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Title of Journal: Curr Microbiol

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Abbravation: Current Microbiology

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Springer-Verlag

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DOI

10.1016/0146-6291(77)90376-9

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1432-0991

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Identification of the Critical Role of Tyr194 in

Authors: X Lu Y Yuan XL Xue GP Zhang SN Zhou
Publish Date: 2006/09/12
Volume: 53, Issue: 4, Pages: 346-350
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Abstract

Enzymatic disruption of quorumsensing QS pathways in pathogenic organisms is a promising antiinfection therapeutic strategy AHLlactonase a potent tool for biocontrol can hydrolyze QS signal molecule Nacylhomoserine lactones AHLs into inactive products thereby blocking the QS systems A marine bacterial isolate Y2 identified as a Bacillus cereus subsp was found capable of inactivating AHLs The aiiA gene encoding the AHLdegrading enzyme from bacterial strain Y2 was cloned and expressed in Escherichia coli The 28kDa recombinant Y2AiiA protein was purified and showed strong AHLdegrading activity Sequence comparisons of Y2aiiA with known AHLlactonases revealed high identities in the deduced aminoacid sequences Functional determination of a potential catalytic residue Tyr194 of AHLlactonases was performed by sitedirected mutagenesis As judged by AHLdegrading bioassay substitution of Tyr194 with Ala resulted in a dramatic decrease of activity compared with wildtype WT recombinant Y2AiiA although the expression level of the mutated Y2AiiA protein was equivalent to that of WT Y2AiiA These results suggested that the conserved residue Tyr194 is critical for catalytic function of the novel AHLlactonase

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