ArticleJournal of industrial microbiology & biotechnology2014
Identification of a vitamin D3-specific hydroxylase genes through actinomycetes genome mining.
Article in Journal of industrial microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 14 citations in OpenAlex.
- Characterization of a CYP107 family vitamin DArchives of biochemistry and biophysics · 2026Article
- Targeted identification of new phaterpenes and elucidation of the relevant biosynthetic pathway inSynthetic and systems biotechnology · 2026Article
- Evolutionary formation of melatonin and vitamin D in early life forms: insects take centre stage.Biological reviews of the Cambridge Philosophical Society · 2024Review
- Bioconversion of vitamin DBiotechnology for biofuels and bioproducts · 2022Review
- Microbial Steroid Production Technologies: Current Trends and Prospects.Microorganisms · 2021Article
- Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.Applied microbiology and biotechnology · 2018Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
We previously completed whole-genome sequencing of a rare actinomycete named Sebekia benihana, and identified the complete S. benihana cytochrome P450 complement (CYPome), including 21 cytochrome P450 hydroxylase (CYP), seven ferredoxin (FD), and four ferredoxin reductase (FDR) genes. Through targeted CYPome disruption, a total of 32 S. benihana CYPome mutants were obtained. Subsequently, a novel cyclosporine A region-specific hydroxylase was successfully determined to be encoded by a CYP-sb21 gene by screening the S. benihana CYPome mutants. Here, we report that S. benihana is also able to mediate vitamin D3 (VD3) hydroxylation. Among the 32 S. benihana CYPome mutants tested, only a single S. benihana CYP mutant, ΔCYP-sb3a, failed to show regio-specific hydroxylation of VD3 to 25-hydroxyvitamin D3 and 1α,25-dihydroxyvitamin D3. Moreover, the VD3 hydroxylation activity in the ΔCYP-sb3a mutant was restored by CYP-sb3a gene complementation. Since all S. benihana FD and FDR disruption mutants maintained VD3 hydroxylation activity, we conclude that CYP-sb3a, a member of the bacterial CYP107 family, is the only essential component of the in vivo regio-specific VD3 hydroxylation process in S. benihana. Expression of the CYP-sb3a gene exhibited VD3 hydroxylation in the VD3 non-hydroxylating Streptomyces coelicolor, implying that the regio-specific hydroxylation of VD3 is carried out by a specific P450 hydroxylase in S. benihana.
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