‘New uses for an Old Enzyme’ – the Old Yellow Enzyme family of flavoenzymes

Old Yellow Enzyme fromCandida macedoniensisCatalyzes the Stereospecific Reduction of the C=C Bond of Ketoisophorone

“…An Old Yellow Enzyme was isolated from brewers' yeast as theˆrst ‰avoprotein by Warburg and Christian, 19,20) and has been thoroughly studied by many researchers. [13][14][15][16][21][22][23] However, the application of an Old Yellow Enzyme to a stereospeciˆc reaction, as described here, had not been previously reported. The discovery of this stereospeciˆc reaction by Old Yellow Enzyme might help in elucidation of its reaction mechanism.…”

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

“…Extensive biochemical and structural studies have been carried out with OYEs, which have demonstrated their ability to reduce a large variety of unsaturated compounds to their saturated counterparts. However, their physiological function has not been completely established, although proposals suggesting a conserved role in the detoxification of electrophilic compounds have been made [106].…”

“…For example, OYE can reduce nitroalkenes to nitroalkanes in a process involving the formation of a nitronate intermediate. OYE1 from Saccharomyces carlsbergensis with Y196F mutation has been shown to cause the accumulation of the nitronate intermediate, which could be then chemically alkylated to generate nitroalkanes with two chiral centers [106]. Another potential application is to use them to easily carry out small modifications in the structure of drugs to alter their pharmaceutical properties, such as morphine alkaloids.…”

“…OYE was first identified in the 1930s as a yellow enzyme able to form a complete respiratory system together with glucose-6-phosphate dehydrogenase acting on glucose-6-phosphate and using molecular oxygen as the final electron acceptor [105]. Since then, variants have been identified in yeasts, plants and bacteria [106]. When it was purified by Theorell in 1935, it was shown to contain a protein, colourless component and a yellow component essential for activity [107].…”

Asymmetric bioreduction of activated alkenes by a novel isolate of Achromobacter species producing enoate reductase

“…The biocatalytic approach is catalyzed by enoate reductases [EC1.3.1.31], members of the "old yellow enzyme" (OYE) family (Stuermer et al 2007;Williams and Bruce 2002), which were first isolated from Saccharomyces carlsbergensis (Warburg and Christian 1932) and later found to be able to catalyze the asymmetric reduction of α,β-unsaturated ketones (Leuenberger et al 1976) and other activated alkenes (Ohta et al 1989). These enzymes are ubiquitous and widely distributed in biological sources including higher plants, bacteria, and lower fungi.…”