ArticleApplied microbiology and biotechnology2018
Rhodococcus strains as source for ene-reductase activity.
Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Whole-genomic and transcriptomic analyses elucidateApplied and environmental microbiology · 2026Article
- Mining and engineering of ene-reductases from marine sediment metagenome for prochiral ACE inhibitor synthesis.Applied and environmental microbiology · 2026Article
- Dynamic Enantioconvergent Desaturation of 4,5-Disubstituted γ-Lactones in Whole Cells ofJournal of the American Chemical Society · 2026Article
- Introducing an Artificial Deazaflavin Cofactor inACS synthetic biology · 2022Article
- Asymmetric Reduction of (R)-Carvone through a Thermostable and Organic-Solvent-Tolerant Ene-Reductase.Chembiochem : a European journal of chemical biology · 2020Article
- Complete Genome Sequence ofMicrobiology resource announcements · 2019Article
- Review
- Editorial:Frontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhodococcus strains are ubiquitous in nature and known to metabolise a wide variety of compounds. At the same time, asymmetric reduction of C=C bonds is important in the production of high-valued chiral building blocks. In order to evaluate if Rhodococci can be used for this task, we have probed several Rhodococcus rhodochrous and R. erythropolis strains for ene-reductase activity. A series of substrates including activated ketones, an aldehyde, an imide and nitro-compound were screened using whole cells of seven Rhodococcus strains. This revealed that whole cells of all Rhodococcus strains showed apparent (S)-selectivity towards ketoisophorone, while most other organisms show (R)-selectivity for this compound. Three putative ene-reductases from R. rhodochrous ATCC 17895 were heterologously expressed in Escherichia coli. One protein was purified and its biocatalytic and biochemical properties were characterised, showing typical (enantioselective) properties for class 3 ene-reductases of the old yellow enzyme family.
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