chrome-azurol-s and isochorismic-acid

chrome-azurol-s has been researched along with isochorismic-acid* in 1 studies

Other Studies

1 other study(ies) available for chrome-azurol-s and isochorismic-acid

Article	Year
Irp9, encoded by the high-pathogenicity island of Yersinia enterocolitica, is able to convert chorismate into salicylate, the precursor of the siderophore yersiniabactin. Journal of bacteriology, 2003, Volume: 185, Issue:18 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. Topics: Bacterial Proteins; Chorismic Acid; Cyclohexenes; Escherichia coli; Genetic Complementation Test; Hydroxybenzoates; Intramolecular Transferases; Lyases; Multigene Family; Mutation; Oxo-Acid-Lyases; Phenols; Protein Precursors; Pseudomonas fluorescens; Salicylates; Siderophores; Thiazoles; Virulence; Yersinia enterocolitica	2003

Article

Year

Irp9, encoded by the high-pathogenicity island of Yersinia enterocolitica, is able to convert chorismate into salicylate, the precursor of the siderophore yersiniabactin.

Journal of bacteriology, 2003, Volume: 185, Issue:18

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.

Topics: Bacterial Proteins; Chorismic Acid; Cyclohexenes; Escherichia coli; Genetic Complementation Test; Hydroxybenzoates; Intramolecular Transferases; Lyases; Multigene Family; Mutation; Oxo-Acid-Lyases; Phenols; Protein Precursors; Pseudomonas fluorescens; Salicylates; Siderophores; Thiazoles; Virulence; Yersinia enterocolitica

2003