A 38 kDa allylic alcohol dehydrogenase from the cultured cells of Nicotiana tabacum

An NADP(+)-dependent alcohol dehydrogenase (allyl-ADH) was isolated from th e cultured cells of Nicotiana tabacum. The allyl-ADH was found to be effici ent for the dehydrogenation of secondary allylic alcohols rather than satur ated secondary alcohols and it was specific for the S-stereoisomer of the a lcohols. The enzyme catalyzed the reversible reaction whereby the carbonyl group of enones is reduced to the corresponding allylic alcohol or vice ver sa. Two possible primary structures of the allyl-ADH were deduced by the se quence analyses of full-length cDNAs (ally-ADH1 and ally-ADH2), which were cloned by the PCR method. These analyses indicated that the allyl-ADHs are composed of 343 amino acids having the molecular weights 38 083 and 37 994, respectively, and they showed approximately 70% homology to the NADP(+)-de pendent oxidoreductases belonging to a plant zeta -crystallin family. (C) 2 000 Elsevier Science Ltd. All rights reserved.