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).

Belongs to the NADP-dependent oxidoreductase L4BD family.

343 amino acids

MAEEVSNKQVILKNYVTGYPKESDMEIKNVTIKLKVPEGSNDVVVKNLYLSCDPYMRSRMRKIEGSYVESFAPGSPITGYGVAKVLESGDPKFQKGDLVWGMTGWEEYSIITPTQTLFKIHDKDVPLSYYTGILGMPGMTAYAGFHEVCSPKKGETVFVSAASGAVGQLVGQFAKMLGCYVVGSAGSKEKVDLLKSKFGFDEAFNYKEEQDLSAALKRYFPDGIDIYFENVGGKMLDAVLVNMKLYGRIAVCGMISQYNLEQTEGVHNLFCLITKRIRMEGFLVFDYYHLYPKYLEMVIPQIKAGKVVYVEDVAHGLESAPTALVGLFSGRNIGKQVVMVSRE

38.1 kDa

(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)

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