Asymmetric alkene reduction by yeast old yellow enzymes and by a novel Zymomonas mobilis reductase |
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Authors: | Müller André Hauer Bernhard Rosche Bettina |
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Institution: | School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia. |
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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 alpha,beta-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 alpha- or beta-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. |
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Keywords: | biotransformation old yellow enzyme (OYE) enoate reductase enantio‐specific alkene reduction citral isomers geranial and neral Zymomonas mobilis |
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