메뉴 건너뛰기




Volumn 9, Issue 5, 2014, Pages

A closer look on the polyhydroxybutyrate- (PHB-) negative phenotype of Ralstonia eutropha PHB-4

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOACID DEHYDROGENASE; 2 OXOGLUTARATE DEHYDROGENASE COMPLEX; 3 ISOPROPYLMALATE DEHYDROGENASE; ACETOIN DEHYDROGENASE COMPLEX; ACETYL COENZYME A; ACETYL COENZYME A ACYLTRANSFERASE; ACETYL COENZYME A REDUCTASE; BACTERIAL PROTEIN; CITRATE SYNTHASE; DEMETHYLMENAQUINONE METHYLTRANSFERASE; HYDROXYBUTYRIC ACID; METHYLTRANSFERASE; OXIDOREDUCTASE; PHAC PROTEIN; POLYHYDROXYALKANOATE SYNTHASE; POLYHYDROXYBUTYRATE 4; PYRUVATE DEHYDROGENASE COMPLEX; PYRUVIC ACID; UNCLASSIFIED DRUG; POLY-BETA-HYDROXYBUTYRATE; POLYESTER;

EID: 84900419352     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0095907     Document Type: Article
Times cited : (42)

References (84)
  • 2
    • 0019364877 scopus 로고
    • Physiology and biochemistry of aerobic hydrogen-oxidizing bacteria
    • Bowien B, Schlegel HG (1981) Physiology and biochemistry of aerobic hydrogen-oxidizing bacteria. Annu Rev Microbiol 35:405-452.
    • (1981) Annu Rev Microbiol , vol.35 , pp. 405-452
    • Bowien, B.1    Schlegel, H.G.2
  • 3
    • 0000694310 scopus 로고
    • Genus Alcaligenes Castellani and Chalmers 1919
    • Krieg NR, Holt JG (ed) The Williams and Wilkins Co., Baltimore, MD
    • Kersters K, De Ley J (1984) Genus Alcaligenes Castellani and Chalmers 1919. In: Krieg NR, Holt JG (ed) Bergey's manual of systematic bacteriology, vol. 1. The Williams and Wilkins Co., Baltimore, MD. pp.361-373.
    • (1984) Bergey's Manual of Systematic Bacteriology , vol.1 , pp. 361-373
    • Kersters, K.1    De Ley, J.2
  • 4
    • 55249110895 scopus 로고    scopus 로고
    • Genomic view of energy metabolism in Ralstonia eutropha H16
    • Cramm R (2009) Genomic view of energy metabolism in Ralstonia eutropha H16. J Mol Microbiol Biotechnol 16:38-52.
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 38-52
    • Cramm, R.1
  • 5
    • 55249098183 scopus 로고    scopus 로고
    • Ralstonia eutropha strain H16 as model organism for PHA metabolism and for biotechnological production of technically interesting biopolymers
    • Reinecke F, Steinbüchel A (2009) Ralstonia eutropha strain H16 as model organism for PHA metabolism and for biotechnological production of technically interesting biopolymers. J Mol Microbiol Biotechnol 16:91-108.
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 91-108
    • Reinecke, F.1    Steinbüchel, A.2
  • 7
    • 0000862288 scopus 로고
    • Produits de deshydration et de polymerisation de lacide β-oxybutyrique
    • Paris
    • Lemoigne M, (1926) Produits de deshydration et de polymerisation de lacide β-oxybutyrique. Bull Soc Chim Bio (Paris) 8:770-782.
    • (1926) Bull Soc Chim Bio , vol.8 , pp. 770-782
    • Lemoigne, M.1
  • 8
    • 0025226099 scopus 로고
    • Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates
    • Anderson AJ, Dawes EA (1990) Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates. Microbiol Rev 54:450-472. (Pubitemid 120004382)
    • (1990) Microbiological Reviews , vol.54 , Issue.4 , pp. 450-472
    • Anderson, A.J.1    Dawes, E.A.2
  • 9
    • 0042344160 scopus 로고    scopus 로고
    • Bacterial and other biological systems for polyester production
    • Steinbüchel A, Füchtenbusch B (1998). Bacterial and other biological systems for polyester production. Trends Biotechnol 16:419-427.
