in the biosynthetis of paerucumarin, PvcA generates an isonitrile-functionalized tyrosine, (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate, that is oxidized by PvcB to give the unsaturated intermediate compound (2E)-3-(4-hydroxyphenyl)-2-isocyanoprop-2-enoate. Oxidation of this compound to a catechol by PvcC/D, followed by intermolecular cyclization of the catechol and the carboxylate, gives paerucumarin. Pseudomonas aeruginosa strains produced a different ratio of paerucumarin to pseudoverdine. PAO1 produces almost exclusively paerucumarin, while PA14 produces approximately a one-to-one mixture of paerucumarin and pseudoverdine
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structure of the PvcB protein, PvcB is a member of the Fe2+/alpha-ketoglutarate dependent oxygenase family of enzymes. A conformational change to order several loops will accompany the binding of ligands
to 2.0 A resolution. The aromatic ring of the substrate binds in a hydrophobic pocket formed by Met114, Tyr115, and Leu116, with potential contributions from Trp83, as well. The carboxyl group of the tyrosine isonitrile does not interact directly with any positively charged residues