Abstract
The Irp9 protein of Yersinia enterocolitica participates in the synthesis of salicylate, the precursor of the siderophore yersiniabactin. In Pseudomonas species, salicylate synthesis is mediated by two enzymes: isochorismate synthase and isochorismate pyruvate-lyase. Both enzymes are required for complementation of a Yersinia irp9 mutant. However, irp9 is not able to complement Escherichia coli entC for the production of enterobactin, which requires isochorismate as a precursor. These results suggest that Irp9 directly converts chorismate into salicylate.
MeSH Terms
Bacterial Proteins/genetics,metabolism
Chorismic Acid/metabolism
Cyclohexenes
Escherichia coli/genetics,metabolism
Genetic Complementation Test
Hydroxybenzoates/pharmacology
Intramolecular Transferases/genetics,metabolism
Lyases/genetics,metabolism
Multigene Family
Mutation
Oxo-Acid-Lyases/genetics,metabolism
Phenols
Protein Precursors/metabolism
Pseudomonas fluorescens/genetics
Salicylates/metabolism
Siderophores/metabolism
Thiazoles
Virulence/genetics
Yersinia enterocolitica/drug effects,metabolism,pathogenicity
Chemicals
Bacterial Proteins
Cyclohexenes
Hydroxybenzoates
Phenols
Protein Precursors
Salicylates
Siderophores
Thiazoles
yersiniabactin
chrome azurol S
isochorismic acid
Lyases
salicylate synthetase
Oxo-Acid-Lyases
chorismate pyruvate lyase
Intramolecular Transferases
isochorismate synthase
Chorismic Acid
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pelludat Cosima
Institut für Mikrobiologie, D-BIOL, ETHZ, 8092 Zürich, Switzerland.
Brem Daniela
Heesemann Jürgen
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