    • (1998) Trends Biotechnol , vol.16 , pp. 419-427
    • Steinbüchel, A.1    Füchtenbusch, B.2
  • 10
    • 0017409907 scopus 로고
    • Micromorphology of gram-negative hydrogen bacteria. I. Cell morphology and flagellation
    • DOI 10.1007/BF00410769
    • Aragno M, Walther-Mauruschat A, Mayer F, Schlegel HG (1977) Micromorphology of Gram-negative hydrogen bacteria. I. Cell morphology and flagellation. Arch Microbiol 114:93-100. (Pubitemid 8167864)
    • (1977) Archives of Microbiology , vol.114 , Issue.2 , pp. 93-100
    • Aragno, M.1    Walther-Mauruschat, A.2    Mayer, F.3    Schlegel, H.G.4
  • 11
    • 0029018968 scopus 로고
    • Diversity of microbial polyhydroxyalkanoic acids
    • Steinbüchel A, Valentin HE (1995) Diversity of microbial polyhydroxyalkanoic acids. FEMS Microbiol Lett 128:219-228.
    • (1995) FEMS Microbiol Lett , vol.128 , pp. 219-228
    • Steinbüchel, A.1    Valentin, H.E.2
  • 13
    • 0024020072 scopus 로고
    • New bacterial copolyesters produced in Alcaligenes eutrophus from organic acids
    • Kunioka M, Nakamura Y, Doi Y (1988) New bacterial copolyesters produced in Alcaligenes eutrophus from organic acids. Polym Commun 29:174-176.
    • (1988) Polym Commun , vol.29 , pp. 174-176
    • Kunioka, M.1    Nakamura, Y.2    Doi, Y.3
  • 14
    • 0002473164 scopus 로고
    • Characterization of two 3-ketothiolases possessing differing substrate specificities in the polyhydroxyalcanoate synthesizing organism Alcaligenes eutrophus
    • Haywood GW, Anderson AJ, Dawes AE (1988) Characterization of two 3-ketothiolases possessing differing substrate specificities in the polyhydroxyalcanoate synthesizing organism Alcaligenes eutrophus . FEMS Microbiol Lett 52:259-264.
    • (1988) FEMS Microbiol Lett , vol.52 , pp. 259-264
    • Haywood, G.W.1    Anderson, A.J.2    Dawes, A.E.3
  • 15
    • 0002473164 scopus 로고
    • The role of NADH-and NADPH-linked acetoacetyl-CoA reductases in the poly-3-hydroxybutyrate synthesizing organism Alcaligenes eutrophus
    • Haywood GW, Anderson AJ, Chu L, Dawes AE (1988) The role of NADH-and NADPH-linked acetoacetyl-CoA reductases in the poly-3-hydroxybutyrate synthesizing organism Alcaligenes eutrophus. FEMS Microbiol Lett 52:259-264.
    • (1988) FEMS Microbiol Lett , vol.52 , pp. 259-264
    • Haywood, G.W.1    Anderson, A.J.2    Chu, L.3    Dawes, A.E.4
  • 16
    • 0002711454 scopus 로고
    • The importance of PHB synthase substrate specificity in polyhydroxyalkanoate synthesis by Alcaligenes eutrophus
    • Haywood GW, Anderson AJ, Dawes AE (1989). The importance of PHB synthase substrate specificity in polyhydroxyalkanoate synthesis by Alcaligenes eutrophus. FEMS Microbiol Lett 57:1-6.
    • (1989) FEMS Microbiol Lett , vol.57 , pp. 1-6
    • Haywood, G.W.1    Anderson, A.J.2    Dawes, A.E.3
  • 17
    • 0015839148 scopus 로고
    • β-Ketothiolase from Hydrogenomonas eutrophus H16 and its significance in the regulation of poly-β-hydroxybutyrate metabolism
    • Oeding V, Schlegel HG (1973) β-Ketothiolase from Hydrogenomonas eutrophus H16 and its significance in the regulation of poly-β- hydroxybutyrate metabolism. Biochem J 134:239-248.
    • (1973) Biochem J , vol.134 , pp. 239-248
    • Oeding, V.1    Schlegel, H.G.2
  • 18
    • 0024445845 scopus 로고
    • Poly-β-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding β-ketothiolase and acetoacetyl-CoA reductase
    • Peoples OP, Sinskey AJ (1989a) Poly-β-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding β-ketothiolase and acetoacetyl-CoA reductase. J Biol Chem 264:15293-15297. (Pubitemid 19242894)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.26 , pp. 15293-15297
    • Peoples, O.P.1    Sinskey, A.J.2
  • 19
    • 0024425823 scopus 로고
    • Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC)
    • Peoples OP, Sinskey AJ (1989b) Poly-β-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC). J Biol Chem 264:15298-15303. (Pubitemid 19242895)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.26 , pp. 15298-15303
    • Peoples, O.P.1    Sinskey, A.J.2
  • 20
    • 0024248526 scopus 로고
    • Cloning of the Alcaligenes eutrophus genes for synthesis of poly-β-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli
    • Schubert P, Steinbüchel A, Schlegel HG (1988) Cloning of the Alcaligenes eutrophus genes for synthesis of poly-β-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli. J Bacteriol 170:5837-5847.
