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Gene Review

fumC  -  fumarate hydratase

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of fumC

 

High impact information on fumC

 

Chemical compound and disease context of fumC

 

Biological context of fumC

 

Anatomical context of fumC

 

Associations of fumC with chemical compounds

 

Analytical, diagnostic and therapeutic context of fumC

References

  1. Rapid and specific detection of the O15:K52:H1 clonal group of Escherichia coli by gene-specific PCR. Johnson, J.R., Owens, K., Sabate, M., Prats, G. J. Clin. Microbiol. (2004) [Pubmed]
  2. Fumarase C activity is elevated in response to iron deprivation and in mucoid, alginate-producing Pseudomonas aeruginosa: cloning and characterization of fumC and purification of native fumC. Hassett, D.J., Howell, M.L., Sokol, P.A., Vasil, M.L., Dean, G.E. J. Bacteriol. (1997) [Pubmed]
  3. 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]
  4. 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]
  5. 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]
  6. Purification and crystallization of fumarase C from Escherichia coli. Weaver, T.M., Levitt, D.G., Banaszak, L.J. J. Mol. Biol. (1993) [Pubmed]
  7. Mutational analysis of amino acid residues involved in argininosuccinate lyase activity in duck delta II crystallin. Chakraborty, A.R., Davidson, A., Howell, P.L. Biochemistry (1999) [Pubmed]
  8. Physical and genetic maps of the Leptospira interrogans serovar icterohaemorrhagiae strain Ictero no.1 chromosome and sequencing of a 19-kb region of the genome containing the 5S rRNA gene. Takahashi, Y., Akase, K., Hirano, H., Fukunaga, M. Gene (1998) [Pubmed]
  9. Structure of free fumarase C from Escherichia coli. Weaver, T. Acta Crystallogr. D Biol. Crystallogr. (2005) [Pubmed]
  10. Induction of the soxRS regulon of Escherichia coli by glycolaldehyde. Benov, L., Fridovich, I. Arch. Biochem. Biophys. (2002) [Pubmed]
  11. 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]
  12. Differential activities of the SoxR protein of Escherichia coli: SoxS is not required for gene activation under iron deprivation. Fuentes, A.M., Díaz-Mejía, J.J., Maldonado-Rodríguez, R., Amábile-Cuevas, C.F. FEMS Microbiol. Lett. (2001) [Pubmed]
  13. Regulation of fumarase (fumB) gene expression in Escherichia coli in response to oxygen, iron and heme availability: role of the arcA, fur, and hemA gene products. Tseng, C.P. FEMS Microbiol. Lett. (1997) [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. Rapid and specific detection of Escherichia coli clonal group A by gene-specific PCR. Johnson, J.R., Owens, K., Manges, A.R., Riley, L.W. J. Clin. Microbiol. (2004) [Pubmed]
  16. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Weaver, T., Banaszak, L. Biochemistry (1996) [Pubmed]
  17. L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology. Takagi, J.S., Tokushige, M., Shimura, Y., Kanehisa, M. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  18. Modulation of the fumarases of Escherichia coli in response to oxidative stress. Liochev, S.I., Fridovich, I. Arch. Biochem. Biophys. (1993) [Pubmed]
  19. Characterization of multiple fumarase proteins in Escherichia coli. Yumoto, N., Tokushige, M. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  20. X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation. Estévez, M., Skarda, J., Spencer, J., Banaszak, L., Weaver, T.M. Protein Sci. (2002) [Pubmed]
 
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