ArticleJournal of the American Chemical Society2012
Roles of the synergistic reductive O-methyltransferase GilM and of O-methyltransferase GilMT in the gilvocarcin biosynthetic pathway.
Article in Journal of the American Chemical Society, 2012. 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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Who cites it
6 citing papers in PubMed.
- Metabolic Blockade-Based Genome Mining of Sea Anemone-AssociatedMarine drugs · 2024Article
- Engineering BioBricks for Deoxysugar Biosynthesis and Generation of New Tetracenomycins.ACS omega · 2023Article
- Review
- The functional differentiation of the post-PKS tailoring oxygenases contributed to the chemical diversities of atypical angucyclines.Synthetic and systems biotechnology · 2018Review
- Baeyer-Villiger C-C bond cleavage reaction in gilvocarcin and jadomycin biosynthesis.Journal of the American Chemical Society · 2012Article
- Cooperation of two bifunctional enzymes in the biosynthesis and attachment of deoxysugars of the antitumor antibiotic mithramycin.Angewandte Chemie (International ed. in English) · 2012Article
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Authors and funding
6 authors.
Funding
Abstract
Two enzymes of the gilvocarcin biosynthetic pathway, GilMT and GilM, with unclear functions were investigated by in vitro studies using purified, recombinant enzymes along with synthetically prepared intermediates. The studies revealed GilMT as a typical S-adenosylmethionine (SAM) dependent O-methyltransferase, but GilM was identified as a pivotal enzyme in the pathway that exhibits dual functionality in that it catalyzes a reduction of a quinone intermediate to a hydroquinone, which goes hand-in-hand with a stabilizing O-methylation and a hemiacetal formation. GilM mediates its reductive catalysis through the aid of GilR that provides FADH(2) for the GilM reaction, through which FAD is regenerated for the next catalytic cycle. This unusual synergy eventually completes the biosynthesis of the polyketide-derived defuco-gilvocarcin chromphore.
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Registered trials
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