    • (1988) J Bacteriol , vol.170 , pp. 5837-5847
    • Schubert, P.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 22
    • 84900407776 scopus 로고    scopus 로고
    • Multiple β-ketothiolase deletion mutants of Ralstonia eutropha: Impact on the composition of 3-mercaptopropionic acid containing copolymer
    • Lindenkamp N, Peplinski K, Volodina E, Ehrenreich A, Steinbüchel A (2010) Multiple β-ketothiolase deletion mutants of Ralstonia eutropha: impact on the composition of 3-mercaptopropionic acid containing copolymer. Appl Environ Microbiol 97:7699-7709.
    • (2010) Appl Environ Microbiol , vol.97 , pp. 7699-7709
    • Lindenkamp, N.1    Peplinski, K.2    Volodina, E.3    Ehrenreich, A.4    Steinbüchel, A.5
  • 24
    • 77954616682 scopus 로고    scopus 로고
    • Genome-wide transcriptome analyses of the "Knallgas" bacterium Ralstonia eutropha H16 with regard to polyhydroxyalkanoate metabolism
    • SGM
    • Peplinski K, Ehrenreich A, Döring C, Bömeke M, Reinecke F, et al. (2010) Genome-wide transcriptome analyses of the "Knallgas" bacterium Ralstonia eutropha H16 with regard to polyhydroxyalkanoate metabolism. Microbiology (SGM) 156:2136-2152.
    • (2010) Microbiology , vol.156 , pp. 2136-2152
    • Peplinski, K.1    Ehrenreich, A.2    Döring, C.3    Bömeke, M.4    Reinecke, F.5
  • 25
    • 0026033649 scopus 로고
    • Physiology and molecular genetics of poly(β-hydroxyalkanoic acid) synthesis in Alcaligenes eutrophus
    • Steinbüchel A, Schlegel HG (1991) Physiology and molecular genetics of poly(β-hydroxyalkanoic acid) synthesis in Alcaligenes eutrophus . Mol Microbiol 5:535-542. (Pubitemid 21896075)
    • (1991) Molecular Microbiology , vol.5 , Issue.3 , pp. 535-542
    • Steinbuchel, A.1    Schlegel, H.G.2
  • 26
    • 0344436087 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of PHA synthases and other proteins required for PHA synthesis
    • DOI 10.1016/S0141-8130(99)00010-0, PII S0141813099000100
    • Rehm BHA, Steinbüchel A (1999) Biochemical and genetic analysis of PHA synthases and other proteins required for PHA synthesis. Int J Biol Macromol 25:3-19. (Pubitemid 29301977)
    • (1999) International Journal of Biological Macromolecules , vol.25 , Issue.1-3 , pp. 3-19
    • Rehm, B.H.A.1    Steinbuchel, A.2
  • 27
    • 0005370966 scopus 로고    scopus 로고
    • PHA synthases: Key enzymes of PHA biosynthesis
    • Steinbüchel A, Doi, eds, Polyesters I, 3a. Wiley-VCH, Weinheim
    • Rehm BHA, Steinbüchel A (2001) PHA synthases: key enzymes of PHA biosynthesis. In: Biopolymers (Steinbüchel A, Doi, eds), Polyesters I, 3a. Wiley-VCH, Weinheim. pp. 173-215.
    • (2001) Biopolymers , pp. 173-215
    • Rehm, B.H.A.1    Steinbüchel, A.2
  • 28
    • 0035234192 scopus 로고    scopus 로고
    • Biochemical and molecular basis of microbial synthesis of polyhydroxyalkanoates in microorganisms
    • Steinbüchel A, Hein S (2001) Biochemical and molecular basis of microbial synthesis of polyhydroxyalkanoates in microorganisms. Adv Biochem Eng Biotechnol 71:81-123.
