ArticleJournal of bacteriology2011
Multiplicity of 3-Ketosteroid-9α-Hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 82 citations in OpenAlex.
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- Insight into Different Stages of Steroid Degradation in ThermophilicInternational journal of molecular sciences · 2022Article
- Microbial Steroid Production Technologies: Current Trends and Prospects.Microorganisms · 2021Article
- Steroid Metabolism in Thermophilic ActinobacteriumMicroorganisms · 2021Article
- Comparative Analysis of Bile-Salt Degradation inApplied and environmental microbiology · 2021Article
- Investigations on the Degradation of the Bile Salt Cholate via the 9,10-Microorganisms · 2021Article
- Proteome, Bioinformatic, and Functional Analyses Reveal a Distinct and Conserved Metabolic Pathway for Bile Salt Degradation in theApplied and environmental microbiology · 2021Article
- Degradation of Bile Acids by Soil and Water Bacteria.Microorganisms · 2021Review
- Efficient conversion of phytosterols into 4-androstene-3,17-dione and its C1,2-dehydrogenized and 9α-hydroxylated derivatives by engineered Mycobacteria.Microbial cell factories · 2021Article
- Further Studies on the 3-Ketosteroid 9α-Hydroxylase ofMicroorganisms · 2021Article
- Different genome-wide transcriptome responses of Nocardioides simplex VKM Ac-2033D to phytosterol and cortisone 21-acetate.BMC biotechnology · 2021Article
- Designed whole-cell-catalysis-assisted synthesis of 9,11-secosterols.Beilstein journal of organic chemistry · 2021Article
- Characterization of CYP125A13, the First Steroid C-27 Monooxygenase fromJournal of microbiology and biotechnology · 2020Article
- Article
- Microbial degradation of steroid sex hormones: implications for environmental and ecological studies.Microbial biotechnology · 2020Review
- Expression, Purification, Refolding, and Characterization of aFrontiers in bioengineering and biotechnology · 2020Article
- The Analysis of Estrogen-Degrading and Functional Metabolism Genes inInternational journal of genomics · 2020Article
- Testosterone Degradative Pathway ofGenes · 2019Article
- Review
- Genome-wide response on phytosterol in 9-hydroxyandrostenedione-producing strain of Mycobacterium sp. VKM Ac-1817D.BMC biotechnology · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The well-known large catabolic potential of rhodococci is greatly facilitated by an impressive gene multiplicity. This study reports on the multiplicity of kshA, encoding the oxygenase component of 3-ketosteroid 9α-hydroxylase, a key enzyme in steroid catabolism. Five kshA homologues (kshA1 to kshA5) were previously identified in Rhodococcus rhodochrous DSM43269. These KshA(DSM43269) homologues are distributed over several phylogenetic groups. The involvement of these KshA homologues in the catabolism of different classes of steroids, i.e., sterols, pregnanes, androstenes, and bile acids, was investigated. Enzyme activity assays showed that all KSH enzymes with KshA(DSM43269) homologues are C-9 α-hydroxylases acting on a wide range of 3-ketosteroids, but not on 3-hydroxysteroids. KshA5 appeared to be the most versatile enzyme, with the broadest substrate range but without a clear substrate preference. In contrast, KshA1 was found to be dedicated to cholic acid catabolism. Transcriptional analysis and functional complementation studies revealed that kshA5 supported growth on any of the different classes of steroids tested, consistent with its broad expression induction pattern. The presence of multiple kshA genes in the R. rhodochrous DSM43269 genome, each displaying unique steroid induction patterns and substrate ranges, appears to facilitate a dynamic and fine-tuned steroid catabolism, with C-9 α-hydroxylation occurring at different levels during microbial steroid degradation.
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