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Volumn 269, Issue 24, 2002, Pages 6184-6194

Oxidation of propionate to pyruvate in Escherichia coli: Involvement of methylcitrate dehydratase and aconitase

Author keywords

2 methylisocitrate; Aconitase; Methylcitrate dehydratase; Propionate metabolism; prp operon

Indexed keywords

ACONITATE HYDRATASE; METHYL GROUP; METHYLCITRATE DEHYDRATASE; PROPIONIC ACID; PROPIONYL COENZYME A; PROTEIN; PROTEIN ACNB; PROTEIN PRP; PYRUVIC ACID; RNA; SYNTHETASE; UNCLASSIFIED DRUG; WATER;

EID: 0036449408     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03336.x     Document Type: Article
Times cited : (104)

References (33)
  • 1
    • 0016217736 scopus 로고
    • A novel pathway for the partial oxidation of propionyl-CoA to pyruvate via seven-carbon tricarboxylic acids in yeast
    • Tabuchi, T., Serizawa, N. & Uchiyama, H. (1974) A novel pathway for the partial oxidation of propionyl-CoA to pyruvate via seven-carbon tricarboxylic acids in yeast. Agric. Biol. Chem. 38, 2571-2572.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 2571-2572
    • Tabuchi, T.1    Serizawa, N.2    Uchiyama, H.3
  • 3
    • 0017387623 scopus 로고
    • Purification and properties of methylisocitrate lyase. A key enzyme in propionate metabolism from Candida lipolytica
    • Tabuchi, T. & Satoh, T. (1977) Purification and properties of methylisocitrate lyase. A key enzyme in propionate metabolism from Candida lipolytica. Agric. Biol. Chem. 41, 169-174.
    • (1977) Agric. Biol. Chem. , vol.41 , pp. 169-174
    • Tabuchi, T.1    Satoh, T.2
  • 4
    • 0001430567 scopus 로고
    • 2-Methylcitrate dehydratase, a new enzyme functioning at the methylcitrate cycle of propionate metabolism
    • Tabuchi, T., Aoki, H., Uchiyama, H. & Nakahara, T. (1981) 2-Methylcitrate dehydratase, a new enzyme functioning at the methylcitrate cycle of propionate metabolism. Agric. Biol. Chem. 45, 2823-2829.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 2823-2829
    • Tabuchi, T.1    Aoki, H.2    Uchiyama, H.3    Nakahara, T.4
  • 5
    • 0029188391 scopus 로고
    • Characteristics of 2-methylisocitrate dehydratase, isolated from Yallowia lipolytica, in comparison with aconitase
    • Tabuchi, T., Umetsu, H., Aoki, H. & Uchiyama, H. (1995) Characteristics of 2-methylisocitrate dehydratase, isolated from Yallowia lipolytica, in comparison with aconitase. Biosci. Biotechnol. Biochem. 59, 2013-2017.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 2013-2017
    • Tabuchi, T.1    Umetsu, H.2    Aoki, H.3    Uchiyama, H.4
  • 6
    • 0029187871 scopus 로고
    • Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism from Yallowia lipolytica
    • Aoki, H., Uchiyama, H., Umetsu, H. & Tabuchi, T. (1995) Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism from Yallowia lipolytica. Biosci. Biotechnol. Biochem. 59, 1825-1828.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1825-1828
    • Aoki, H.1    Uchiyama, H.2    Umetsu, H.3    Tabuchi, T.4
  • 7
  • 8
    • 0032882589 scopus 로고    scopus 로고
    • Salmonella typhimurium LT2 catabolizes propionate via the 2- methylcitric acid cycle
    • Horswill, A.R. & Escalante-Semerena, J.C. (1999) Salmonella typhimurium LT2 catabolizes propionate via the 2- methylcitric acid cycle. J. Bacteriol. 181, 5615-5623.
    • (1999) J. Bacteriol. , vol.181 , pp. 5615-5623
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 9
    • 0034819414 scopus 로고    scopus 로고
    • 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: Characterization and comparison of both enzymes
    • Brock, M., Darley, D., Textor, S. & Buckel, W. (2001) 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: Characterization and comparison of both enzymes. Eur. J. Biochem. 268, 3577-3586.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3577-3586
    • Brock, M.1    Darley, D.2    Textor, S.3    Buckel, W.4
  • 10
    • 0033049615 scopus 로고    scopus 로고
    • The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase
    • Horswill, A.R. & Escalante-Semerena, J.C. (1999) The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase. Microbiology 145, 1381-1388.
