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Volumn 227, Issue 1, 2003, Pages 9-16

Two phenotypically compensating isocitrate dehydrogenases in Ralstonia eutropha

Author keywords

Isocitrate dehydrogenase; Isocitrate lyase; Malate synthase; Polyhydroxyalkanoic acids; Ralstonia eutropha

Indexed keywords

ACETIC ACID; ISOCITRATE DEHYDROGENASE; POLY(3 HYDROXYBUTYRIC ACID); ISOENZYME;

EID: 1542543656     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00612-8     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0021801376 scopus 로고
    • Branch point control by the phosphorylation state of isocitrate dehydrogenase: A quantitative examination of fluxes during a regulatory transition
    • Walsh, K. and Koshland, D.E. (1985) Branch point control by the phosphorylation state of isocitrate dehydrogenase: a quantitative examination of fluxes during a regulatory transition. J. Biol. Chem. 260, 8430-8437.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8430-8437
    • Walsh, K.1    Koshland, D.E.2
  • 2
    • 0022985811 scopus 로고
    • The central metabolic pathways of Escherichia coli: Relationship between flux and control at a branch point, efficiency of conversion of biomass, and excretion of acetate
    • Holms, W.H. (1986) The central metabolic pathways of Escherichia coli: relationship between flux and control at a branch point, efficiency of conversion of biomass, and excretion of acetate. Curr. Top. Cell. Regul. 28, 69-105.
    • (1986) Curr. Top. Cell. Regul. , vol.28 , pp. 69-105
    • Holms, W.H.1
  • 3
    • 0020355238 scopus 로고
    • A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle
    • LaPorte, D.C. and Koshland, D.E.J. (1982) A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle. Nature 300, 458-460.
    • (1982) Nature , vol.300 , pp. 458-460
    • Laporte, D.C.1    Koshland, D.E.J.2
  • 4
    • 0000980429 scopus 로고
    • Structure, functions and regulation of NAD and NAPD dependent isocitrate dehydrogenase in higher plants and in other organisms
    • Chen, R.-D. and Gadal, P. (1990) Structure, functions and regulation of NAD and NAPD dependent isocitrate dehydrogenase in higher plants and in other organisms. Plant Physiol. Biochem. 28, 411-427.
    • (1990) Plant Physiol. Biochem. , vol.28 , pp. 411-427
    • Chen, R.-D.1    Gadal, P.2
  • 5
    • 0015476702 scopus 로고
    • Synthese der Enzyme des Tricarbonsäure-Cyclus in Hydrogenomonas eutropha Stamm H16
    • Glaeser, H. and Schlegel, H.G. (1972) Synthese der Enzyme des Tricarbonsäure-Cyclus in Hydrogenomonas eutropha Stamm H16. Arch. Mikrobiol. 86, 315-325.
    • (1972) Arch. Mikrobiol. , vol.86 , pp. 315-325
    • Glaeser, H.1    Schlegel, H.G.2
  • 6
    • 34250969714 scopus 로고
    • Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen
    • Schlegel, H.G., Kaltwasser, H. and Gottschalk, G. (1961) Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 38, 209-222.
    • (1961) Arch. Mikrobiol. , vol.38 , pp. 209-222
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 8
    • 85010439719 scopus 로고
    • A procedure for the isolation of desoxyribonucleic acids from microorganisms
    • Marmur, J. (1961) A procedure for the isolation of desoxyribonucleic acids from microorganisms. J. Mol. Biol. 3, 208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 9
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H.C. and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7, 1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 10
    • 0017751996 scopus 로고
    • Packaging recombinant DNA molecules into bacteriophage particles in vitro
    • Hohn, B. and Murray, K. (1977) Packaging recombinant DNA molecules into bacteriophage particles in vitro. Proc. Natl. Acad. Sci. USA 74, 3259-3263.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3259-3263
    • Hohn, B.1    Murray, K.2
  • 11
    • 0034858524 scopus 로고    scopus 로고
    • The methylcitric acid pathway in Ralstonia eutropha: New genes identified involved in propionate metabolism
