153330-60-0Relevant academic research and scientific papers
Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents
Yanto, Yanto,Winkler, Christoph K.,Lohr, Stephanie,Hall, Melanie,Faber, Kurt,Bommarius, Andreas S.
, p. 2540 - 2543 (2011)
Asymmetric trans-bioreduction of activated alkenes by KYE1 from Kluyveromyces lactis and Yers-ER from Yersinia bercovieri, two ene-reductases from the Old Yellow Enzyme family, showed a broad substrate spectrum with a moderate to excellent degree of stereoselectivity. Both substrate- and enzyme-based stereocontrols were observed to furnish opposite stereoisomeric products. The effects of organic solvents on enzyme activity and stereoselectivity were outlined in this study, where two-phase systems hexane and toluene are shown to sustain bioreduction efficiency even at high organic solvent content.
Asymmetric synthesis of O-protected acyloins using enoate reductases: Stereochemical control through protecting group modification
Winkler, Christoph K.,Stueckler, Clemens,Mueller, Nicole J.,Pressnitz, Desiree,Faber, Kurt
experimental part, p. 6354 - 6358 (2011/02/24)
O-Protected cyclic acyloins were obtained in nonracemic form through asymmetric bioreduction of α,β-unsaturated alkoxy ketones by using 11 different enoate reductases from the "Old Yellow Enzyme" family. The stereochemical outcome of the biotransformation could be switched by variation of the O-protecting group or by the ring size of the substrate, which allows access to both stereoisomers in up to >97 % ee Whereas α-alkoxy enones were readily accepted as substrates, β-analogs were not converted. Overall, α-alkoxy enones represent a novel type of substrate for flavin-dependent ene-reductases. Copyright
