메뉴 건너뛰기




Volumn 29, Issue 4, 1998, Pages 945-954

A glycyl radical solution: Oxygen-dependent interconversion of pyruvate formate-lyase

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A; BACTERIAL ENZYME; FORMIC ACID; LYASE;

EID: 0031866036     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00941.x     Document Type: Review
Times cited : (108)

References (33)
  • 1
    • 0020433094 scopus 로고
    • Involvement of oxygen-sensitive pyruvate formate-lyase in mixed-acid fermentation by Streptococcus mutans under strictly anaerobic conditions
    • Abbe, K., Takahashi, S., and Yamada, T. (1982) Involvement of oxygen-sensitive pyruvate formate-lyase in mixed-acid fermentation by Streptococcus mutans under strictly anaerobic conditions. J Bacteriol 152: 175-182.
    • (1982) J Bacteriol , vol.152 , pp. 175-182
    • Abbe, K.1    Takahashi, S.2    Yamada, T.3
  • 3
    • 0030924033 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of the Lactococcus lactis pfl gene, encoding pyruvate formate-lyase
    • Arnau, J., Jorgensen, F., Madsen, S.M., Vrang, A., and Israelsen, H. (1997) Cloning, expression, and characterization of the Lactococcus lactis pfl gene, encoding pyruvate formate-lyase. J Bacteriol 179: 5884-5891.
    • (1997) J Bacteriol , vol.179 , pp. 5884-5891
    • Arnau, J.1    Jorgensen, F.2    Madsen, S.M.3    Vrang, A.4    Israelsen, H.5
  • 4
    • 0025150580 scopus 로고
    • Sulfur-centered free radicals
    • Asmus, K.D. (1990) Sulfur-centered free radicals. Methods Enzymol 186: 168-180.
    • (1990) Methods Enzymol , vol.186 , pp. 168-180
    • Asmus, K.D.1
  • 7
    • 1242335574 scopus 로고
    • Covalent structure of biodegrative threonine dehydratase of Escherichia coli: Homology with other dehydratases
    • Datta, P., Goss, T.J., Omnass, J.R., and Patil, R.V. (1987) Covalent structure of biodegrative threonine dehydratase of Escherichia coli: homology with other dehydratases. Proc Natl Acad Sci USA 84: 393-397.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 393-397
    • Datta, P.1    Goss, T.J.2    Omnass, J.R.3    Patil, R.V.4
  • 10
    • 0030915255 scopus 로고    scopus 로고
    • HlyX, the FNR homologue of Actinobacillus pleuropneumoniae, is a [4Fe-4S]-containing oxygen-responsive transcription regulator that anaerobically activates FNR-dependent Class I promoters via an enhanced AR1 contact
    • Green, J., and Baldwin, M.L. (1997) HlyX, the FNR homologue of Actinobacillus pleuropneumoniae, is a [4Fe-4S]-containing oxygen-responsive transcription regulator that anaerobically activates FNR-dependent Class I promoters via an enhanced AR1 contact. Mol Microbiol 24: 593-605.
    • (1997) Mol Microbiol , vol.24 , pp. 593-605
    • Green, J.1    Baldwin, M.L.2
  • 11
    • 0029797082 scopus 로고    scopus 로고
    • Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic switch in vitro
    • Green, J., Bennett, B., Jordan, P., Ralph, E.T., Thomson, A.J., and Guest, J.R. (1996) Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic switch in vitro. Biochem J 316: 887-892.
    • (1996) Biochem J , vol.316 , pp. 887-892
    • Green, J.1    Bennett, B.2    Jordan, P.3    Ralph, E.T.4    Thomson, A.J.5    Guest, J.R.6
  • 12
    • 0031973793 scopus 로고    scopus 로고
    • Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate
    • Heβlinger, C., Fairhurst, S.A., and Sawers, G (1998) Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol Microbiol 27: 477-492.
    • (1998) Mol Microbiol , vol.27 , pp. 477-492
    • Helinger, C.1    Fairhurst, S.A.2    Sawers, G.3
  • 13
    • 0001465771 scopus 로고    scopus 로고
    • Anaerobic dissimilation of pyruvate
    • Neidhardt, F.C., Curtiss R., III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington DC: American Society for Microbiology Press
