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An enone reductase from Nicotiana tabacum: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant proteins |
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| Authors: | Matsushima Akihito Sato Yuya Otsuka Miki Watanabe Takayoshi Yamamoto Hiroaki Hirata Toshifumi |
| Affiliation: | a Natural Science Center for Basic Research and Development, Radioisotope Center, Hiroshima University, 1-4-2 Kagamiyama, Higashi-Hiroshima 739-8526, Japan b Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8526, Japan c R&D Management Corporate Development Center, Daicel Chemical Industries, Ltd., Himeji Research Center, 1239 Shinzaike, Aboshi-ku, Himeji, Hyogo 671-1283, Japan |
| Abstract: | In the course of the purification of enone reductase participating to the reduction of pulegone, two reductases (NtRed-1 and NtRed-2) were isolated from cultured cells of Nicotiana tabacum. The partial amino acid sequences of the reductases revealed that NtRed-1 was allyl-alcohol dehydrogenase (Accession No. BAA89423) and NtRed-2 was malate dehydrogenase (Accession No. CAC12826). cDNA cloning and expression of these reductases in Escherichia coli were performed. Reduction with recombinant proteins was examined with cyclic α,β-unsaturated ketones, such as pulegone, carvone and verbenone, as substrates. It was found that the recombinant NtRed-1 catalyses the hydrogenation of the exocyclic C-C double bond of pulegone. |
| Keywords: | Nicotiana tabacum Enone reductase Allyl-alcohol dehydrogenase Malate dehydrogenase cDNA cloning Recombinant proteins Reduction of pulegone Reduction of enones |
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