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Originally published In Press as doi:10.1074/jbc.M212324200 on March 6, 2003

J. Biol. Chem., Vol. 278, Issue 19, 16893-16898, May 9, 2003
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Isochorismate Synthase (PchA), the First and Rate-limiting Enzyme in Salicylate Biosynthesis of Pseudomonas aeruginosa*

Catherine Gaille, Cornelia Reimmann, and Dieter HaasDagger

From the Institut de Microbiologie Fondamentale, Université de Lausanne, CH-1015 Lausanne, Switzerland

In Pseudomonas aeruginosa the extracellular metabolite and siderophore pyochelin is synthesized from two major precursors, chorismate and L-cysteine via salicylate as an intermediate. The regulatory role of isochorismate synthase, the first enzyme in the pyochelin biosynthetic pathway, was studied. This enzyme is encoded by pchA, the last gene in the pchDCBA operon. The PchA protein was purified to apparent electrophoretic homogeneity from a PchA-overexpressing P. aeruginosa strain. The native enzyme was a 52-kDa monomer in solution, and its activity strictly depended on Mg2+. At pH 7.0, the optimum, a Km = 4.5 µM and a kcat = 43.1 min-1 were determined for chorismate. No feedback inhibitors or other allosteric effectors were found. The intracellular PchA concentration critically determined the rate of salicylate formation both in vitro and in vivo. In cultures grown in iron-limiting media to high cell densities, overexpression of the pchA gene resulted in overproduction of salicylate as well as in enhanced pyochelin formation. From this work and earlier studies, it is proposed that one important factor influencing the flux through the pyochelin biosynthetic pathway is the PchA concentration, which is determined at a transcriptional level, with pyochelin acting as a positive signal and iron as a negative signal.

* This work was supported by Swiss National Foundation for Scientific Research Grant 31-56608.99.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 41-21-692-56-31; Fax: 41-21-692-56-35; E-mail: Dieter.Haas@imf.unil.ch.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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