    • Brämer, C.O. and Steinbüchel, A. (2001) The methylcitric acid pathway in Ralstonia eutropha: new genes identified involved in propionate metabolism. Microbiology 147, 2203-2214.
    • (2001) Microbiology , vol.147 , pp. 2203-2214
    • Brämer, C.O.1    Steinbüchel, A.2
  • 12
    • 0000925040 scopus 로고
    • Colony hybridization: A method for the isolation of cloned DNAs that contain a specific gene
    • Grunstein, M. and Hogness, D.S. (1975) Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc. Natl. Acad. Sci. USA 72, 3961-3965.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3961-3965
    • Grunstein, M.1    Hogness, D.S.2
  • 14
    • 0032693153 scopus 로고    scopus 로고
    • Biotransformation of eugenol to vanillin by a mutant of Pseudomonas sp. strain HR199 constructed by disruption of the vanillin dehydrogenase (vdh) gene
    • Overhage, J., Priefert, H., Rabenhorst, J. and Steinbüchel, A. (1999) Biotransformation of eugenol to vanillin by a mutant of Pseudomonas sp. strain HR199 constructed by disruption of the vanillin dehydrogenase (vdh) gene. Appl. Microbiol. Biotechnol. 52, 820-828.
    • (1999) Appl. Microbiol. Biotechnol. , vol.52 , pp. 820-828
    • Overhage, J.1    Priefert, H.2    Rabenhorst, J.3    Steinbüchel, A.4
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0025124122 scopus 로고
    • Formation of blends of various poly(3-hydroxyalkanoic acids) by a recombinant strain of Pseudomonas oleovorans
    • Timm, A., Byrom, D. and Steinbüchel, A. (1990) Formation of blends of various poly(3-hydroxyalkanoic acids) by a recombinant strain of Pseudomonas oleovorans. Appl. Microbiol. Biotechnol. 33, 296-301.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 296-301
    • Timm, A.1    Byrom, D.2    Steinbüchel, A.3
  • 18
    • 0014560279 scopus 로고
    • Oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii: Purification and characterization
    • Chung, A.E. and Franzen, J.S. (1969) Oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii: purification and characterization. Biochemistry 8, 3175-3184.
    • (1969) Biochemistry , vol.8 , pp. 3175-3184
    • Chung, A.E.1    Franzen, J.S.2
  • 19
    • 0026075229 scopus 로고
    • Purification and characterization of a monomeric isocitrate dehydrogenase with dual coenzyme specificity from the photosynthetic bacterium, Rhodomicrobium vannielii
    • Leyland, M.L. and Kelly, D. (1991) Purification and characterization of a monomeric isocitrate dehydrogenase with dual coenzyme specificity from the photosynthetic bacterium, Rhodomicrobium vannielii. Eur. J. Biochem. 202, 85-93.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 85-93
    • Leyland, M.L.1    Kelly, D.2
  • 20
    • 0032961383 scopus 로고    scopus 로고
    • Cis-acting elements responsible for low-temperature-inducible expression of the gene coding for the thermolabile isocitrate dehydrogenase isozyme of a psychrophilic bacterium, Vibrio sp. strain ABE-1
    • Sahara, T., Suzuki, M., Tsuruha, J.I., Takada, Y. and Fukunaga, N. (1999) Cis-acting elements responsible for low-temperature-inducible expression of the gene coding for the thermolabile isocitrate dehydrogenase isozyme of a psychrophilic bacterium, Vibrio sp. strain ABE-1. J. Bacteriol. 181, 2602-2611.
    • (1999) J. Bacteriol. , vol.181 , pp. 2602-2611
    • Sahara, T.1    Suzuki, M.2    Tsuruha, J.I.3    Takada, Y.4    Fukunaga, N.5
  • 23
    • 0023703923 scopus 로고
    • Glyoxylate bypass operon of Escherichia coli: Cloning and determination of the functional map
    • Chung, T., Klumpp, D.J. and LaPorte, D.C. (1988) Glyoxylate bypass operon of Escherichia coli: cloning and determination of the functional map. J. Bacteriol. 170, 386-392.
    • (1988) J. Bacteriol. , vol.170 , pp. 386-392
    • Chung, T.1    Klumpp, D.J.2    Laporte, D.C.3
  • 24
    • 0033046562 scopus 로고    scopus 로고
    • Metabolic engineering of poly(3-hydroxyalkanoates): From DNA to plastic
