Chorismate pyruvate-lyase from converts chorismate to 4-hydroxybenzoate. The enzyme was enriched 3000-fold by overexpression and chromatographic purification. It has an apparent value for chorismate of 6·1 μM and an isoelectric point of pH 6·45. The enzyme activity did not require metal cofactors. Promoter sequences in the 5′ flanking sequences of the operon were localized by transcription and translation of active chorismate pyruvate-lyase from different PCR fragments. Sequencing of the gene of the mutant strain AN244 revealed a G→A transition resulting in a change from glutamic acid to lysine. A feeding experiment with [1,7-C]shikimate confirmed the chorismate pyruvate-lyase as the sole enzymic source of 4-hydroxybenzoate .


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