Structural highlights
Function
[DBR_TOBAC] Reduces the C=C double bonds of alpha, beta unsaturated enones, but has no activity on enones with an endocyclic C=C double-bond. Shows a high specificity for NADPH as the hybrid donor. Substrates are 1-nitrocyclohexene, 2-methylpentenal, trans-cinnamaldehyde, methyl-trans-2-methylcinnamaldehyde, trans-2-nonenal and 1-octen-3-one. Reduced activity with aplha-methyl transcinnamaldehyde, 1-cyclohexene-1-carboxaldehyde, methyl crotonate, (R)-pulegone, and dimethyl itaconate and no activity with maleimides, citral, (5R)- or (5S)-carvone, (S)-perillyl alcohol, and substituted cyclohexenones and cyclopentenones (PubMed:17945329, Ref.3). May also act as a allyl-alcohol dehydrogenase by catalyzing the dehydrogenation of secondary allylic alcohols rather than saturated secondary alcohols. Allyl-alcohol dehydrogenase is specific for the S-stereoisomer of the alcohols (PubMed:11117876).[1] [2] [REFERENCE:3]
See Also
References
- ↑ Hirata T, Tamura Y, Yokobatake N, Shimoda K, Ashida Y. A 38 kDa allylic alcohol dehydrogenase from the cultured cells of Nicotiana tabacum. Phytochemistry. 2000 Oct;55(4):297-303. PMID:11117876
- ↑ Matsushima A, Sato Y, Otsuka M, Watanabe T, Yamamoto H, Hirata T. An enone reductase from Nicotiana tabacum: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant proteins. Bioorg Chem. 2008 Feb;36(1):23-8. Epub 2007 Oct 22. PMID:17945329 doi:http://dx.doi.org/10.1016/j.bioorg.2007.08.005