    • Madison, L.L. and Huisman, G.W. (1999) Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic. Microbiol. Mol. Biol. Rev. 63, 21-53.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 21-53
    • Madison, L.L.1    Huisman, G.W.2
  • 25
    • 0034104601 scopus 로고    scopus 로고
    • Inactivation of isocitrate lyase leads to increased production of medium-chain-length poly(3-hydroxyalkanoates) in Pseudomonas putida
    • Klinke, S., Dauner, M., Scott, G., Kessler, B. and Witholt, B. (2000) Inactivation of isocitrate lyase leads to increased production of medium-chain-length poly(3-hydroxyalkanoates) in Pseudomonas putida. Appl. Environ. Microbiol. 66, 909-913.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 909-913
    • Klinke, S.1    Dauner, M.2    Scott, G.3    Kessler, B.4    Witholt, B.5
  • 26
    • 0029969492 scopus 로고    scopus 로고
    • Metabolic characteristics of isocitrate dehydrogenase leaky mutant of Alcaligenes eutrophus and its utilization for poly-β-hydroxybutyrate production
    • Park, J.S. and Lee, Y.H. (1996) Metabolic characteristics of isocitrate dehydrogenase leaky mutant of Alcaligenes eutrophus and its utilization for poly-β-hydroxybutyrate production. J. Ferment. Bioeng. 81, 197-205.
    • (1996) J. Ferment. Bioeng. , vol.81 , pp. 197-205
    • Park, J.S.1    Lee, Y.H.2
  • 27
    • 0019997397 scopus 로고
    • Mutagenesis of Alcaligenes eutrophus by insertion of the drug-resistance transposon Tn5
    • Srivastava, S., Urban, M. and Friedrich, B. (1982) Mutagenesis of Alcaligenes eutrophus by insertion of the drug-resistance transposon Tn5. Arch. Microbiol. 131, 203-207.
    • (1982) Arch. Microbiol. , vol.131 , pp. 203-207
    • Srivastava, S.1    Urban, M.2    Friedrich, B.3
  • 28
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection
    • Bullock, W.O., Fernandez, J.M. and Stuart, J.M. (1987) XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection. Biotechniques 5, 376-379.
    • (1987) Biotechniques , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Stuart, J.M.3
  • 29
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria
    • Simon, R., Priefer, U. and Pühler, A. (1983) A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Biotechnology 1, 781-791.
    • (1983) Biotechnology , vol.1 , pp. 781-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 30
    • 0019186616 scopus 로고
    • A small cosmid for efficient cloning of large DNA fragments
    • Hohn, C. and Collins, J. (1980) A small cosmid for efficient cloning of large DNA fragments. Gene 11, 291-298.
    • (1980) Gene , vol.11 , pp. 291-298
    • Hohn, C.1    Collins, J.2
  • 31
    • 0002433715 scopus 로고
    • Vector plasmids for in vivo and in vitro manipulations of Gram negative bacteria
    • (Pühler, A., Ed.). Springer, Berlin
    • Simon, R., Priefer, U. and Pühler, A. (1983) Vector plasmids for in vivo and in vitro manipulations of Gram negative bacteria. In: Molecular Genetics of the Bacteria/plant Interaction (Pühler, A., Ed.). Springer, Berlin.
    • (1983) Molecular Genetics of the Bacteria/plant Interaction
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 32
    • 0028329566 scopus 로고
    • Control of polyhydroxyalkanoate synthesis in Azotobacter vinelandii stain UWD
    • Manchak, J. and Page, W.J. (1994) Control of polyhydroxyalkanoate synthesis in Azotobacter vinelandii stain UWD. Microbiology 140, 953-963.
    • (1994) Microbiology , vol.140 , pp. 953-963
    • Manchak, J.1    Page, W.J.2
  • 33
    • 0037142769 scopus 로고    scopus 로고
    • Metabolic pathway analysis of a recombinant yeast for rational strain development
    • Carlson, R., Fell, D. and Srienc, F. (2002) Metabolic pathway analysis of a recombinant yeast for rational strain development. Biotechnol. Bioeng. 79, 121-134.
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 121-134
    • Carlson, R.1    Fell, D.2    Srienc, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.