    • (2001) Adv Biochem Eng Biotechnol , vol.71 , pp. 81-123
    • Steinbüchel, A.1    Hein, S.2
  • 29
    • 0026709113 scopus 로고
    • Identification, cloning and sequence analysis of the poly(3- hydroxyalcanoic acid) synthase gene of the Gram-positive bacterium Rhodococcus ruber
    • Pieper U, Steinbüchel A (1992) Identification, cloning and sequence analysis of the poly(3-hydroxyalcanoic acid) synthase gene of the Gram-positive bacterium Rhodococcus ruber. FEMS Microbiol Lett 96:73-80.
    • (1992) FEMS Microbiol Lett , vol.96 , pp. 73-80
    • Pieper, U.1    Steinbüchel, A.2
  • 30
    • 0027278889 scopus 로고
    • Cloning and characterization of the Methylobacterium extorquens polyhydroxyalkanoic-acid-synthase structural gene
    • Valentin HE, Steinbüchel A (1993) Cloning and characterization of the Methylobacterium extorquens polyhydroxyalkanoic acid synthase structural gene. Appl Microbiol Biotechnol 39:309-317. (Pubitemid 23167180)
    • (1993) Applied Microbiology and Biotechnology , vol.39 , Issue.3 , pp. 309-317
    • Valentin, H.E.1    Steinbuchel, A.2
  • 31
  • 32
    • 0025002088 scopus 로고
    • Formation of polyesters consisting of medium-chain-length 3-hydroxyalkanoic acids from gluconate by Pseudomonas aeruginosa and other fluorescent pseudomonads
    • Timm A, Steinbüchel A (1990) Formation of polyesters consisting of medium-chain-length 3-hydroxyalkanoic acids from gluconate by Pseudomonas aeruginosa and other fluorescent pseudomonads. Appl Environ Microbiol 56:3360-3367. (Pubitemid 20380710)
    • (1990) Applied and Environmental Microbiology , vol.56 , Issue.11 , pp. 3360-3367
    • Timm, A.1    Steinbuchel, A.2
  • 33
    • 0027032280 scopus 로고
    • Isolation and identification of granule-associated proteins relevant for poly(3-hydroxyalkanoic acid) biosynthesis in Chromatium vinosum D
    • Liebergesell M, Schmidt B, Steinbüchel A (1992) Isolation and identification of granule associated proteins relevant for poly(hydroxyalkanoic acid) biosynthesis in Chromatium vinosum D. FEMS Microbiol Lett 78:227-232. (Pubitemid 23000259)
    • (1992) FEMS Microbiology Letters , vol.99 , Issue.2-3 , pp. 227-232
    • Liebergesell, M.1    Schmidt, B.2    Steinbuchel, A.3
  • 34
    • 0034967745 scopus 로고    scopus 로고
    • PhaC and PhaR are required for polyhydroxyalkanoic acid synthase activity in Bacillus megaterium
    • DOI 10.1128/JB.183.14.4235-4243.2001
    • McCool GJ, Cannon MC (2001) PhaC and PhaR are required for polyhydroxyalkanoic acid synthase activity in Bacillus megaterium. J Bacteriol 183: 4235-4243. (Pubitemid 32568075)
    • (2001) Journal of Bacteriology , vol.183 , Issue.14 , pp. 4235-4243
    • McCool, G.J.1    Cannon, M.C.2
  • 35
    • 0035155574 scopus 로고    scopus 로고
    • Identification of a new class of biopolymer: Bacterial synthesis of a sulfur containing polymer with thioester linkages
    • SGM
    • Lütke-Eversloh T, Bergander K, Luftmann H, Steinbüchel A (2001) Identification of a new class of biopolymer: bacterial synthesis of a sulfur containing polymer with thioester linkages. Microbiology (SGM) 147:11-19.
    • (2001) Microbiology , vol.147 , pp. 11-19
    • Lütke-Eversloh, T.1    Bergander, K.2    Luftmann, H.3    Steinbüchel, A.4
  • 36
    • 0003092872 scopus 로고
    • Novel energy and carbon sources. A. The production of biomass from hydrogen and carbon dioxide
    • Schlegel HG, Lafferty RM (1971) Novel energy and carbon sources. A. The production of biomass from hydrogen and carbon dioxide. Adv Biochem Eng 1: 143-168.
    • (1971) Adv Biochem Eng , vol.1 , pp. 143-168
    • Schlegel, H.G.1    Lafferty, R.M.2
  • 37
    • 0015457787 scopus 로고
    • The microbe as a source of food
    • Kihlberg R (1972) The microbe as a source of food. Annu Rev Microbiol 26: 427-466.
