Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family.
The asymmetric bioreduction of alkenes bearing an electron-withdrawing group using flavin-dependent enzymes from the 'old yellow enzyme' family at the expense of NAD(P)H yields the corresponding non-racemic alkanes going in hand with the creation of up to two chiral carbon centres. To avoid external cofactor recycling, this intriguing biotransformation was hitherto performed using whole microbial cells, which frequently showed insufficient stereoselectivities and/or undesired side reactions because of the action of competing enzymatic activities. Co-expression of enoate reductases with the corresponding redox enzymes for NAD(P)H recycling in a suitable host enables to overcome these drawbacks to furnish highly stereoselective and 'clean' C=C bioreductions on a preparative scale that are difficult to perform by conventional means.
Stuermer
Rainer
R
BASF AG, GVF/E-B9, D-67056 Ludwigshafen, Germany.
Hauer
Bernhard
B
Hall
Melanie
M
Faber
Kurt
K
D000475:Alkenes / Q000378:metabolism*; D001419:Bacteria / Q000378:metabolism; D005658:Fungi / Q000378:metabolism; D023281:Genomics; D009249:NADP / Q000378:metabolism; D009252:NADPH Dehydrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D013237:Stereoisomerism
D000475:Alkenes; D009249:NADP; D010088:Oxidoreductases; D009252:NADPH Dehydrogenase