ArticleNature communications2019
Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Article
- Selective ONature communications · 2026Article
- Self-Assembled Living Microreactors for Selective Microcystin Removal via Cascade Sieving, Adsorption and Biodegradation.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- The aldehyde dehydrogenase superfamilies: correlations and deviations in structure and function.Applied microbiology and biotechnology · 2025Review
- Structure-function analysis of 2-sulfamoylacetic acid synthase in altemicidin biosynthesis.The Journal of antibiotics · 2025Article
- Metabolism of oxyfluorfen by actinobacteriaFrontiers in microbiology · 2025Article
- Evaluation of Paraoxonase-1 Activity of Arylesterase and Lactonase and Their Correlation with Oxidative Stress in Children with Type 1 Diabetes Mellitus.Reports of biochemistry & molecular biology · 2024Article
- Factors affecting macromolecule orientations in thin films formed in cryo-EM.Acta crystallographica. Section D, Structural biology · 2024Article
- Biosynthesis of the bacterial antibiotic 3,7-dihydroxytropolone through enzymatic salvaging of catabolic shunt products.Chemical science · 2024Article
- Proteomic analysis of meropenem-induced outer membrane vesicles released by carbapenem-resistantMicrobiology spectrum · 2024Article
- Structure determination by cryoEM at 100 keV.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Progress in structural and functional study of the bacterial phenylacetic acid catabolic pathway, its role in pathogenicity and antibiotic resistance.Frontiers in microbiology · 2022Review
- Mechanisms and Effects of Substrate Channelling in Enzymatic Cascades.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Structural Characterization of Multienzyme Assemblies: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Bacterial Tropone Natural Products and Derivatives: Overview of their Biosynthesis, Bioactivities, Ecological Role and Biotechnological Potential.Chembiochem : a European journal of chemical biology · 2020Review
- Computational Methods for Single-Particle Electron Cryomicroscopy.Annual review of biomedical data science · 2020Review
- Five enzymes of the Arg/N-degron pathway form a targeting complex: The concept of superchanneling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
7 authors.
Funding
Abstract
Substrate channeling is a mechanism for the internal transfer of hydrophobic, unstable or toxic intermediates from the active site of one enzyme to another. Such transfer has previously been described to be mediated by a hydrophobic tunnel, the use of electrostatic highways or pivoting and by conformational changes. The enzyme PaaZ is used by many bacteria to degrade environmental pollutants. PaaZ is a bifunctional enzyme that catalyzes the ring opening of oxepin-CoA and converts it to 3-oxo-5,6-dehydrosuberyl-CoA. Here we report the structures of PaaZ determined by electron cryomicroscopy with and without bound ligands. The structures reveal that three domain-swapped dimers of the enzyme form a trilobed structure. A combination of small-angle X-ray scattering (SAXS), computational studies, mutagenesis and microbial growth experiments suggests that the key intermediate is transferred from one active site to the other by a mechanism of electrostatic pivoting of the CoA moiety, mediated by a set of conserved positively charged residues.
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