Статья

The Quorum-Quenching Lactonase from <i>Bacillus thuringiensis</i> Is a Metalloprotein

Pei W. ThomasDivision of Medicinal Chemistry, College of Pharmacy, Graduate Programs in Biochemistry and Cell and Molecular Biology, and The Center for Molecular and Cellular Toxicology, The University of Texas at Austin, Austin, Texas 78712, and Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131Everett StoneDivision of Medicinal Chemistry, College of Pharmacy, Graduate Programs in Biochemistry and Cell and Molecular Biology, and The Center for Molecular and Cellular Toxicology, The University of Texas at Austin, Austin, Texas 78712, and Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131Alison L. CostelloDivision of Medicinal Chemistry, College of Pharmacy, Graduate Programs in Biochemistry and Cell and Molecular Biology, and The Center for Molecular and Cellular Toxicology, The University of Texas at Austin, Austin, Texas 78712, and Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131David L. TierneyDivision of Medicinal Chemistry, College of Pharmacy, Graduate Programs in Biochemistry and Cell and Molecular Biology, and The Center for Molecular and Cellular Toxicology, The University of Texas at Austin, Austin, Texas 78712, and Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131Walter FastDivision of Medicinal Chemistry, College of Pharmacy, Graduate Programs in Biochemistry and Cell and Molecular Biology, and The Center for Molecular and Cellular Toxicology, The University of Texas at Austin, Austin, Texas 78712, and Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131

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ABI

Аннотация

Lactonases from Bacillus species hydrolyze the N-acylhomoserine lactone (AHL) signaling molecules used in quorum-sensing pathways of many Gram-negative bacteria, including Pseudomonas aeruginosa and Erwinia carotovora, both significant pathogens. Because of sequence similarity, these AHL lactonases have been assigned to the metallo-beta-lactamase superfamily of proteins, which includes metalloenzymes of diverse activity, mechanism, and metal content. However, a recent study claims that AHL lactonase from Bacillus sp. 240B1 is not a metalloprotein [Wang, L. H., et al. (2004) J. Biol. Chem. 279, 13645]. Here, the gene for an AHL lactonase from Bacillus thuringiensis is cloned, and the protein is expressed, purified, and found to bind 2 equiv of zinc. The metal-bound form of AHL lactonase catalyzes the hydrolysis of N-hexanoyl-(S)-homoserine lactone but not the (R) enantiomer. Removal of both zinc ions results in loss of activity, and reconstitution with zinc restores activity, indicating the importance of metal ions for catalytic activity. Metal content, sequence alignments, and X-ray absorption spectroscopy of the zinc-containing lactonase all support a proposed dinuclear zinc binding site similar to that found in glyoxalase II.

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Идентификаторы

DOI: 10.1021/bi050050m

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