    • (1999) Microbiology , vol.145 , pp. 1381-1388
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 11
    • 0035901535 scopus 로고    scopus 로고
    • In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate
    • Horswill, A.R. & Escalante-Semerena, J.C. (2001) In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate. Biochemistry 40, 4703-4713.
    • (2001) Biochemistry , vol.40 , pp. 4703-4713
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 12
    • 77956929977 scopus 로고
    • Stereochemistry of enzyme-catalysed reactions at carbon
    • Sigman, D.S. & Boyer, P.D., eds. Academic Press Inc., San Diego, USA
    • Creighton, D.J. & Murthy, N.R.S.K. (1990) Stereochemistry of enzyme-catalysed reactions at carbon. In The Enzymes, Vol. 19, 3rd Edn (Sigman, D.S. & Boyer, P.D., eds), pp. 324-421. Academic Press Inc., San Diego, USA.
    • (1990) The Enzymes, 3rd Edn , vol.19 , pp. 324-421
    • Creighton, D.J.1    Murthy, N.R.S.K.2
  • 13
    • 0017377138 scopus 로고
    • Identification of D-threo-alpha-methylisocitrate as stereochemically specific substrate for bovine heart aconitase and inhibitor of TPN-linked isocitrate dehydrogenase
    • Beach, R.L., Aogaichi, T. & Plaut, G.W. (1977) Identification of D-threo-alpha-methylisocitrate as stereochemically specific substrate for bovine heart aconitase and inhibitor of TPN-linked isocitrate dehydrogenase. J. Biol. Chem. 252, 2702-2709.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2702-2709
    • Beach, R.L.1    Aogaichi, T.2    Plaut, G.W.3
  • 14
    • 0036148845 scopus 로고    scopus 로고
    • AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates
    • Blank, L., Green, J. & Guest, J.R. (2002) AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates. Microbiology 148, 133-146.
    • (2002) Microbiology , vol.148 , pp. 133-146
    • Blank, L.1    Green, J.2    Guest, J.R.3
  • 15
    • 0002666144 scopus 로고
    • Sensitive mutants of bacteriophage lambda
    • Campbell, A. (1961) Sensitive mutants of bacteriophage lambda. Virology 14, 22-32.
    • (1961) Virology , vol.14 , pp. 22-32
    • Campbell, A.1
  • 16
    • 0001614970 scopus 로고
    • Gram-negative mesophilic sulfate reducing bacteria
    • Balows, A., Trüper, H.G., Dworkin, M., Harder, W. & Schleifer, K.-H., eds. Springer, Heidelberg, Germany
    • Widdel, F. & Bak, F. (1991) Gram-negative mesophilic sulfate reducing bacteria. In The Prokaryotes (Balows, A., Trüper, H.G., Dworkin, M., Harder, W. & Schleifer, K.-H., eds), pp. 3352-3378. Springer, Heidelberg, Germany.
    • (1991) The Prokaryotes , pp. 3352-3378
    • Widdel, F.1    Bak, F.2
  • 17
    • 0034095188 scopus 로고    scopus 로고
    • Methylcitrate synthase from Aspergillus nidulans: Implications for propionate as an antifungal agent
    • Brock, M., Fischer, R., Linder, D. & Buckel, W. (2000) Methyl-citrate synthase from Aspergillus nidulans: Implications for propionate as an antifungal agent. Mol. Microbiol. 35, 961-973.
    • (2000) Mol. Microbiol. , vol.35 , pp. 961-973
    • Brock, M.1    Fischer, R.2    Linder, D.3    Buckel, W.4
  • 18
    • 0001308238 scopus 로고
    • Preparation and assay of acetyl phosphate
    • Stadtman, E.R. (1969) Preparation and assay of acetyl phosphate. Methods Enzymol. 1, 228-231.
    • (1969) Methods Enzymol. , vol.1 , pp. 228-231
    • Stadtman, E.R.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0029854465 scopus 로고    scopus 로고
    • Identification of human myocardial proteins separated by two-dimensional electrophoresis using an effective sample preparation for mass spectrometry
    • Otto, A., Thiede, B., Muller, E.C., Scheler, C., Wittmann-Liebold, B. & Jungblut, P. (1996) Identification of human myocardial proteins separated by two-dimensional electrophoresis using an effective sample preparation for mass spectrometry. Electrophoresis 17, 1643-1650.
    • (1996) Electrophoresis , vol.17 , pp. 1643-1650
    • Otto, A.1    Thiede, B.2    Muller, E.C.3    Scheler, C.4    Wittmann-Liebold, B.5    Jungblut, P.6
  • 23