    • (1972) Annu Rev Microbiol , vol.26 , pp. 427-466
    • Kihlberg, R.1
  • 38
    • 0014722272 scopus 로고
    • The isolation of mutants not accumulating poly-β-hydroxybutyric acid
    • Schlegel HG, Lafferty R, Krauss I (1970a) The isolation of mutants not accumulating poly-β-hydroxybutyric acid. Arch Mikrobiol 71: 283-294.
    • (1970) Arch Mikrobiol , vol.71 , pp. 283-294
    • Schlegel, H.G.1    Lafferty, R.2    Krauss, I.3
  • 39
    • 0014947663 scopus 로고
    • Bacterial mutants of Hydrogenomonas lacking poly-β-hydroxybutyric acid
    • Schlegel HG, Lafferty R, Krauss I (1970b) Bacterial mutants of Hydrogenomonas lacking poly-β-hydroxybutyric acid. Experientia 26: 554-555.
    • (1970) Experientia , vol.26 , pp. 554-555
    • Schlegel, H.G.1    Lafferty, R.2    Krauss, I.3
  • 40
    • 44949155313 scopus 로고    scopus 로고
    • Targeted engineering of Cupriavidus necator chromosome for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from vegetable oil
    • Mifune J, Nakamura S, Fukui T (2008) Targeted engineering of Cupriavidus necator chromosome for biosynthesis of poly(3-hydroxybutyrate-co-3- hydroxyhexanoate) from vegetable oil. Can J Chem 86:621-627.
    • (2008) Can J Chem , vol.86 , pp. 621-627
    • Mifune, J.1    Nakamura, S.2    Fukui, T.3
  • 41
    • 34250969714 scopus 로고
    • Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen
    • Schlegel HG, Kaltwasser H, 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
  • 43
    • 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
  • 44
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim HC, Doly J (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acid Res 7:1513-1523.
    • (1979) Nucleic Acid Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 45
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl Acids Symp Ser 41:95-98.
    • (1999) Nucl Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 46
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166:557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J D, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-80. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 84864719646 scopus 로고    scopus 로고
    • Ralstonia eutropha H16 flagellation changes according to nutrient supply and state of poly(3-hydroxybutyrate) accumulation
    • Raberg M, Reinecke F, Reichelt R, Malkus U, König S, et al. (2008) Ralstonia eutropha H16 flagellation changes according to nutrient supply and state of poly(3-hydroxybutyrate) accumulation. Appl Environ Microbiol 62:2540-2546.
    • (2008) Appl Environ Microbiol , vol.62 , pp. 2540-2546
    • Raberg, M.1    Reinecke, F.2    Reichelt, R.3    Malkus, U.4    König, S.5
  • 50
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-25.
    • (1976) Anal Biochem , vol.72 , pp. 248-325
    • Bradford, M.M.1
  • 51
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, Wilm O, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, O.2    Vorm, O.3    Mann, M.4
  • 52
    • 31344470498 scopus 로고    scopus 로고
    • The extracellular proteome of Bacillus licheniformis grown in different media and under different nutrient starvation conditions
    • Voigt B, Schweder T, Sibbald MJ, Albrecht D, Ehrenreich A, et al. (2006) The extracellular proteome of Bacillus licheniformis grown in different media and under different nutrient starvation conditions. Proteomics 6:268-28.
    • (2006) Proteomics , vol.6 , pp. 268-328
    • Voigt, B.1    Schweder, T.2    Sibbald, M.J.3    Albrecht, D.4    Ehrenreich, A.5
  • 53
    • 4344627575 scopus 로고    scopus 로고
    • The complex structure of polyhydroxybutyrate (PHB) granules: Four orthologous and paralogous phasins occur in Ralstonia eutropha
    • Pötter M, Müller H, Reinecke F, Wieczorek R, Fricke F, et al. (2004) The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha. Microbiology (SGM) 150:2301-2311. (Pubitemid 39117642)
    • (2004) Microbiology , vol.150 , Issue.7 , pp. 2301-2311
    • Potter, M.1    Muller, H.2    Reinecke, F.3    Wieczorek, R.4    Fricke, F.5    Bowien, B.6    Friedrich, B.7    Steinbuchel, A.8
  • 54
    • 80053443148 scopus 로고    scopus 로고
    • Interaction between poly(3-hydroxybutyrate) granule-associated proteins as revealed by two-hybrid analysis and identification of a new phasin in Ralstonia eutropha H16
    • SGM
    • Pfeiffer D, Jendrossek D (2011) Interaction between poly(3- hydroxybutyrate) granule-associated proteins as revealed by two-hybrid analysis and identification of a new phasin in Ralstonia eutropha H16. Microbiology (SGM) 157:2795-2807.
