Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 1. Product-Bound Structures†‡

@inproceedings{Liu2008MechanismOT,
  title={Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 1. Product-Bound Structures†‡},
  author={Dali Liu and Jessica Momb and Pei Wang Thomas and Aaron Moulin and Gregory A. Petsko and Walter Fast and Dagmar Ringe},
  booktitle={Biochemistry},
  year={2008}
}
Enzymes capable of hydrolyzing N-acyl- l-homoserine lactones (AHLs) used in some bacterial quorum-sensing pathways are of considerable interest for their ability to block undesirable phenotypes. Most known AHL hydrolases that catalyze ring opening (AHL lactonases) are members of the metallo-beta-lactamase enzyme superfamily and rely on a dinuclear zinc site for catalysis and stability. Here we report the three-dimensional structures of three product complexes formed with the AHL lactonase from… CONTINUE READING

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