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Volumn 19, Issue , 2013, Pages 116-127

A reverse glyoxylate shunt to build a non-native route from C4 to C2 in Escherichia coli

Author keywords

Acetyl coA biosynthesis; Central metabolism; Glyoxylate shunt; Non native pathways; Primary metabolism; Reversibility

Indexed keywords

ACETYL-COA; CENTRAL METABOLISMS; GLYOXYLATE; NON-NATIVE; REVERSIBILITY;

EID: 84883554005     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2013.06.004     Document Type: Article
Times cited : (51)

References (27)
  • 1
    • 33745530619 scopus 로고    scopus 로고
    • Biochemical thermodynamics: applications of mathematica
    • Alberty R.A. Biochemical thermodynamics: applications of mathematica. Methods Biochem. Anal. 2006, 48:1-458.
    • (2006) Methods Biochem. Anal. , vol.48 , pp. 1-458
    • Alberty, R.A.1
  • 2
    • 0014019775 scopus 로고
    • The anaplerotic fixation of carbon dioxide by Escherichia coli
    • Ashworth J.M., Kornberg H.L. The anaplerotic fixation of carbon dioxide by Escherichia coli. Proc. R. Soc. London B. Biol. Sci. 1966, 165:179-188.
    • (1966) Proc. R. Soc. London B. Biol. Sci. , vol.165 , pp. 179-188
    • Ashworth, J.M.1    Kornberg, H.L.2
  • 5
    • 84859369657 scopus 로고    scopus 로고
    • A survey of carbon fixation pathways through a quantitative lens
    • Bar-Even A., Noor E., Milo R. A survey of carbon fixation pathways through a quantitative lens. J. Exp. Bot. 2012, 63:2325-2342.
    • (2012) J. Exp. Bot. , vol.63 , pp. 2325-2342
    • Bar-Even, A.1    Noor, E.2    Milo, R.3
  • 6
    • 79953201555 scopus 로고    scopus 로고
    • Ecological aspects of the distribution of different autotrophic CO2 fixation pathways
    • Berg I.A. Ecological aspects of the distribution of different autotrophic CO2 fixation pathways. Appl. Environ. Microbiol. 2011, 77:1925-1936.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1925-1936
    • Berg, I.A.1
  • 7
    • 0030969849 scopus 로고    scopus 로고
    • Molecular and mutational analysis of a DNA region separating two methylotrophy gene clusters in Methylobacterium extorquens AM1
    • Chistoserdova L., Lidstrom M.E. Molecular and mutational analysis of a DNA region separating two methylotrophy gene clusters in Methylobacterium extorquens AM1. Microbiology 1997, 143(Pt 5):1729-1736.
    • (1997) Microbiology , vol.143 , Issue.PART 5 , pp. 1729-1736
    • Chistoserdova, L.1    Lidstrom, M.E.2
  • 8
    • 0028215037 scopus 로고
    • Genetics of the serine cycle in Methylobacterium extorquens AM1: identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA
    • Chistoserdova L.V., Lidstrom M.E. Genetics of the serine cycle in Methylobacterium extorquens AM1: identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA. J. Bacteriol. 1994, 176:1957-1968.
    • (1994) J. Bacteriol. , vol.176 , pp. 1957-1968
    • Chistoserdova, L.V.1    Lidstrom, M.E.2
  • 9
    • 0031782955 scopus 로고    scopus 로고
    • Regulation of acetate metabolism by protein phosphorylation in enteric bacteria
    • Cozzone A.J. Regulation of acetate metabolism by protein phosphorylation in enteric bacteria. Annu. Rev. Microbiol. 1998, 52:127-164.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 127-164
    • Cozzone, A.J.1
  • 11
    • 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., Alber B.E. 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. 2010, 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
  • 14
    • 77952566391 scopus 로고    scopus 로고
    • Biochemical characterization of the C4-dicarboxylate transporter DctA from Bacillus subtilis
    • Groeneveld M., Weme R.G., Duurkens R.H., Slotboom D.J. Biochemical characterization of the C4-dicarboxylate transporter DctA from Bacillus subtilis. J. Bacteriol. 2010, 192:2900-2907.