    • (2011) Microbiology , vol.157 , pp. 2795-2807
    • Pfeiffer, D.1    Jendrossek, D.2
  • 55
    • 84868620054 scopus 로고    scopus 로고
    • Localization of poly(3-hydroxybutyrate) (PHB) granule-associated proteins during PHB granule formation and identification of two new phasins, PhaP6 and PhaP7, in Ralstonia eutropha H16
    • Pfeiffer D, Jendrossek D (2012) Localization of poly(3-hydroxybutyrate) (PHB) granule-associated proteins during PHB granule formation and identification of two new phasins, PhaP6 and PhaP7, in Ralstonia eutropha H16. J Bacteriol 194:5909-5921.
    • (2012) J Bacteriol , vol.194 , pp. 5909-5921
    • Pfeiffer, D.1    Jendrossek, D.2
  • 56
    • 0029039870 scopus 로고
    • Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus
    • Wieczorek R, Pries A, Steinbüchel A, Mayer F (1995) Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus. J Bacteriol 177:2425-2.
    • (1995) J Bacteriol , vol.177 , pp. 2425-2432
    • Wieczorek, R.1    Pries, A.2    Steinbüchel, A.3    Mayer, F.4
  • 57
    • 0035861886 scopus 로고    scopus 로고
    • A new family of CoA-transferases
    • Heider J (2001) A new family of CoA-transferases. FEBS Lett 509:345-349.
    • (2001) FEBS Lett , vol.509 , pp. 345-349
    • Heider, J.1
  • 58
    • 0032813519 scopus 로고    scopus 로고
    • Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
    • DOI 10.1038/11563
    • Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG (1999) Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat Struct Biol 6:785-792. (Pubitemid 29360241)
    • (1999) Nature Structural Biology , vol.6 , Issue.8 , pp. 785-792
    • Aevarsson, A.1    Seger, K.2    Turley, S.3    Sokatch, J.R.4    Hol, W.G.J.5
  • 59
    • 0033960004 scopus 로고    scopus 로고
    • Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase
    • Knapp JE, Carroll D, Lawson JE, Ernst SR, Reed LJ, et al. (2000) Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase. Protein Sci 9:37-48. (Pubitemid 30070937)
    • (2000) Protein Science , vol.9 , Issue.1 , pp. 37-48
    • Knapp, J.E.1    Carroll, D.2    Lawson, J.E.3    Ernst, S.R.4    Reed, L.J.5    Hackert, M.L.6
  • 60
    • 0024358061 scopus 로고
    • Biochemical and genetic analyses of acetoin catabolism in Alcaligenes eutrophus
    • Fründ C, Priefert H, Steinbüchel A, Schlegel HG (1989) Biochemical and genetic analyses of acetoin catabolism in Alcaligenes eutrophus. J Bacteriol 171:6539-6548. (Pubitemid 20006933)
    • (1989) Journal of Bacteriology , vol.171 , Issue.12 , pp. 6539-6548
    • Frund, C.1    Priefert, H.2    Steinbuchel, A.3    Schlegel, H.G.4
  • 61
    • 0026086021 scopus 로고
    • Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system
    • Oppermann FB, Schmidt B, Steinbüchel A (1991) Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J Bacteriol 173:757-767.
    • (1991) J Bacteriol , vol.173 , pp. 757-767
    • Oppermann, F.B.1    Schmidt, B.2    Steinbüchel, A.3
  • 62
    • 0024320832 scopus 로고
    • The thiM locus and its relation to phosphorylation of hydroxyethylthiazole in Escherichia coli
    • Mizote T, Nakayama H (1989) The thiM locus and its relation to phosphorylation of hydroxethylthiazole in Escherichia coli. J Bacteriol 171: 3228-3232. (Pubitemid 19145677)
    • (1989) Journal of Bacteriology , vol.171 , Issue.6 , pp. 3228-3232
    • Mizote, T.1    Nakayama, H.2
  • 63
    • 0037161258 scopus 로고    scopus 로고
    • Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 Å resolution
    • DOI 10.1021/bi0118557
    • Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, et al. (2002) Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 Å resolution. Biochemistry 41:5213-5221. (Pubitemid 34411676)
    • (2002) Biochemistry , vol.41 , Issue.16 , pp. 5213-5221
    • Arjunan, P.1    Nemeria, N.2    Brunskill, A.3    Chandrasekhar, K.4    Sax, M.5    Yan, Y.6    Jordan, F.7    Guest, J.R.8    Furey, W.9
  • 65
    • 0017759115 scopus 로고
    • Characterization of the isolated transferase subunit of citrate lyase as a CoA transferase. Evidence against a covalent enzyme substrate intermediate
    • Dimroth P, Loyal R, Eggerer H (1977) Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate. Eur J Biochem 80: 479-88. (Pubitemid 8218220)
    • (1977) European Journal of Biochemistry , vol.80 , Issue.2 , pp. 479-488
    • Dimroth, P.1    Loyal, R.2    Eggerer, H.3
  • 66
    • 0001046363 scopus 로고
    • Coenzyme A transferase. Kinetics and exchange reactions
    • Hersh LB, Jencks WP (1967) Coenzyme A transferase. Kinetics and exchange reactions. J Biol Chem 242: 3468-3480.
