ArticleProceedings of the National Academy of Sciences of the United States of America2004
Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 99 citations in OpenAlex.
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- Phenazines are involved in the antagonism of a novel subspecies of Pseudomonas chlororaphis strain S1Bt23 against Pythium ultimum.Scientific reports · 2024Article
- Phenazine biosynthesis protein MoPhzF regulates appressorium formation and host infection through canonical metabolic and noncanonical signaling function in Magnaporthe oryzae.The New phytologist · 2024Article
- Recent Developments in the Biological Activities, Bioproduction, and Applications ofMolecules (Basel, Switzerland) · 2023Review
- Beyond the ABCs-Discovery of Three New Plasmid Types inMicroorganisms · 2022Article
- Genetic engineering of Pseudomonas chlororaphis Lzh-T5 to enhance production of trans-2,3-dihydro-3-hydroxyanthranilic acid.Scientific reports · 2021Article
- Functional genomics study of Pseudomonas putida to determine traits associated with avoidance of a myxobacterial predator.Scientific reports · 2021Article
- Proteomic Characterization of Antibiotic Resistance inInternational journal of molecular sciences · 2021Article
- Jekyll or Hyde? The genome (and more) of Nesidiocoris tenuis, a zoophytophagous predatory bug that is both a biological control agent and a pest.Insect molecular biology · 2021Article
- Metabolic Potential, Ecology and Presence of Associated Bacteria Is Reflected in Genomic Diversity of Mucoromycotina.Frontiers in microbiology · 2021Article
- Alteration of the Route to Menaquinone towards Isochorismate-Derived Metabolites.Chembiochem : a European journal of chemical biology · 2019Article
- Novel pathway of 3-hydroxyanthranilic acid formation in limazepine biosynthesis reveals evolutionary relation between phenazines and pyrrolobenzodiazepines.Scientific reports · 2018Article
- Mechanisms and Specificity of Phenazine Biosynthesis Protein PhzF.Scientific reports · 2017Article
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- Reverse Methanogenesis and Respiration in Methanotrophic Archaea.Archaea (Vancouver, B.C.) · 2017Review
- Comparative genomics of pyridoxal 5'-phosphate-dependent transcription factor regulons inMicrobial genomics · 2016Article
- New Concept of the Biosynthesis of 4-Alkyl-L-Proline Precursors of Lincomycin, Hormaomycin, and Pyrrolobenzodiazepines: Could a γ-Glutamyltransferase Cleave the C-C Bond?Frontiers in microbiology · 2016Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Phenazines produced by Pseudomonas and Streptomyces spp. are heterocyclic nitrogen-containing metabolites with antibiotic, antitumor, and antiparasitic activity. The antibiotic properties of pyocyanin, produced by Pseudomonas aeruginosa, were recognized in the 1890s, although this blue phenazine is now known to be a virulence factor in human disease. Despite their biological significance, the biosynthesis of phenazines is not fully understood. Here we present structural and functional studies of PhzF, an enzyme essential for phenazine synthesis in Pseudomonas spp. PhzF shares topology with diaminopimelate epimerase DapF but lacks the same catalytic residues. The structure of PhzF in complex with its substrate, trans-2,3-dihydro-3-hydroxyanthranilic acid, suggests that it is an isomerase using the conserved glutamate E45 to abstract a proton from C3 of the substrate. The proton is returned to C1 of the substrate after rearrangement of the double-bond system, yielding an enol that converts to the corresponding ketone. PhzF is a dimer that may be bifunctional, providing a shielded cavity for ketone dimerization via double Schiff-base formation to produce the phenazine scaffold. Our proposed mechanism is supported by mass and NMR spectroscopy. The results are discussed in the context of related structures and protein sequences of unknown biochemical function.
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