Disease relevance of ubiC

• This gene of Escherichia coli encodes chorismate pyruvate-lyase (CPL), an enzyme that converts chorismate into 4HB and is not normally present in plants [1].

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 [2].
• Transgenic plants showed high chorismate pyruvate-lyase activity and accumulated 4HB as beta-glucosides, with the glucose attached to either the hydroxy or the carboxyl function of 4HB [3].
• The biosynthetic pathway to 4-hydroxybenzoate (4HB), a precursor of the naphthoquinone pigment shikonin, was modified in Lithospermum erythrorhizon hairy root cultures by introduction of the bacterial gene ubiC [1].
• The bacterial gene ubiC encodes chorismate pyruvate-lyase, an enzyme which converts chorismate to 4-hydroxybenzoate and which is not normally present in plants [4].
• In both cases, chorismate pyruvate-lyase activity and a resulting formation of 4-hydroxybenzoate was detected [4].

Anatomical context of ubiC

• Expression of bacterial chorismate pyruvate-lyase in tobacco: evidence for the presence of chorismate in the plant cytosol [4].

References