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Gene Review:

ubiC - chorismate pyruvate lyase

Escherichia coli O157:H7 str. EDL933

Smith, N. et al., Gallagher, D.T. et al., Barker, J.L. et al., Holden, M.J. et al., Nichols, B.P. et al., et al.

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Disease relevance of ubiC

In Escherichia coli, CL is monomeric, with 164 residues [1].

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

Crystallization and 1.1-A diffraction of chorismate lyase from Escherichia coli [8].

References

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]
Structural characterization of GntR/HutC family signaling domain. Gorelik, M., Lunin, V.V., Skarina, T., Savchenko, A. Protein Sci. (2006) [Pubmed]
Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. Nichols, B.P., Green, J.M. J. Bacteriol. (1992) [Pubmed]
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]
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]
Chorismate lyase: kinetics and engineering for stability. Holden, M.J., Mayhew, M.P., Gallagher, D.T., Vilker, V.L. Biochim. Biophys. Acta (2002) [Pubmed]
Microbial synthesis of p-hydroxybenzoic acid from glucose. Barker, J.L., Frost, J.W. Biotechnol. Bioeng. (2001) [Pubmed]
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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