ArticleACS chemical biology2013
Molecular insight into substrate recognition and catalysis of Baeyer-Villiger monooxygenase MtmOIV, the key frame-modifying enzyme in the biosynthesis of anticancer agent mithramycin.
Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 50 citations in OpenAlex.
- Preparation and Bioactivity Evaluation of Novel Dihydrotanshinone I Derivatives via Biotransformation byJournal of fungi (Basel, Switzerland) · 2026Article
- A Hooker Oxygenase Archetype in Polyketide Biosynthesis Challenging the Baeyer-Villiger Monooxygenase Paradigm.Journal of the American Chemical Society · 2026Article
- Recombinant Expression and Characterization of a Novel Type I Baeyer-Villiger Monooxygenase from aInternational journal of molecular sciences · 2025Article
- Development of tetracycline analogues with increased aqueous stability for the treatment of mycobacterial infections.Tuberculosis (Edinburgh, Scotland) · 2025Article
- A flavin-monooxygenase catalyzing oxepinone formation and the complete biosynthesis of vibralactone.Nature communications · 2023Article
- Three Rings to Rule Them All: How Versatile Flavoenzymes Orchestrate the Structural Diversification of Natural Products.Biochemistry · 2022Article
- Catalytic Control of Spiroketal Formation in Rubromycin Polyketide Biosynthesis.Angewandte Chemie (International ed. in English) · 2021Article
- Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides.Nature communications · 2021Article
- Discovery of a Cryptic Intermediate in Late Steps of Mithramycin Biosynthesis.Angewandte Chemie (International ed. in English) · 2020Article
- The biosynthetic pathway to tetromadurin (SF2487/A80577), a polyether tetronate antibiotic.PloS one · 2020Article
- Unexpected enzyme-catalysed [4+2] cycloaddition and rearrangement in polyether antibiotic biosynthesis.Nature catalysis · 2019Article
- Article
- Comparative Transcriptome Analysis Reveals the Mechanism Underlying 3,5-Dibromo-4-Hydroxybenzoate Catabolism via a New Oxidative Decarboxylation Pathway.Applied and environmental microbiology · 2018Article
- The Uncommon Enzymology of Cis-Acyltransferase Assembly Lines.Chemical reviews · 2017Review
- New insights into bacterial type II polyketide biosynthesis.F1000Research · 2017Review
- Substitution of a Single Amino Acid Reverses the Regiospecificity of the Baeyer-Villiger Monooxygenase PntE in the Biosynthesis of the Antibiotic Pentalenolactone.Biochemistry · 2016Article
- The Structure of the Antibiotic Deactivating, N-hydroxylating Rifampicin Monooxygenase.The Journal of biological chemistry · 2016Article
- Insights into Complex Oxidation during BE-7585A Biosynthesis: Structural Determination and Analysis of the Polyketide Monooxygenase BexE.ACS chemical biology · 2016Article
- The Origin and Evolution of Baeyer-Villiger Monooxygenases (BVMOs): An Ancestral Family of Flavin Monooxygenases.PloS one · 2015Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Baeyer-Villiger monooxygenases (BVMOs) have been shown to play key roles for the biosynthesis of important natural products. MtmOIV, a homodimeric FAD- and NADPH-dependent BVMO, catalyzes the key frame-modifying steps of the mithramycin biosynthetic pathway, including an oxidative C-C bond cleavage, by converting its natural substrate premithramycin B into mithramycin DK, the immediate precursor of mithramycin. The drastically improved protein structure of MtmOIV along with the high-resolution structure of MtmOIV in complex with its natural substrate premithramycin B are reported here, revealing previously undetected key residues that are important for substrate recognition and catalysis. Kinetic analyses of selected mutants allowed us to probe the substrate binding pocket of MtmOIV and also to discover the putative NADPH binding site. This is the first substrate-bound structure of MtmOIV providing new insights into substrate recognition and catalysis, which paves the way for the future design of a tailored enzyme for the chemo-enzymatic preparation of novel mithramycin analogues.
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