    • Kessler, D., and Knappe, J. (1996) Anaerobic dissimilation of pyruvate. In Escherichia coli and Salmonella: Cellular and Molecular Biology. Neidhardt, F.C., Curtiss R., III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington DC: American Society for Microbiology Press, pp. 199-205.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 199-205
    • Kessler, D.1    Knappe, J.2
  • 14
    • 0026662009 scopus 로고
    • Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli
    • Kessler, D., Herth, W., and Knappe, J. (1992) Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli. J Biol Chem 267: 18073-18079.
    • (1992) J Biol Chem , vol.267 , pp. 18073-18079
    • Kessler, D.1    Herth, W.2    Knappe, J.3
  • 16
    • 0027320421 scopus 로고
    • Pyruvate formate-lyase mechanism involving the protein-based glycyl radical
    • Knappe, J., Elbert, S., Frey, M., and Wagner, A.F.V. (1993) Pyruvate formate-lyase mechanism involving the protein-based glycyl radical. Biochem Soc Trans 21: 731-734.
    • (1993) Biochem Soc Trans , vol.21 , pp. 731-734
    • Knappe, J.1    Elbert, S.2    Frey, M.3    Wagner, A.F.V.4
  • 17
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk, H.P., Clayton, R.A., Tomb, J.F., White, O., Nelson, K.E., Ketchum, K.A., et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390: 364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3    White, O.4    Nelson, K.E.5    Ketchum, K.A.6
  • 18
    • 0038434902 scopus 로고    scopus 로고
    • Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme
    • Külzer, R., Pils, T., Kappl, R., Hüttermann, J., and Knappe, J. (1998) Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. J Biol Chem 273: 4897-4903.
    • (1998) J Biol Chem , vol.273 , pp. 4897-4903
    • Külzer, R.1    Pils, T.2    Kappl, R.3    Hüttermann, J.4    Knappe, J.5
  • 19
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera, B.A., Beinert, H., Khoroshilova, N., Kennedy, M.C., and Kiley, P.J. (1996) DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J Biol Chem 271: 2762-2768.
    • (1996) J Biol Chem , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 20
    • 0031980567 scopus 로고    scopus 로고
    • Biochemical and genetic characterisation of benzylsuccinate synthase from Thauera aromatica: A new gtycyl radical enzyme catalysing the first step in anaerobic toluene metabolism
    • Leuthner, B., Leutwein, C., Schulz, H., Hörth, P., Haehnel, W., Schiltz, E., et al. (1998) Biochemical and genetic characterisation of benzylsuccinate synthase from Thauera aromatica: a new gtycyl radical enzyme catalysing the first step in anaerobic toluene metabolism. Mol Microbiol 28: 615-628.
    • (1998) Mol Microbiol , vol.28 , pp. 615-628
    • Leuthner, B.1    Leutwein, C.2    Schulz, H.3    Hörth, P.4    Haehnel, W.5    Schiltz, E.6
  • 21
    • 0029006940 scopus 로고
    • Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate
    • Parast, C.V., Wong, K.K., and Kozarich, J.W. (1995) Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate. Biochemistry 34: 5712-5717.
    • (1995) Biochemistry , vol.34 , pp. 5712-5717
    • Parast, C.V.1    Wong, K.K.2    Kozarich, J.W.3
  • 22
    • 0031106730 scopus 로고    scopus 로고
    • The evolution of ribonucleotide reduction
    • Reichard, P. (1997) The evolution of ribonucleotide reduction. Trends Biochem 22: 81-85.
    • (1997) Trends Biochem , vol.22 , pp. 81-85
    • Reichard, P.1
  • 23
    • 0023776034 scopus 로고
    • Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate formate-lyase-activating enzyme deduced from the DNA nucleotide sequence
    • Rödel, W., Plaga, W., Frank, R., and Knappe, J. (1988) Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate formate-lyase-activating enzyme deduced from the DNA nucleotide sequence. Eur J Biochem 177: 153-158.
    • (1988) Eur J Biochem , vol.177 , pp. 153-158
    • Rödel, W.1    Plaga, W.2    Frank, R.3    Knappe, J.4
