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Gene Review:

ubiC - chorismate pyruvate lyase

Escherichia coli CFT073

Viitanen, P.V. et al., Stadthagen, G. et al.

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High impact information on ubiC

These results establish Rv2949c as a chorismate pyruvate-lyase responsible for the direct conversion of chorismate to p-hydroxybenzoate and identify Rv2949c as the sole enzymatic source of p-hydroxybenzoic acid in M. tuberculosis [1].
CPL catalyzes the direct conversion of chorismate, an important branch point intermediate in the shikimate pathway that is exclusively synthesized in plastids, to pHBA and pyruvate [2].
Integration of CPL into the chloroplast genome provides a dramatic demonstration of the high-flux potential of the shikimate pathway for chorismate biosynthesis, and could prove to be a cost-effective route to pHBA [2].

Anatomical context of ubiC

These experiments demonstrate that the current limitation for pHBA production in nuclear-transformed plants is CPL enzyme activity, and that the process becomes substrate-limited only when the enzyme is present at very high levels in the compartment of interest, such as the case with plastid transformation [2].

References

p-Hydroxybenzoic acid synthesis in Mycobacterium tuberculosis. Stadthagen, G., Korduláková, J., Griffin, R., Constant, P., Bottová, I., Barilone, N., Gicquel, B., Daffé, M., Jackson, M. J. Biol. Chem. (2005) [Pubmed]
Metabolic engineering of the chloroplast genome using the Echerichia coli ubiC gene reveals that chorismate is a readily abundant plant precursor for p-hydroxybenzoic acid biosynthesis. Viitanen, P.V., Devine, A.L., Khan, M.S., Deuel, D.L., Van Dyk, D.E., Daniell, H. Plant Physiol. (2004) [Pubmed]

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