Purification and enzymatic characterization of trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from Rhodococcus opacus and enzymatic formation of α, ß-unsaturated ketones.

ABSTRACT

Trans-o-hydroxybenzylidenepyruvate (tHBPA) hydratase-aldolase (RnoE) catalyzes the conversion of tHBPA to 2-hydroxybenzaldehyde and pyruvate. We purified RnoE from Rhodococcus opacus and characterized its enzymatic properties. It exhibited maximum enzyme activity at 60°C and catalyzed the reverse reaction, converting various aromatic benzaldehydes and pyruvate to benzylidenepyruvate, indicating that this enzyme can be adapted for the enzymatic synthesis of α, ß-unsaturated ketones.