  • 24
    • 0025373543 scopus 로고
    • Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli
    • Sauter, M., and Sawers, G. (1990) Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli. Mol Microbiol 4: 355-363.
    • (1990) Mol Microbiol , vol.4 , pp. 355-363
    • Sauter, M.1    Sawers, G.2
  • 25
    • 0027490506 scopus 로고
    • Specific transcriptional requirements for positive regulation of the anaerobically inducible pfl operon by ArcA and FNR
    • Sawers, G. (1993) Specific transcriptional requirements for positive regulation of the anaerobically inducible pfl operon by ArcA and FNR. Mol Microbiol 10: 737-747.
    • (1993) Mol Microbiol , vol.10 , pp. 737-747
    • Sawers, G.1
  • 26
    • 0024670832 scopus 로고
    • Novel transcriptional control of the pyruvate formate-lyase gene: Upstream regulatory sequences and multiple promoters regulate ananerobic expression
    • Sawers, G., and Böck, A. (1989) Novel transcriptional control of the pyruvate formate-lyase gene: upstream regulatory sequences and multiple promoters regulate ananerobic expression. J Bacterial 171: 2485-2498.
    • (1989) J Bacterial , vol.171 , pp. 2485-2498
    • Sawers, G.1    Böck, A.2
  • 27
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: Functional analysis and comparative genetics
    • Smith, D.R., Doucette-Stamm, L.A., Deloughery, C., Lee, H., Dubois, J., Aldredge, T. et al. (1997) Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: functional analysis and comparative genetics. J Bacteriol 179: 7135-7155.
    • (1997) J Bacteriol , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3    Lee, H.4    Dubois, J.5    Aldredge, T.6
  • 28
    • 0028237747 scopus 로고
    • Isolation and characterization of hypophosphite-resistant mutants of Escherichia coli: Identification of the FocA protein, encoded by the pfl operon, as a putative formate transporter
    • Suppmann, B., and Sawers, G. (1994) Isolation and characterization of hypophosphite-resistant mutants of Escherichia coli: identification of the FocA protein, encoded by the pfl operon, as a putative formate transporter. Mol Microbiol 11: 965-982.
    • (1994) Mol Microbiol , vol.11 , pp. 965-982
    • Suppmann, B.1    Sawers, G.2
  • 29
    • 0015520637 scopus 로고
    • Properties and function of the pyruvate formate-lyase reaction in clostridiae
    • Thauer, R.K., Kirschniawy, F.S., and Jungermann, K.A. (1972) Properties and function of the pyruvate formate-lyase reaction in clostridiae. Eur J Biochem 27: 282-290.
    • (1972) Eur J Biochem , vol.27 , pp. 282-290
    • Thauer, R.K.1    Kirschniawy, F.S.2    Jungermann, K.A.3
  • 30
    • 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, D.G., and Gibson, T.J. (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: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0029882154 scopus 로고    scopus 로고
    • Molecular characterization of the genes encoding pyruvate formate-lyase and its activating enzyme of Clostridium pasteurianum
    • Weidner, G., and Sawers, G. (1996) Molecular characterization of the genes encoding pyruvate formate-lyase and its activating enzyme of Clostridium pasteurianum. J Bacteriol 178: 2440-2444.
    • (1996) J Bacteriol , vol.178 , pp. 2440-2444
    • Weidner, G.1    Sawers, G.2
  • 33
    • 0030061538 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the pfl gene encoding pyruvate formate-lyase from Streptococcus mutans
    • Yamamoto, Y., Sato, Y., Takahashi-Abbe, S., Abbe, K., Yamada, T., and Kizaki, H. (1996) Cloning and sequence analysis of the pfl gene encoding pyruvate formate-lyase from Streptococcus mutans. Infect Immun 64: 385-391.
    • (1996) Infect Immun , vol.64 , pp. 385-391
    • Yamamoto, Y.1    Sato, Y.2    Takahashi-Abbe, S.3    Abbe, K.4    Yamada, T.5    Kizaki, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.