Enzymatic asymmetric hydroxylation of unnatural substrates with soybean lipoxygenase

Abstract

Surrogate substrates mimicking the natural substrate (linoleic acid) bearing a spacing prosthetic group with a non-ionic hydroxyl terminus undergo asymmetric hydroxylation with soybean lipoxygenase. The prosthetic modifier supplies the missing structural features needed for enzymatic recognition and controls the regiochemical outcome of the reaction by its high hydrophobic content. The effect of pH on the regiochemistry clearly shows that all the substrates can arrange themselves at the active site of soybean lipoxygenase in only one orientation leading to formation of hydroperoxides by oxygenation at the ω-6 carbon.