Enzymatic synthesis of chiral amino acid sulfoxides by Fe(II)/α-ketoglutarate-dependent dioxygenase

Abstract

Asymmetric sulfoxidation of sulfur-containing l-amino acids was successfully achieved through bioconversion using IDO, which is an Fe(II)/α-ketoglutarate-dependent dioxygenase previously found in Bacillus thuringiensis strain 2e2. The IDO catalyzed sulfoxidation of l-methionine, l-ethionine, S-methyl-l-cysteine, S-ethyl-l-cysteine, and S-allyl-l-cysteine into the corresponding (S)-configured sulfoxides such as (+)-methiin and (+)-alliin, which are responsible for valuable physiological activities in mammals, and have high stereoselectivity. Herein we have established an effective preparative laboratory scale production method to obtain enantiomerically pure chiral sulfoxides using an IDO biocatalyst.