    • (2010) J. Bacteriol. , vol.192 , pp. 2900-2907
    • Groeneveld, M.1    Weme, R.G.2    Duurkens, R.H.3    Slotboom, D.J.4
  • 15
    • 0028113546 scopus 로고
    • Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli
    • Gruer M.J., Guest J.R. Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli. Microbiology 1994, 140(Pt 10):2531-2541.
    • (1994) Microbiology , vol.140 , Issue.PART 10 , pp. 2531-2541
    • Gruer, M.J.1    Guest, J.R.2
  • 17
    • 0021746740 scopus 로고
    • Purification and some kinetic properties of rat liver ATP citrate lyase
    • Houston B., Nimmo H.G. Purification and some kinetic properties of rat liver ATP citrate lyase. Biochem. J. 1984, 224:437-443.
    • (1984) Biochem. J. , vol.224 , pp. 437-443
    • Houston, B.1    Nimmo, H.G.2
  • 18
    • 33846109956 scopus 로고    scopus 로고
    • 2 fixation via the reductive tricarboxylic acid cycle in different lineages within the phylum Aquificae: evidence for two ways of citrate cleavage
    • 2 fixation via the reductive tricarboxylic acid cycle in different lineages within the phylum Aquificae: evidence for two ways of citrate cleavage. Environ. Microbiol. 2007, 9:81-92.
    • (2007) Environ. Microbiol. , vol.9 , pp. 81-92
    • Hugler, M.1    Huber, H.2    Molyneaux, S.J.3    Vetriani, C.4    Sievert, S.M.5
  • 20
    • 0022860142 scopus 로고
    • Three classes of Escherichia coli mutants selected for aerobic expression of fumarate reductase
    • Iuchi S., Kuritzkes D.R., Lin E.C. Three classes of Escherichia coli mutants selected for aerobic expression of fumarate reductase. J. Bacteriol. 1986, 168:1415-1421.
    • (1986) J. Bacteriol. , vol.168 , pp. 1415-1421
    • Iuchi, S.1    Kuritzkes, D.R.2    Lin, E.C.3
  • 21
    • 0022356550 scopus 로고
    • Transcription of the Escherichia coli fumarate reductase genes (frdABCD) and their coordinate regulation by oxygen, nitrate, and fumarate
    • Jones H.M., Gunsalus R.P. Transcription of the Escherichia coli fumarate reductase genes (frdABCD) and their coordinate regulation by oxygen, nitrate, and fumarate. J. Bacteriol. 1985, 164:1100-1109.
    • (1985) J. Bacteriol. , vol.164 , pp. 1100-1109
    • Jones, H.M.1    Gunsalus, R.P.2
  • 22
    • 33748780101 scopus 로고    scopus 로고
    • Both subunits of ATP-citrate lyase from Chlorobium tepidum contribute to catalytic activity
    • Kim W., Tabita F.R. Both subunits of ATP-citrate lyase from Chlorobium tepidum contribute to catalytic activity. J. Bacteriol. 2006, 188:6544-6552.
    • (2006) J. Bacteriol. , vol.188 , pp. 6544-6552
    • Kim, W.1    Tabita, F.R.2
  • 23
    • 0000581636 scopus 로고
    • Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle
    • Kornberg H.L., Krebs H.A. Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle. Nature 1957, 179:988-991.
    • (1957) Nature , vol.179 , pp. 988-991
    • Kornberg, H.L.1    Krebs, H.A.2
  • 24
    • 0020059725 scopus 로고
    • Genetic regulation of the glyoxylate shunt in Escherichia coli K-12
    • Maloy S.R., Nunn W.D. Genetic regulation of the glyoxylate shunt in Escherichia coli K-12. J. Bacteriol. 1982, 149:173-180.
    • (1982) J. Bacteriol. , vol.149 , pp. 173-180
    • Maloy, S.R.1    Nunn, W.D.2
  • 26
    • 0035152663 scopus 로고    scopus 로고
    • Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity
    • Tseng C.P., Yu C.C., Lin H.H., Chang C.Y., Kuo J.T. Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity. J. Bacteriol. 2001, 183:461-467.
    • (2001) J. Bacteriol. , vol.183 , pp. 461-467
    • Tseng, C.P.1    Yu, C.C.2    Lin, H.H.3    Chang, C.Y.4    Kuo, J.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.