ArticleBiochemistry2014
Acyl-ACP substrate recognition in Burkholderia mallei BmaI1 acyl-homoserine lactone synthase.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The acquisition of additional control over quorum sensing regulation reduces the variability of final cell density in Burkholderia.Communications biology · 2025Article
- Article
- Quorum sensing modulates bacterial virulence and colonization dynamics of the gastrointestinal pathogenGut microbes · 2023Article
- Article
- Carrier protein mediated cargo sensing in quorum signal synthases.Chemical communications (Cambridge, England) · 2023Article
- The Role of Quorum Sensing Molecules in Bacterial-Plant Interactions.Metabolites · 2023Review
- Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria.Molecules (Basel, Switzerland) · 2022Review
- Structural insights into acyl-ACP selective recognition by the Aeromonas hydrophila AHL synthase AhyI.BMC microbiology · 2021Article
- Complete genome sequence of fish-pathogenic Aeromonas hydrophila HX-3 and a comparative analysis: insights into virulence factors and quorum sensing.Scientific reports · 2020Article
- Enzymatic Assays to Investigate Acyl-Homoserine Lactone Autoinducer Synthases.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Molecular basis for the substrate specificity of quorum signal synthases.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Interplay between 4-Hydroxy-3-Methyl-2-Alkylquinoline andFrontiers in microbiology · 2017Article
- A Comparative Analysis of Acyl-Homoserine Lactone Synthase Assays.Chembiochem : a European journal of chemical biology · 2015Article
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Authors and funding
6 authors.
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Abstract
The acyl-homoserine lactone (AHL) autoinducer mediated quorum sensing regulates virulence in several pathogenic bacteria. The hallmark of an efficient quorum sensing system relies on the tight specificity in the signal generated by each bacterium. Since AHL signal specificity is derived from the acyl-chain of the acyl-ACP (ACP = acyl carrier protein) substrate, AHL synthase enzymes must recognize and react with the native acyl-ACP with high catalytic efficiency while keeping reaction rates with non-native acyl-ACPs low. The mechanism of acyl-ACP substrate recognition in these enzymes, however, remains elusive. In this study, we investigated differences in catalytic efficiencies for shorter and longer chain acyl-ACP substrates reacting with an octanoyl-homoserine lactone synthase Burkholderia mallei BmaI1. With the exception of two-carbon shorter hexanoyl-ACP, the catalytic efficiencies of butyryl-ACP, decanoyl-ACP, and octanoyl-CoA reacting with BmaI1 decreased by greater than 20-fold compared to the native octanoyl-ACP substrate. Furthermore, we also noticed kinetic cooperativity when BmaI1 reacted with non-native acyl-donor substrates. Our kinetic data suggest that non-native acyl-ACP substrates are unable to form a stable and productive BmaI1·acyl-ACP·SAM ternary complex and are thus effectively discriminated by the enzyme. These results offer insights into the molecular basis of substrate recognition for the BmaI1 enzyme.
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