    • 0033572854 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)
    • Jordan, P.A., Tang, Y., Bradbury, A.J., Thomson, A.J. & Guest, J.R. (1999) Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB). Biochem. J. 344, 739-746.
    • (1999) Biochem. J. , vol.344 , pp. 739-746
    • Jordan, P.A.1    Tang, Y.2    Bradbury, A.J.3    Thomson, A.J.4    Guest, J.R.5
  • 24
    • 0021112587 scopus 로고
    • The role of iron in the activation-inactivation of aconitase
    • Kennedy, M.C., Emptage, M.H., Dreyer, J.L. & Beinert, H. (1983) The role of iron in the activation-inactivation of aconitase. J. Biol. Chem. 258, 11098-11105.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11098-11105
    • Kennedy, M.C.1    Emptage, M.H.2    Dreyer, J.L.3    Beinert, H.4
  • 25
    • 0024457799 scopus 로고
    • Assay and purification of the adenosylcobalamin-dependent 2-methyleneglutarate mutase from Clostridium barkeri
    • Michel, C., Hartrampf, G. & Buckel, W. (1989) Assay and purification of the adenosylcobalamin-dependent 2-methyleneglutarate mutase from Clostridium barkeri. Eur. J. Biochem. 184, 103-107.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 103-107
    • Michel, C.1    Hartrampf, G.2    Buckel, W.3
  • 27
    • 0030853330 scopus 로고    scopus 로고
    • Reduction of aerobic acetate production by Escherichia coli
    • Farmer, W.R. & Liao, J.C. (1997) Reduction of aerobic acetate production by Escherichia coli. Appl. Environ. Microbiol. 63, 3205-3210.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3205-3210
    • Farmer, W.R.1    Liao, J.C.2
  • 28
    • 0001628218 scopus 로고
    • Stereochemistry of Krebs' cycle hydrations and related reactions
    • Gawron, O., Glaid, A.J. & Fondy, T.P. (1961) Stereochemistry of Krebs' cycle hydrations and related reactions. J. Am. Chem. Soc. 83, 3634-3640.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 3634-3640
    • Gawron, O.1    Glaid, A.J.2    Fondy, T.P.3
  • 29
    • 0031438608 scopus 로고    scopus 로고
    • Transcriptional regulation of the aconitase genes (acnA and acnB) of Escherichia coli
    • Cunningham, L., Gruer, M.J. & Guest, J.R. (1997) Transcriptional regulation of the aconitase genes (acnA and acnB) of Escherichia coli. Microbiology 143, 3795-3805.
    • (1997) Microbiology , vol.143 , pp. 3795-3805
    • Cunningham, L.1    Gruer, M.J.2    Guest, J.R.3
  • 30
    • 0028588718 scopus 로고
    • Identification of the stereoisomeric configurations of methylcitric acid produced by Si-citrate synthase and methylcitrate synthase using capillary gas chromatography-mass spectrometry
    • van Rooyen, J.P., Mienie, L.J., Erasmus, E., De Wet, W.J., Ketting, D., Duran, M. & Wadman, S.K. (1994) Identification of the stereoisomeric configurations of methylcitric acid produced by Si-citrate synthase and methylcitrate synthase using capillary gas chromatography-mass spectrometry. J. Inherit. Metab. Dis. 17, 738-747.
    • (1994) J. Inherit. Metab. Dis. , vol.17 , pp. 738-747
    • Van Rooyen, J.P.1    Mienie, L.J.2    Erasmus, E.3    De Wet, W.J.4    Ketting, D.5    Duran, M.6    Wadman, S.K.7
  • 31
    • 0029052367 scopus 로고
    • Steric and conformational features of the aconitase mechanism
    • Lauble, H. & Stout, C.D. (1995) Steric and conformational features of the aconitase mechanism. Proteins 22, 1-11.
    • (1995) Proteins , vol.22 , pp. 1-11
    • Lauble, H.1    Stout, C.D.2
  • 32
    • 0034858524 scopus 로고    scopus 로고
    • The methylcitric acid pathway in Ralstonia eutropha: New genes identified involved in propionate metabolism
    • Brämer, C.O. & 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
  • 33
    • 0036091651 scopus 로고    scopus 로고
    • Glycerol-3-phosphate-induced catabolite repression in Escherichia coli
    • Eppler, T., Postma, P., Schütz, A., Völker, U. & Boos, W. (2002) Glycerol-3-phosphate-induced catabolite repression in Escherichia coli. J. Bacteriol. 184, 3044-3052.
    • (2002) J. Bacteriol. , vol.184 , pp. 3044-3052
    • Eppler, T.1    Postma, P.2    Schütz, A.3    Völker, U.4    Boos, W.5


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