Abstract

Firefly luciferase is a multifunctional enzyme. At least three enzymatic activities have been reported thus far. The first is the well-known light-emitting activity, and the second is the thioesterification capability toward various unnatural carboxylic acids. In particular, we disclosed the additional enantiodifferentiation activity toward 2-arylpropanoic acids, such as ketoprofen, where each enantiomer displays a different activity under physiological conditions. The thioesterified enantiomer could be converted to the antipode by enzymatic chiral inversion processes, such as the deracemization reaction. We could construct a sufficient deracemizative luminous d-luciferin production system by combining firefly luciferase and thioesterase. The third enzyme activity is the amide bond formation activity with cysteine derivatives. Therefore, this chapter will introduce the great potential of firefly luciferase as a biotransformation enzyme for the beneficial preparation of optically active compounds and N-acyl-cysteine derivatives.

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