Characterization of xenobiotic reductase A (XenA): study of active site residues, substrate spectrum and stability

摘要

Xenobiotic reductase A (XenA) has broad catalytic activity and reduces various α,β-unsaturated and nitro compounds with moderate to excellent stereoselectivity. Single mutants C25G and C25V are able to reduce nitrobenzene, a non-active substrate for the wild type, to produce aniline. Total turnover is dominated by chemical rather than thermal instability. The Old Yellow Enzyme (OYE) family is a class of flavin-dependent enzymes that catalyze the stereoselective reduction of activated C=C bonds at the expense of nicotinamide cofactors. This asymmetric bioreduction creates up to two new stereogenic centers and thus has gained increasing interest as a new tool in chiral intermediates synthesis.