AI Article Synopsis
- The study highlights the importance of posttranslational isoprenylation of tryptophan in the function of the Bacillus quorum sensing pheromone, ComX.
- A modifying enzyme named ComQ is responsible for converting the ComX precursor into ComX pheromone and shows similarities to isoprenyl pyrophosphate synthases.
- Research focused on a specific non-conserved region of ComQ revealed that a conserved aspartic acid is crucial for the enzyme’s activity and its ability to bind to ComX, enhancing our understanding of tryptophan isoprenylation mechanisms.
Article Abstract
Posttranslational isoprenylation of a tryptophan residue identified from Bacillus quorum sensing pheromone, ComX pheromone, is unique and essential for the bioactivity. A modifying enzyme, ComQ, forms ComX pheromone from the ComX precursor and isoprenyl pyrophosphate and exhibits moderate similarity to isoprenyl pyrophosphate synthases. We investigated non-conserved region in ComQ, corresponding to isopentenyl pyrophosphate binding region of the synthases, using in vitro cell-free isoprenylation. These results suggested that the only conserved aspartic acid residue in the region of ComQ is critical for enzyme activity and responsible for ComX binding. Our findings should contribute to basic understanding of the mechanism of tryptophan isoprenylation.
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| http://dx.doi.org/10.1080/09168451.2014.891932 | DOI Listing |
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