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Bioorg Chem. 2008 Feb;36(1):23-8. Epub 2007 Oct 22.

An enone reductase from Nicotiana tabacum: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant proteins.

Author information

1
Natural Science Center for Basic Research and Development, Radioisotope Center, Hiroshima University, 1-4-2 Kagamiyama, Higashi-Hiroshima 739-8526, 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 alpha,beta-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.

PMID:
17945329
DOI:
10.1016/j.bioorg.2007.08.005
[Indexed for MEDLINE]

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