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Alterations in protein folding and the regulation of conformational states have become increasingly important to the functionality of key molecules in signaling, cell growth, and cell death. Molecular chaperones, because of their properties in protein quality control, afford conformational flexibility to proteins and serve to integrate stress-signaling(More)
It is generally accepted that ancient organisms must have possessed small genomes producing fewer gene products than contemporary organisms. Since the evolution of high specificity is surely a demanding process, primitive enzymes are likely to have been broad-specificity catalysts, utilizing a family of related substrates and producing a family of related(More)
The phhC gene of Pseudomonas aeruginosa encodes a protein which is a member of the Family I aminotransferases. At high expression levels in the heterologous Escherichia coli system, PhhC can compensate for the absence of AspC (which functions in L-aspartate biosynthesis) and TyrB (which functions in aromatic biosynthesis). In the native organism, PhhC is(More)
hisH encodes imidazole acetol phosphate (IAP) aminotransferase in Zymomonas mobilis and is located immediately upstream of tyrC, a gene which codes for cyclohexadienyl dehydrogenase. A plasmid containing hisH was able to complement an Escherichia coli histidine auxotroph which lacked the homologous aminotransferase. DNA sequencing of hisH revealed an open(More)
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(More)
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