ArticleFEMS microbiology letters2009
Characterization of SgcE6, the flavin reductase component supporting FAD-dependent halogenation and hydroxylation in the biosynthesis of the enediyne antitumor antibiotic C-1027.
Article in FEMS microbiology letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- The X-Ray Crystal Structure of BorF, the Flavin Reductase Subunit of a Two-Component Flavin-Dependent Tryptophan Halogenase.Proteins · 2026Article
- Exploring the role of flavin-dependent monooxygenases in the biosynthesis of aromatic compounds.Biotechnology for biofuels and bioproducts · 2024Review
- MolDiscovery: learning mass spectrometry fragmentation of small molecules.Nature communications · 2021Article
- Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.Biology · 2018Review
- Article
- Genome neighborhood network reveals insights into enediyne biosynthesis and facilitates prediction and prioritization for discovery.Journal of industrial microbiology & biotechnology · 2016Article
- Nonproteinogenic amino acid building blocks for nonribosomal peptide and hybrid polyketide scaffolds.Angewandte Chemie (International ed. in English) · 2013Review
- Cloning and sequencing of the kedarcidin biosynthetic gene cluster from Streptoalloteichus sp. ATCC 53650 revealing new insights into biosynthesis of the enediyne family of antitumor antibiotics.Molecular bioSystems · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The C-1027 enediyne antitumor antibiotic from Streptomyces globisporus possesses an (S)-3-chloro-5-hydroxy-beta-tyrosine moiety, the chloro- and hydroxy-substituents of which are installed by a flavin-dependent halogenase SgcC3 and monooxygenase SgcC, respectively. Interestingly, a single flavin reductase, SgcE6, can provide reduced flavin to both enzymes. Bioinformatics analysis reveals that, similar to other flavin reductases involved in natural product biosynthesis, SgcE6 belongs to the HpaC-like subfamily of the Class I flavin reductases. The present study describes the steady-state kinetic characterization of SgcE6 as a strictly NADH- and FAD-specific enzyme.
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