp. 22-28
    • Chistoserdova, L.1    Laukel, M.2    Portais, J.-C.3    Vorholt, J.A.4    Lidstrom, M.E.5
  • 40
    • 77949745939 scopus 로고    scopus 로고
    • Alternative route for glyoxylate consumption during growth on two-carbon compounds by Methylobacterium extorquens AM1
    • Okubo, Y., Yang, S., Chistoserdova, L., and Lidstrom, M. E. (2010) Alternative route for glyoxylate consumption during growth on two-carbon compounds by Methylobacterium extorquens AM1. J. Bacteriol. 192, 1813-1823
    • (2010) J. Bacteriol. , vol.192 , pp. 1813-1823
    • Okubo, Y.1    Yang, S.2    Chistoserdova, L.3    Lidstrom, M.E.4
  • 41
    • 0037240872 scopus 로고    scopus 로고
    • The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: Purification and properties
    • DOI 10.1046/j.1432-1033.2003.03391.x
    • Laukel, M., Chistoserdova, L., Lidstrom, M. E., and Vorholt, J. A. (2003) The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: purification and properties. Eur. J. Biochem. 270, 325-333 (Pubitemid 36114930)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.2 , pp. 325-333
    • Laukel, M.1    Chistoserdova, L.2    Lidstrom, M.E.3    Vorholt, J.A.4
  • 42
    • 0015022135 scopus 로고
    • The biosynthesis of serine and glycine in Pseudomonas AM1 with special reference to growth on carbon sources other than C1 compounds
    • Harder, W., and Quayle, J. R. (1971) The biosynthesis of serine and glycine in Pseudomonas AM1 with special reference to growth on carbon sources other than C1 compounds. Biochem. J. 121, 753-762
    • (1971) Biochem. J. , vol.121 , pp. 753-762
    • Harder, W.1    Quayle, J.R.2
  • 43
    • 0036843686 scopus 로고    scopus 로고
    • Poly-beta-hydroxybutyrate biosynthesis in the facultative methylotroph methylobacterium extorquens AM1: Identification and mutation of gap11, gap20, and phaR
    • DOI 10.1128/JB.184.22.6174-6181.2002
    • Korotkova, N., Chistoserdova, L., and Lidstrom, M. E. (2002) Poly-betahydroxybutyrate biosynthesis in the facultative methylotroph Methylobacterium extorquens AM1: identification and mutation of gap11, gap20, and phaR. J. Bacteriol. 184, 6174-6181 (Pubitemid 35265898)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6174-6181
    • Korotkova, N.1    Chistoserdova, L.2    Lidstrom, M.E.3
  • 44
    • 78049248963 scopus 로고    scopus 로고
    • Methanol assimilation in Methylobacterium extorquens AM1: Demonstration of all enzymes and their regulation
    • Smejkalova, H., Erb, T. J., and Fuchs, G. (2010) Methanol assimilation in Methylobacterium extorquens AM1: Demonstration of all enzymes and their regulation. PLoS One 5, e13001
    • (2010) PLoS One , vol.5
    • Smejkalova, H.1    Erb, T.J.2    Fuchs, G.3


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