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Appl. Environ. Microbiol., Feb 1997, 567-573, Vol 63, No. 2
RS Fischer, J Song, W Gu and RA Jensen
L-Arogenate is a commonplace amino acid in nature in consideration of its
role as a ubiquitous precursor of L-phenylalanine and/or L-tyrosine.
However, the questions of whether it serves as a chemoattractant molecule
and whether it can serve as a substrate for catabolism have never been
studied. We found that Pseudomonas aeruginosa recognizes L-arogenate as a
chemoattractant molecule which can be utilized as a source of both carbon
and nitrogen. Mutants lacking expression of either cyclohexadienyl
dehydratase or phenylalanine hydroxylase exhibited highly reduced growth
rates when utilizing L-arogenate as a nitrogen source. Utilization of
L-arogenate as a source of either carbon or nitrogen was dependent upon
(sigma)(sup54), as revealed by the use of an rpoN null mutant. The evidence
suggests that catabolism of L-arogenate proceeds via alternative pathways
which converge at 4-hydroxyphenylpyruvate. In one pathway, prephenate
formed in the periplasm by deamination of L-arogenate is converted to
4-hydroxyphenylpyruvate by cyclohexadienyl dehydrogenase. The second route
depends upon the sequential action of periplasmic cyclohexadienyl
dehydratase, phenylalanine hydroxylase, and aromatic aminotransferase.
Copyright © 1997, American Society for Microbiology
L-Arogenate Is a Chemoattractant Which Can Be Utilized as the Sole Source of Carbon and Nitrogen by Pseudomonas aeruginosa
Department of Microbiology & Cell Science, University of Florida, Gainesville, Florida 32611-0700
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