    • (1967) J Biol Chem , vol.242 , pp. 3468-3480
    • Hersh, L.B.1    Jencks, W.P.2
  • 67
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: Natural catalysts for plastics
    • Rehm BHA (2003) Polyester synthases: natural catalysts for plastics. Biochem J 376:15-33.
    • (2003) Biochem J , vol.376 , pp. 15-33
    • Rehm, B.H.A.1
  • 68
    • 0001603904 scopus 로고
    • Genetic engineering of PHB synthase from Alcaligenes eutrophus H16
    • Kalousek S, Dennis D, Lubitz W (1992) Genetic engineering of PHB synthase from Alcaligenes eutrophus H16. FEMS Microbiol Rev 103:426-427.
    • (1992) FEMS Microbiol Rev , vol.103 , pp. 426-427
    • Kalousek, S.1    Dennis, D.2    Lubitz, W.3
  • 69
    • 0037203912 scopus 로고    scopus 로고
    • Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: In vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model
    • DOI 10.1016/S0167-4838(01)00299-0, PII S0167483801002990
    • Rehm BHA, Antonio RV, Spiekermann P, Amara AA, Steinbüchel A (2002) Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: in vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model. Biochim Biophys Acta 1594:178-190. (Pubitemid 34131737)
    • (2002) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1594 , Issue.1 , pp. 178-190
    • Rehm, B.H.A.1    Antonio, R.V.2    Spiekermann, P.3    Amara, A.A.4    Steinbuchel, A.5
  • 70
    • 0035917520 scopus 로고    scopus 로고
    • Analysis of mutational effects of a polyhydroxybutyrate (PHB) polymerase on bacterial PHB accumulation using an in vivo assay system
    • DOI 10.1016/S0378-1097(01)00125-2, PII S0378109701001252
    • Taguchi S, Maehara A, Takase K, Nakahara M, Nakamura H, et al. (2001) Analysis of mutational effects of a polyhydroxybutyrate (PHB) polymerase on bacterial PHB accumulation using an in vivo assay system. FEMS Microbiol Lett 198:65-71. (Pubitemid 32452242)
    • (2001) FEMS Microbiology Letters , vol.198 , Issue.1 , pp. 65-71
    • Taguchi, S.1    Maehara, A.2    Takase, K.3    Nakahara, M.4    Nakamura, H.5    Doi, Y.6
  • 71
    • 0018133572 scopus 로고
    • Metabolite concentrations in Alcaligenes eutrophus H 16 and a mutant defective in poly-hydroxybutyrate synthesis
    • Cook AM, Schlegel HG (1978) Metabolite concentrations in Alcaligenes eutrophus H16 and a mutant defective in polyhydroxybutyrate synthesis. Arch Microbiol 119:231-235. (Pubitemid 9077863)
    • (1978) Archives of Microbiology , vol.119 , Issue.3 , pp. 231-235
    • Cook, A.M.1    Schlegel, H.G.2
  • 72
    • 0000001045 scopus 로고    scopus 로고
    • Investigation of regulatory mechanism of flux of acetyl-CoA in Alcaligenes eutrophus using PHB negative mutant and transformants harboring cloned phbCAB genes
    • Jung YM, Lee YH (1997) Investigation of regulatory mechanism of flux of acetyl-CoA in Alcaligenes eutrophus using PHB negative mutant and transformants harboring cloned phbCAB genes. J Microbiol Biotechnol 7:215-22.
