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ECs2318  -  fumarase A

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs2318


High impact information on ECs2318


Chemical compound and disease context of ECs2318

  • We report here that E. coli fumarase A, fumarase B, and aconitase are also inactivated in vivo by hyperbaric O2 [7].
  • Escherichia coli fumarase A catalyzes the isomerization of enol and keto oxalacetic acid [10].
  • The level of fumarase activity in Bacillus subtilis depends on the nutritional environment; in rich medium low vegetative levels increase towards the end of the exponential phase, whereas in minimal glucose medium levels are relatively high throughout growth [11].

Biological context of ECs2318

  • A tungstate derivative used in the X-ray analysis is a competitive inhibitor and places the active site of fumarase in a region which includes atoms from three of the four subunits [12].
  • Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli [13].
  • Class I contains fumarases A and B, which have amino acid sequences that are 90% identical to each other, but have almost no similarity to the sequence of porcine fumarase [14].
  • The iron-containing FumA fumarase is the more abundant enzyme under most conditions of aerobic cell growth except when iron is limiting; FumC, which lacks iron, appears to be a backup enzyme that is synthesized optimally only when iron is low or when superoxide radicals accumulate [15].
  • Several other genes including the sdhA-D, sucA-D, and fumA genes, encoding key constituents of the Krebs cycle, proved to be repressed by the loss of both transcription factors [16].

Associations of ECs2318 with chemical compounds

  • The isomerization reaction apparently takes place at the same active site as the fumarase reaction since both reactions show a similar sensitivity to inactivation by O2, both reactions are strongly inhibited by 2-hydroxy-3-nitropropionate, and the isomerization reaction is inhibited by fumarate and malate [10].
  • In this work it is shown that purified fumarase A contains a [4Fe-4S] cluster [14].
  • Fumarase A and aconitase, two enzymes with 4Fe-4S clusters that bind a linear 4-carbon dicarboxylic acid moiety in the trans conformation during their normal hydro-lyase reaction, do catalyze this isomerization [10].
  • The A-site has been demonstrated by studying crystalline fumarase with the bound competitive inhibitors-citrate and 1,2,4,5-benzenetetracarboxylic acid [17].
  • (The mobility of fumarase A in native polyacrylamide gel electrophoresis and the elution volume on a gel permeation column indicate that it is a homodimer.) Its visible and circular dichroism spectra are characteristic of proteins containing an Fe-S cluster [14].

Analytical, diagnostic and therapeutic context of ECs2318


  1. The role of the allosteric B site in the fumarase reaction. Rose, I.A., Weaver, T.M. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  2. Complete nucleotide sequence of the fumarase gene (citG) of Bacillus subtilis 168. Miles, J.S., Guest, J.R. Nucleic Acids Res. (1985) [Pubmed]
  3. Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of Escherichia coli K-12. Bell, P.J., Andrews, S.C., Sivak, M.N., Guest, J.R. J. Bacteriol. (1989) [Pubmed]
  4. Cloning, mapping, and expression of the fumarase gene of Escherichia coli K-12. Guest, J.R., Roberts, R.E. J. Bacteriol. (1983) [Pubmed]
  5. Purification and characterization of fumarase from the syntrophic propionate-oxidizing bacterium strain MPOB. Van Kuijk, B.L., Van Loo, N.D., Arendsen, A.F., Hagen, W.R., Stams, A.J. Arch. Microbiol. (1996) [Pubmed]
  6. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Liochev, S.I., Fridovich, I. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  7. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. Flint, D.H., Tuminello, J.F., Emptage, M.H. J. Biol. Chem. (1993) [Pubmed]
  8. The specificity of fumarate as a switching factor of the bacterial flagellar motor. Barak, R., Giebel, I., Eisenbach, M. Mol. Microbiol. (1996) [Pubmed]
  9. Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family. Fujii, T., Sakai, H., Kawata, Y., Hata, Y. J. Mol. Biol. (2003) [Pubmed]
  10. Escherichia coli fumarase A catalyzes the isomerization of enol and keto oxalacetic acid. Flint, D.H. Biochemistry (1993) [Pubmed]
  11. The regulation of the fumarase (citG) gene of Bacillus subtilis 168. Feavers, I.M., Price, V., Moir, A. Mol. Gen. Genet. (1988) [Pubmed]
  12. The multisubunit active site of fumarase C from Escherichia coli. Weaver, T.M., Levitt, D.G., Donnelly, M.I., Stevens, P.P., Banaszak, L.J. Nat. Struct. Biol. (1995) [Pubmed]
  13. Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli. Miles, J.S., Guest, J.R. Nucleic Acids Res. (1984) [Pubmed]
  14. Fumarase a from Escherichia coli: purification and characterization as an iron-sulfur cluster containing enzyme. Flint, D.H., Emptage, M.H., Guest, J.R. Biochemistry (1992) [Pubmed]
  15. Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC genes of Escherichia coli: role of the arcA, fnr, and soxR gene products. Park, S.J., Gunsalus, R.P. J. Bacteriol. (1995) [Pubmed]
  16. Functional interactions between the carbon and iron utilization regulators, Crp and Fur, in Escherichia coli. Zhang, Z., Gosset, G., Barabote, R., Gonzalez, C.S., Cuevas, W.A., Saier, M.H. J. Bacteriol. (2005) [Pubmed]
  17. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Weaver, T., Banaszak, L. Biochemistry (1996) [Pubmed]
  18. Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase. Colombo, S., Grisa, M., Tortora, P., Vanoni, M. FEBS Lett. (1994) [Pubmed]
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