@article{2328, keywords = {Gene Expression Regulation, Bacterial, Quorum Sensing, Escherichia coli, Vibrio cholerae, Bacterial Proteins, Ketones, Substrate Specificity, Cholera, Acyl Coenzyme A, Cloning, Molecular, Kinetics, Pyridoxal Phosphate, Recombinant Proteins, S-Adenosylmethionine, Transaminases}, author = {Yunzhou Wei and Lark Perez and Wai-Leung Ng and Martin Semmelhack and Bonnie Bassler}, title = {Mechanism of Vibrio cholerae autoinducer-1 biosynthesis.}, abstract = {

Vibrio cholerae, the causative agent of the disease cholera, uses a cell to cell communication process called quorum sensing to control biofilm formation and virulence factor production. The major V. cholerae quorum-sensing signal CAI-1 has been identified as (S)-3-hydroxytridecan-4-one, and the CqsA protein is required for CAI-1 production. However, the biosynthetic route to CAI-1 remains unclear. Here we report that (S)-adenosylmethionine (SAM) is one of the two biosynthetic substrates for CqsA. CqsA couples SAM and decanoyl-coenzyme A to produce a previously unknown but potent quorum-sensing molecule, 3-aminotridec-2-en-4-one (Ea-CAI-1). The CqsA mechanism is unique; it combines two enzymatic transformations, a β,γ-elimination of SAM and an acyltransferase reaction into a single PLP-dependent catalytic process. Ea-CAI-1 is subsequently converted to CAI-1, presumably through the intermediate tridecane-3,4-dione (DK-CAI-1). We propose that the Ea-CAI-1 to DK-CAI-1 conversion occurs spontaneously, and we identify the enzyme responsible for the subsequent step: conversion of DK-CAI-1 into CAI-1. SAM is the substrate for the synthesis of at least three different classes of quorum-sensing signal molecules, indicating that bacteria have evolved a strategy to leverage an abundant substrate for multiple signaling purposes.

}, year = {2011}, journal = {ACS Chem Biol}, volume = {6}, pages = {356-65}, month = {2011 Apr 15}, issn = {1554-8937}, doi = {10.1021/cb1003652}, language = {eng}, }