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Gene Review

ubiC  -  chorismate pyruvate lyase

Escherichia coli O157:H7 str. EDL933

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Disease relevance of ubiC


High impact information on ubiC

  • C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops [2].
  • The enzyme chorismate lyase (CL) catalyzes the removal of pyruvate from chorismate to produce 4-hydroxy benzoate (4HB) for the ubiquinone pathway [1].
  • We have determined the structure of the CL product complex by crystallographic heavy-atom methods and report the structure at 1.4-A resolution for a fully active double Cys-to-Ser mutant and at 2.0-A resolution for the wild-type [1].
  • Of the several enzymes that convert chorismate to intermediates of E. coli biosynthetic pathways, chorismate lyase is the last to be isolated and characterized [3].
  • Chorismate lyase (CL) removes the pyruvyl group from chorismate to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway [4].

Chemical compound and disease context of ubiC

  • We previously reported the crystal structure at 1.4A resolution of the Escherichia coli CL with bound 4HB product, showing that the product is bound in an internal cavity behind two flaps [4].

Biological context of ubiC

  • Genome comparisons reveal that chorismate lyase orthologs are found in several bacteria, chloroplasts of eukaryotic algae and euryarchaea [5].
  • Chorismate lyase: kinetics and engineering for stability [6].

Associations of ubiC with chemical compounds

  • Use of overexpressed chorismate lyase to increase the rate of chorismic acid aromatization was mitigated by attendant decreases in the specific activity of DAHP synthase and feedback inhibition caused by p-hydroxybenzoic acid [7].
  • Second, a 2.4A structure of CL complexed with the inhibitor vanillate shows the flaps partly opened relative to their product-bound positions [4].
  • By removing the enolpyruvyl group from chorismate, chorismate lyase (CL) produces p-hydroxybenzoate (p-HB) for the ubiquinone biosynthetic pathway [6].

Analytical, diagnostic and therapeutic context of ubiC


  1. The crystal structure of chorismate lyase shows a new fold and a tightly retained product. Gallagher, D.T., Mayhew, M., Holden, M.J., Howard, A., Kim, K.J., Vilker, V.L. Proteins (2001) [Pubmed]
  2. Structural characterization of GntR/HutC family signaling domain. Gorelik, M., Lunin, V.V., Skarina, T., Savchenko, A. Protein Sci. (2006) [Pubmed]
  3. Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. Nichols, B.P., Green, J.M. J. Bacteriol. (1992) [Pubmed]
  4. Structural analysis of ligand binding and catalysis in chorismate lyase. Smith, N., Roitberg, A.E., Rivera, E., Howard, A., Holden, M.J., Mayhew, M., Kaistha, S., Gallagher, D.T. Arch. Biochem. Biophys. (2006) [Pubmed]
  5. HutC/FarR-like bacterial transcription factors of the GntR family contain a small molecule-binding domain of the chorismate lyase fold. Aravind, L., Anantharaman, V. FEMS Microbiol. Lett. (2003) [Pubmed]
  6. Chorismate lyase: kinetics and engineering for stability. Holden, M.J., Mayhew, M.P., Gallagher, D.T., Vilker, V.L. Biochim. Biophys. Acta (2002) [Pubmed]
  7. Microbial synthesis of p-hydroxybenzoic acid from glucose. Barker, J.L., Frost, J.W. Biotechnol. Bioeng. (2001) [Pubmed]
  8. Crystallization and 1.1-A diffraction of chorismate lyase from Escherichia coli. Stover, C., Mayhew, M.P., Holden, M.J., Howard, A., Gallagher, D.T. J. Struct. Biol. (2000) [Pubmed]
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