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Gene Review

ECs0991  -  3-phosphoshikimate 1-carboxyvinyltransferase

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs0991

 

High impact information on ECs0991

 

Chemical compound and disease context of ECs0991

 

Biological context of ECs0991

 

Anatomical context of ECs0991

  • Since the expressed EPSPS protein was found as an insoluble form in the inclusion body, it was extracted by 6 M urea after sonication, and then purified through immobilized nickel-affinity column chromatography to isolate EPSPS having a molecular mass of 57 kDa [14].
 

Associations of ECs0991 with chemical compounds

 

Other interactions of ECs0991

 

Analytical, diagnostic and therapeutic context of ECs0991

References

  1. Protein trans-splicing in transgenic plant chloroplast: reconstruction of herbicide resistance from split genes. Chin, H.G., Kim, G.D., Marin, I., Mersha, F., Evans, T.C., Chen, L., Xu, M.Q., Pradhan, S. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. A single amino acid substitution in the enzyme 5-enolpyruvylshikimate-3-phosphate synthase confers resistance to the herbicide glyphosate. Stalker, D.M., Hiatt, W.R., Comai, L. J. Biol. Chem. (1985) [Pubmed]
  3. Expression of human IL-1 beta in Salmonella typhimurium. A model system for the delivery of recombinant therapeutic proteins in vivo. Carrier, M.J., Chatfield, S.N., Dougan, G., Nowicka, U.T., O'Callaghan, D., Beesley, J.E., Milano, S., Cillari, E., Liew, F.Y. J. Immunol. (1992) [Pubmed]
  4. Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate-bound state and S3P-GLP-bound state. Park, H., Hilsenbeck, J.L., Kim, H.J., Shuttleworth, W.A., Park, Y.H., Evans, J.N., Kang, C. Mol. Microbiol. (2004) [Pubmed]
  5. Molecular characterization of the Aeromonas hydrophila aroA gene and potential use of an auxotrophic aroA mutant as a live attenuated vaccine. Hernanz Moral, C., Flaño del Castillo, E., López Fierro, P., Villena Cortés, A., Anguita Castillo, J., Cascón Soriano, A., Sánchez Salazar, M., Razquín Peralta, B., Naharro Carrasco, G. Infect. Immun. (1998) [Pubmed]
  6. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Stallings, W.C., Abdel-Meguid, S.S., Lim, L.W., Shieh, H.S., Dayringer, H.E., Leimgruber, N.K., Stegeman, R.A., Anderson, K.S., Sikorski, J.A., Padgette, S.R., Kishore, G.M. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  7. A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states. Eschenburg, S., Kabsch, W., Healy, M.L., Schonbrunn, E. J. Biol. Chem. (2003) [Pubmed]
  8. Evidence for a reactive gamma-carboxyl group (Glu-418) at the herbicide glyphosate binding site of 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli. Huynh, Q.K. J. Biol. Chem. (1988) [Pubmed]
  9. Identification of the reactive cysteines of Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase and their nonessentiality for enzymatic catalysis. Padgette, S.R., Huynh, Q.K., Aykent, S., Sammons, R.D., Sikorski, J.A., Kishore, G.M. J. Biol. Chem. (1988) [Pubmed]
  10. Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site. Padgette, S.R., Re, D.B., Gasser, C.S., Eichholtz, D.A., Frazier, R.B., Hironaka, C.M., Levine, E.B., Shah, D.M., Fraley, R.T., Kishore, G.M. J. Biol. Chem. (1991) [Pubmed]
  11. Chloroplast transport of a ribulose bisphosphate carboxylase small subunit-5-enolpyruvyl 3-phosphoshikimate synthase chimeric protein requires part of the mature small subunit in addition to the transit peptide. Comai, L., Larson-Kelly, N., Kiser, J., Mau, C.J., Pokalsky, A.R., Shewmaker, C.K., McBride, K., Jones, A., Stalker, D.M. J. Biol. Chem. (1988) [Pubmed]
  12. Glyphosate-resistant goosegrass. Identification of a mutation in the target enzyme 5-enolpyruvylshikimate-3-phosphate synthase. Baerson, S.R., Rodriguez, D.J., Tran, M., Feng, Y., Biest, N.A., Dill, G.M. Plant Physiol. (2002) [Pubmed]
  13. A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics. Anderson, K.S., Sikorski, J.A., Johnson, K.A. Biochemistry (1988) [Pubmed]
  14. The 5-enolpyruvylshikimate-3-phosphate synthase of glyphosate-tolerant soybean expressed in Escherichia coli shows no severe allergenicity. Chang, H.S., Kim, N.H., Park, M.J., Lim, S.K., Kim, S.C., Kim, J.Y., Kim, J.A., Oh, H.Y., Lee, C.H., Huh, K., Jeong, T.C., Nam, D.H. Mol. Cells (2003) [Pubmed]
  15. Structural constraints on the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase from rotational-echo double-resonance NMR. McDowell, L.M., Schmidt, A., Cohen, E.R., Studelska, D.R., Schaefer, J. J. Mol. Biol. (1996) [Pubmed]
  16. The complex Arom locus of Aspergillus nidulans. Evidence for multiple gene fusions and convergent evolution. Hawkins, A.R. Curr. Genet. (1987) [Pubmed]
  17. Site-directed mutagenesis of Petunia hybrida 5-enolpyruvylshikimate-3-phosphate synthase: Lys-23 is essential for substrate binding. Huynh, Q.K., Bauer, S.C., Bild, G.S., Kishore, G.M., Borgmeyer, J.R. J. Biol. Chem. (1988) [Pubmed]
  18. Crystallization of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli. Abdel-Meguid, S.S., Smith, W.W., Bild, G.S. J. Mol. Biol. (1985) [Pubmed]
  19. Identification of a glyphosate-resistant mutant of rice 5-enolpyruvylshikimate 3-phosphate synthase using a directed evolution strategy. Zhou, M., Xu, H., Wei, X., Ye, Z., Wei, L., Gong, W., Wang, Y., Zhu, Z. Plant Physiol. (2006) [Pubmed]
  20. EPSP synthase: binding studies using isothermal titration microcalorimetry and equilibrium dialysis and their implications for ligand recognition and kinetic mechanism. Ream, J.E., Yuen, H.K., Frazier, R.B., Sikorski, J.A. Biochemistry (1992) [Pubmed]
  21. Synergistic inhibitor binding to Streptococcus pneumoniae 5-enolpyruvylshikimate-3-phosphate synthase with both monovalent cations and substrate. Du, W., Liu, W.S., Payne, D.J., Doyle, M.L. Biochemistry (2000) [Pubmed]
 
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