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

Purification and enzymatic characterization of trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from Rhodococcus opacus and enzymatic formation of α, β-unsaturated ketones.
Biosci Biotechnol Biochem. 2019 Jun 04;:1-5
Authors: Suzuki T, Takizawa N
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, β-unsaturated ketones.
PMID: 31161894 [PubMed - as supplied by publisher]

Source: Bioscience, Biotechnology, and Biochemistry - June 3, 2019 Category: Biochemistry Authors: Suzuki T, Takizawa N Tags: Biosci Biotechnol Biochem Source Type: research