Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate Modeling and Active Site Mutations†

@inproceedings{Momb2008MechanismOT,
  title={Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate Modeling and Active Site Mutations†},
  author={Jessica Momb and Canhui Wang and Dali Liu and Pei Wang Thomas and Gregory A. Petsko and Hua Zhong Guo and Dagmar Ringe and Walter Fast},
  booktitle={Biochemistry},
  year={2008}
}
The N-acyl- l-homoserine lactone hydrolases (AHL lactonases) have attracted considerable attention because of their ability to quench AHL-mediated quorum-sensing pathways in Gram-negative bacteria and because of their relation to other enzymes in the metallo-beta-lactamase superfamily. To elucidate the detailed catalytic mechanism of AHL lactonase, mutations are made on residues that presumably contribute to substrate binding and catalysis. Steady-state kinetic studies are carried out on both… CONTINUE READING
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