ArticleScientific reports2014
The structural basis of an NADP⁺-independent dithiol oxidase in FK228 biosynthesis.
Article in Scientific reports, 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Convergent evolution in toxin detection and resistance provides evidence for conserved bacterial-fungal interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Evaluation of Antioxidant Therapeutic Value of ACE Inhibitor as Adjunct Therapy on Type 2 Diabetes Mellitus Patients with Cardiovascular Disease.ACS pharmacology & translational science · 2022Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Chemical reviews · 2017Review
- Generate a bioactive natural product library by mining bacterial cytochrome P450 patterns.Synthetic and systems biotechnology · 2016Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The disulfide bond is unusual in natural products and critical for thermal stability, cell permeability and bioactivity. DepH from Chromobacterium violaceum No. 968 is an FAD-dependent enzyme responsible for catalyzing the disulfide bond formation of FK228, an anticancer prodrug approved for the treatment of cutaneous T-cell lymphoma. Here we report the crystal structures of DepH and DepH complexed with a substrate analogue S,S'-dimethyl FK228 at 1.82 Å and 2.00 Å, respectively. Structural and biochemical analyses revealed that DepH, in contrast to the well characterized low molecular weight thioredoxin reductases (LMW TrxRs), is an NADP(+)-independent dithiol oxidase. DepH not only lacks a conserved GGGDXAXE motif necessary for NADP(+) binding in the canonical LMW TrxRs, but also contains a 11-residue sequence which physically impedes the binding of NADP(+). These observations explain the difference between NADP(+)-independent small molecule dithiol oxidases and NADP(+)-dependent thioredoxin reductases and provide insights for understanding the catalytic mechanism of dithiol oxidases involved in natural product biosynthesis.
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