    • (1997) J Microbiol Biotechnol , vol.7 , pp. 215-222
    • Jung, Y.M.1    Lee, Y.H.2
  • 73
    • 0001646868 scopus 로고
    • Excretion of pyruvate by mutants of Alcaligenes eutrophus, which are impaired in the accumulation of poly(β-hydroxybutyric acid) (PHB), under conditions permitting synthesis of PHB
    • Steinbüchel A, Schlegel HG (1989) Excretion of pyruvate by mutants of Alcaligenes eutrophus, which are impaired in the accumulation of poly(β-hydroxybutyric acid) (PHB), under conditions permitting synthesis of PHB. Appl Microbiol Biotechnol 31:168-175.
    • (1989) Appl Microbiol Biotechnol , vol.31 , pp. 168-175
    • Steinbüchel, A.1    Schlegel, H.G.2
  • 75
    • 0000572930 scopus 로고
    • Pyruvic acid production from 1,2-propandiol by thiamine requiring A cinetobacter sp 80-M
    • Izumi Y, Matsumura Y, Tani Y, Yamada H (1982) Pyruvic acid production from 1,2-propandiol by thiamine requiring A cinetobacter sp 80-M. Agric Biol Chem 46:2673-2678.
    • (1982) Agric Biol Chem , vol.46 , pp. 2673-2678
    • Izumi, Y.1    Matsumura, Y.2    Tani, Y.3    Yamada, H.4
  • 76
    • 0043169022 scopus 로고
    • Wirkungsmechanismus von Thiaminpyrophosphat
    • Holzer H (1961) Wirkungsmechanismus von Thiaminpyrophosphat. Angew Chem 73:721-727.
    • (1961) Angew Chem , vol.73 , pp. 721-727
    • Holzer, H.1
  • 77
    • 34250166461 scopus 로고    scopus 로고
    • Acetoin metabolism in bacteria
    • DOI 10.1080/10408410701364604, PII 779367204
    • Xiao Z, Xu P, (2007) Acetoin metabolism in bacteria. Crit Rev Biochem Microbiol 33:127-140. (Pubitemid 46897713)
    • (2007) Critical Reviews in Microbiology , vol.33 , Issue.2 , pp. 127-140
    • Xiao, Z.1    Xu, P.2
  • 78
    • 79953268441 scopus 로고    scopus 로고
    • Versatile metabolic adaptations of Ralstonia eutropha H16 to a loss of PdhL, the E3 component of the pyruvate dehydrogenase complex
    • Raberg M, Bechmann J. Brandt U, Schlüter J, Uischner B, et al. (2011) Versatile metabolic adaptations of Ralstonia eutropha H16 to a loss of PdhL, the E3 component of the pyruvate dehydrogenase complex. Appl Environ Microbiol 77:2254-2263.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 2254-2263
    • Raberg, M.1    Bechmann, J.2    Brandt, U.3    Schlüter, J.4    Uischner, B.5
  • 81
    • 84883817711 scopus 로고    scopus 로고
    • A propionate CoA-transferase of Ralstonia eutropha H16 with broad substrate specificity catalyzing the CoA thioester formation of various carboxylic acids
    • Lindenkamp N, Schürmann M, Steinbüchel A (2012) A propionate CoA-transferase of Ralstonia eutropha H16 with broad substrate specificity catalyzing the CoA thioester formation of various carboxylic acids. Appl Microbiol Biotechnol 97:7699-7709.
    • (2012) Appl Microbiol Biotechnol , vol.97 , pp. 7699-7709
    • Lindenkamp, N.1    Schürmann, M.2    Steinbüchel, A.3
  • 82
    • 0031038898 scopus 로고    scopus 로고
    • A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: Isolation and identification of the Escherichia coli ubiE gene
    • Lee PT, Hsu AY, Ha HT, Clarke CF (1997) A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J Bacteriol 179:1748-1754. (Pubitemid 27100466)
    • (1997) Journal of Bacteriology , vol.179 , Issue.5 , pp. 1748-1754
    • Lee, P.T.1    Hsu, A.Y.2    Ha, H.T.3    Clarke, C.F.4
  • 83
    • 0348194347 scopus 로고
    • The biosynthesis of leucine III. The conversion of α-hydroxy- βcarboxyisocaproate to α-ketoisocaproate
    • Burns RO, Umbarger HE, Gross SR (1963) The biosynthesis of leucine III. The conversion of α-hydroxy-βcarboxyisocaproate to α-ketoisocaproate. Biochemistry 2:1053-1058.
    • (1963) Biochemistry , vol.2 , pp. 1053-1058
    • Burns, R.O.1    Umbarger, H.E.2    Gross, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.