ArticleThe Journal of biological chemistry2011
Defining a structural and kinetic rationale for paralogous copies of phenylacetate-CoA ligases from the cystic fibrosis pathogen Burkholderia cenocepacia J2315.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Enzymatic Basis for the Oxidative Branch of Aromatic Amino Acid Fermentation Leading to p-cresol Formation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Conservation, origin, and remodeling of the phenyl acetate degradation pathway.Microbial genomics · 2026Article
- Genomic perplexity and the evolution of context-dependent function.Molecular biology and evolution · 2026Article
- Enzymatic synthesis of azide by a promiscuous N-nitrosylase.Nature chemistry · 2024Article
- Characterization of 2-phenanthroate:CoA ligase from the sulfate-reducing, phenanthrene-degrading enrichment culture TRIP.Applied and environmental microbiology · 2024Article
- Isophthalate:coenzyme A ligase initiates anaerobic degradation of xenobiotic isophthalate.BMC microbiology · 2022Article
- Cryo-EM structure of the fatty acid reductase LuxC-LuxE complex provides insights into bacterial bioluminescence.The Journal of biological chemistry · 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
- Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily.Applied and environmental microbiology · 2021Review
- Bacterial Tropone Natural Products and Derivatives: Overview of their Biosynthesis, Bioactivities, Ecological Role and Biotechnological Potential.Chembiochem : a European journal of chemical biology · 2020Review
- Molecular Mechanisms of Bacterial Bioluminescence.Computational and structural biotechnology journal · 2018Review
- Crystal structure of the thioesterification conformation ofThe Journal of biological chemistry · 2017Article
- Structural Insights into Anthranilate Priming during Type II Polyketide Biosynthesis.ACS chemical biology · 2016Article
- Metabolism of β-valine via a CoA-dependent ammonia lyase pathway.Applied microbiology and biotechnology · 2015Article
- Review
- Domain atrophy creates rare cases of functional partial protein domains.Genome biology · 2015Article
- The ecology of bacterial genes and the survival of the new.International journal of evolutionary biology · 2012Article
- 3-Hydroxyphenylacetic acid induces the Burkholderia cenocepacia phenylacetic acid degradation pathway - toward understanding the contribution of aromatic catabolism to pathogenesis.Frontiers in cellular and infection microbiology · 2011Article
Corrections and comments
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2 authors at 1 institution in 1 country.
Funding
Abstract
The phenylacetic acid (PAA) degradation pathway is the sole aerobic route for phenylacetic acid metabolism in bacteria and facilitates degradation of environmental pollutants such as styrene and ethylbenzene. The PAA pathway also is implicated in promoting Burkholderia cenocepacia infections in cystic fibrosis patients. Intriguingly, the first enzyme in the PAA pathway is present in two copies (paaK1 and paaK2), yet each subsequent enzyme is present in only a single copy. Furthermore, sequence divergence indicates that PaaK1 and PaaK2 form a unique subgroup within the adenylate-forming enzyme (AFE) superfamily. To establish a biochemical rationale for the existence of the PaaK paralogs in B. cenocepacia, we present high resolution x-ray crystal structures of a selenomethionine derivative of PaaK1 in complex with ATP and adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 in distinct conformations. Structural analysis reveals a novel N-terminal microdomain that may serve to recruit subsequent PAA enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2. The potential for different kinetic profiles was suggested by a structurally divergent extension of the aryl substrate pocket in PaaK1 relative to PaaK2. Functional characterization confirmed this prediction, with PaaK1 possessing a lower K(m) for phenylacetic acid and better able to accommodate 3' and 4' substitutions on the phenyl ring. Collectively, these results offer detailed insight into the reaction mechanism of a novel subgroup of the AFE superfamily and provide a clear biochemical rationale for the presence of paralogous copies of PaaK of B. cenocepacia.
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