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- W2003708857 abstract "The genes encoding yeast old yellow enzymes (OYE 1, 2, and 3) and NAD(P)H-dependent 2-cyclohexen-1-one reductase from Zymomonas mobilis (NCR) were expressed separately in Escherichia coli. All four recombinant strains reduced the carbon double bond in α,β-unsaturated alkenals and alkenones, however rates and enantio-specificities differed. Which of the two possible enantiomers was predominantly formed, was not only dependent on the choice of enzyme but also on the substrate: In addition to a dependency on methylation in α- or β-position, the data of this study illustrate that firstly the E- or Z-configuration (cis- or trans-) of the carbon double-bond and secondly the remainder of the substrate molecule play roles in determining enantio-specificity. Based on the currently accepted mechanism of flavin mediated anti-hydrogenation of the carbon double bond, the data in this study may be explained by a flipped orientation of some of the substrates in the active center of OYE. Biotechnol. Bioeng. 2007; 98: 22–29. © 2007 Wiley Periodicals, Inc." @default.
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- W2003708857 date "2007-01-01" @default.
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- W2003708857 title "Asymmetric alkene reduction by yeast old yellow enzymes and by a novelZymomonas mobilis reductase" @default.
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- W2003708857 doi "https://doi.org/10.1002/bit.21415" @default.
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