ArticleThe Journal of biological chemistry2011
Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
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- Efficient and sustainable removal of linear alkylbenzene sulfonate in a membrane biofilm: Oxygen supply dosage impacts mineralization pathway.Water research X · 2024Article
- Biosynthesis of the bacterial antibiotic 3,7-dihydroxytropolone through enzymatic salvaging of catabolic shunt products.Chemical science · 2024Article
- Three Rings to Rule Them All: How Versatile Flavoenzymes Orchestrate the Structural Diversification of Natural Products.Biochemistry · 2022Article
- Progress in structural and functional study of the bacterial phenylacetic acid catabolic pathway, its role in pathogenicity and antibiotic resistance.Frontiers in microbiology · 2022Review
- A Flavoprotein Dioxygenase Steers Bacterial Tropone Biosynthesis via Coenzyme A-Ester Oxygenolysis and Ring Epoxidation.Journal of the American Chemical Society · 2021Article
- Bacterial Tropone Natural Products and Derivatives: Overview of their Biosynthesis, Bioactivities, Ecological Role and Biotechnological Potential.Chembiochem : a European journal of chemical biology · 2020Review
- Epoxidation Catalyzed by the Nonheme Iron(II)- and 2-Oxoglutarate-Dependent Oxygenase, AsqJ: Mechanistic Elucidation of Oxygen Atom Transfer by a Ferryl Intermediate.Journal of the American Chemical Society · 2020Article
- Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway.Nature communications · 2019Article
- Effect of UV irradiation on Sulfolobus acidocaldarius and involvement of the general transcription factor TFB3 in the early UV response.Nucleic acids research · 2018Article
- A robust platform for chemical genomics in bacterial systems.Molecular biology of the cell · 2016Article
- An event-driven approach for studying gene block evolution in bacteria.Bioinformatics (Oxford, England) · 2015Article
- Review
- Mechanism and selectivity of the dinuclear iron benzoyl-coenzyme A epoxidase BoxB.Chemical science · 2015Article
- Evolution of the cytosolic iron-sulfur cluster assembly machinery in Blastocystis species and other microbial eukaryotes.Eukaryotic cell · 2014Article
- Protein-protein interactions in the β-oxidation part of the phenylacetate utilization pathway: crystal structure of the PaaF-PaaG hydratase-isomerase complex.The Journal of biological chemistry · 2012Article
- Epoxy Coenzyme A Thioester pathways for degradation of aromatic compounds.Applied and environmental microbiology · 2012Review
- Canadian macromolecular crystallography facility: a suite of fully automated beamlines.Journal of structural and functional genomics · 2012Article
- Article
- Microbial degradation of aromatic compounds - from one strategy to four.Nature reviews. Microbiology · 2011Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The utilization of phenylacetic acid (PA) in Escherichia coli occurs through a hybrid pathway that shows features of both aerobic and anaerobic metabolism. Oxygenation of the aromatic ring is performed by a multisubunit phenylacetyl-coenzyme A oxygenase complex that shares remote homology of two subunits to well studied bacterial multicomponent monooxygenases and was postulated to form a new bacterial multicomponent monooxygenase subfamily. We expressed the subunits PaaA, B, C, D, and E of the PA-CoA oxygenase and showed that PaaABC, PaaAC, and PaaBC form stable subcomplexes that can be purified. In vitro reconstitution of the oxygenase subunits showed that each of the PaaA, B, C, and E subunits are necessary for catalysis, whereas PaaD is not essential. We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. We conclude that PaaAC forms a catalytic core with a monooxygenase fold with PaaA being the catalytic α subunit and PaaC, the structural β subunit. PaaAC forms heterotetramers that are organized very differently from other known multisubunit monooxygenases and lacks their conservative network of hydrogen bonds between the di-iron center and protein surface, suggesting different association with the reductase and different mechanisms of electron transport. The PaaA structure shows adaptation of the common access route to the active site for binding a CoA-bound substrate. The enzyme-substrate complex shows the orientation of the aromatic ring, which is poised for oxygenation at the ortho-position, in accordance with the expected chemistry. The PA-CoA oxygenase complex serves as a paradigm for the new subfamily multicomponent monooxygenases comprising several hundred homologs.
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