Quinate metabolism in Pseudomonas aeruginosa

Abstract

Data obtained with the Warburg constant-volume respirometer and from enzyme analysis have demonstrated that the method of regulation of the "hydroaromatic" degradation pathway found in Pseudomonas aeruginosa is vastly different from that previously discovered in Acinetobacter calcoaceticus and perhaps also significantly different from P. putida. Two mutants have been analyzed: the first with multiple impairment of degradative abilities; the second with a single defect, i.e. a lack of quinic dehydrogenase activity. Quinic dehydrogenase has also been shown to function for shikimate utilization in P. aeruginosa, even though 5-dehydroshikimate reductase in vitro catalyzes the same reaction. The possible relationship of these findings to pyocyanine formation is discussed.