ArticleBiochemistry2009
Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway .
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 85 citations in OpenAlex.
- Sustainable Biocatalytic Cascades: A Versatile Tool in the Synthesis of Natural Products With Therapeutic Potential.Chembiochem : a European journal of chemical biology · 2026Review
- A Hooker Oxygenase Archetype in Polyketide Biosynthesis Challenging the Baeyer-Villiger Monooxygenase Paradigm.Journal of the American Chemical Society · 2026Article
- Genome Mining and Genetic Manipulation Reveal New Isofuranonaphthoquinones inInternational journal of molecular sciences · 2024Article
- A flavin-monooxygenase catalyzing oxepinone formation and the complete biosynthesis of vibralactone.Nature communications · 2023Article
- Deciphering Chemical Mediators Regulating Specialized Metabolism in a Symbiotic Cyanobacterium.Angewandte Chemie (International ed. in English) · 2022Article
- Structure-Activity Relationships of Pyrazolo[1,5-ACS infectious diseases · 2021Article
- Discovery of a Cryptic Intermediate in Late Steps of Mithramycin Biosynthesis.Angewandte Chemie (International ed. in English) · 2020Article
- Article
- Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019Review
- Article
- Biosynthesis of Rishirilide B.Antibiotics (Basel, Switzerland) · 2018Article
- Substitution of a Single Amino Acid Reverses the Regiospecificity of the Baeyer-Villiger Monooxygenase PntE in the Biosynthesis of the Antibiotic Pentalenolactone.Biochemistry · 2016Article
- Insights into Complex Oxidation during BE-7585A Biosynthesis: Structural Determination and Analysis of the Polyketide Monooxygenase BexE.ACS chemical biology · 2016Article
- Biosynthesis: A carbonate architect emerges.Nature chemical biology · 2014Article
- Molecular insight into substrate recognition and catalysis of Baeyer-Villiger monooxygenase MtmOIV, the key frame-modifying enzyme in the biosynthesis of anticancer agent mithramycin.ACS chemical biology · 2013Article
- Antimicrobial drug resistance affects broad changes in metabolomic phenotype in addition to secondary metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Mutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivity.FEBS open bio · 2013Article
- Flavoenzymes: versatile catalysts in biosynthetic pathways.Natural product reports · 2013Review
- Baeyer-Villiger C-C bond cleavage reaction in gilvocarcin and jadomycin biosynthesis.Journal of the American Chemical Society · 2012Article
- Identification of a novel Baeyer-Villiger monooxygenase from Acinetobacter radioresistens: close relationship to the Mycobacterium tuberculosis prodrug activator EtaA.Microbial biotechnology · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Baeyer-Villiger monooxygenases (BVMOs), mostly flavoproteins, were shown to be powerful biocatalysts for synthetic organic chemistry applications and were also suggested to play key roles for the biosyntheses of various natural products. Here we present the three-dimensional structure of MtmOIV, a 56 kDa homodimeric FAD- and NADPH-dependent monooxygenase, which catalyzes the key frame-modifying step of the mithramycin biosynthetic pathway and currently the only BVMO proven to react with its natural substrate via a Baeyer-Villiger reaction. MtmOIV's structure was determined by X-ray crystallography using molecular replacement to a resolution of 2.9 A. MtmOIV cleaves a C-C bond, essential for the conversion of the biologically inactive precursor, premithramycin B, into the active drug mithramycin. The MtmOIV structure combined with substrate docking calculations and site-directed mutagenesis experiments identifies several residues that participate in cofactor and substrate binding. Future experimentation aimed at broadening the substrate specificity of the enzyme could facilitate the generation of chemically diverse mithramycin analogues through combinatorial biosynthesis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.