This drawback would interfere with the development of AHL-lactonase as peptide drugs. Since AHL-acylases have none of the drawbacks described above, Aac could become a potential quorum-quenching agent in the near feature. Conclusion This paper describes the identification of AHL-acylase, Aac, from R. solanacearumGMI1000 with ESI-MS mass spectrometry analysis and whole cell bioassay, together
with the analysis of MIC test of aculeacin A. The results showed strong evidence that the Aac in R. solanacearumGMI1000 functions as an AHL-acylase and not an aculeacin A acylase. Thus, we Akt inhibitor review consider that renaming the aac gene of R. solanacearumGMI1000 as “”the alaS gene”" is necessary in further studies for the purpose of clarity. Moreover, this is the first report to find an AHL-acylase in a phytopathogen. Acknowledgements We would like to thank Dr. Christian Boucher (INRA-CNRS, France) for kindly Protein Tyrosine Kinase inhibitor providing us E. coli CA027ZC09, Dr. Paul Williams (University of Nottingham, UK) for kindly rendering us C. violaceum CV026, and the reviewers useful suggestions. This work was supported by the Frontier and Innovative Research of National Taiwan University under project number 96R0105. References 1. Swift S, Downie JA, Whitehead NA, Barnard AM, Salmond GP, Williams P: Quorum sensing as a population-density-dependent
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