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Quorum-Quenching Acylases in Pseudomonas aeruginosa

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Pseudomonas

The β-lactam acylases, mostly found by screening samples from natural sources, represent a unique family of heterodimeric N-terminal nucleophile hydrolases. Interestingly, most of the strains found producing β-lactam acylases are Pseudomonas species. We have shown that these enzymes show high selectivity towards the acid side chain, but are far more promiscuous with regard to the amine moiety of the substrate. It is therefore highly unlikely that the industrially relevant deacylation of β-lactam compounds has evolved specifically in nature. Interestingly, no less than four putative acylases of the N-terminal nucleophile family have been identified in the Pseudomonas aeruginosa PAO1 genome. We have investigated these four putative acylases of which one could be expressed in Escherichia coli. Interestingly, the enzyme was found to catalyse the hydrolysis of acylhomoserine- lactones as reported for Ralstonia acylase suggesting a role in quorum quenching.

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Authors and Affiliations

  1. Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713, Groningen, AV, The Netherlands

    Joanna Krzeslak, Wim J. Quax & Mariana Wahjudi

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  1. Joanna Krzeslak
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  1. Estación Experimental del Zaidín – CSIC, E-18008, Granada, Spain

    Juan-Luis Ramos

  2. Institut de Biologie Structurale et Microbiologie, CNRS, 13402 Marseille Cedex 20, France

    Alain Filloux

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Krzeslak, J., Quax, W.J., Wahjudi, M. (2007). Quorum-Quenching Acylases in Pseudomonas aeruginosa. In: Ramos, JL., Filloux, A. (eds) Pseudomonas. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6097-7_15

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