1977
DOI: 10.1099/00221287-99-1-139
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Catabolism of L-Lysine by Pseudomonas aeruginosa

Abstract: SUMMARYPseudomonas aeruginosa PACI grows poorly on L-lysine as sole source of carbon but mutant derivatives which grow rapidly were readily isolated. Studies with one such mutant, P. aeruginosa ~~~5 8 6 , supported the existence of a route for L-lysine catabolism which differs from those reported previously in other species of Pseudomonas. The postulated route, the cadaverine or decarboxylase pathway, is initiated by the decarboxylation of L-lysine and involves the following steps: L-lysine -+ cadaverine -+ I … Show more

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Cited by 123 publications
(107 citation statements)
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“…This compound is probably converted to a-aminoadipate, 2-oxoadipate and glutarate via a pathway similar to that of Pseudornonus aeruginosa (Fothergill & Guest, 1977). The high derepression of the L-lysine edehydrogenase activity from yeast cells grown in lysine-containing medium indicates that the enzyme plays an important role in the catabolism of lysine in C. albicans.…”
Section: Discussionmentioning
confidence: 99%
“…This compound is probably converted to a-aminoadipate, 2-oxoadipate and glutarate via a pathway similar to that of Pseudornonus aeruginosa (Fothergill & Guest, 1977). The high derepression of the L-lysine edehydrogenase activity from yeast cells grown in lysine-containing medium indicates that the enzyme plays an important role in the catabolism of lysine in C. albicans.…”
Section: Discussionmentioning
confidence: 99%
“…Nutrient yeast broth (NYB) and nutrient agar were those of Stanisich & Holloway (1972). The minimal salts medium contained (1-l, pH 7.2): KzHP04, 12.5 g; KH2P04, 3.8 g; (NH4)$0,, 1.0 g; 5 ml of a trace elements solution (Fothergill & Guest, 1977). The carbon source, generally potassium lactate, was added as a sterile solution to the sterilized basal medium at a final concentration of 20 mM unless stated otherwise.…”
Section: Methodsmentioning
confidence: 99%
“…Both monooxygenase and decarboxylase pathways converge at 5-aminovalerate, which is then converted to glutarate by a pair of transaminase and semialdehyde dehydrogenase encoded by the gabDT operon (Chou et al, 2013;Revelles et al, 2004). Glutarate is proposed to produce acetyl-CoA that can enter the Krebs cycle (Numa et al, 1964), and glutaryl-CoA dehydrogenase enzyme (an enzyme in glutarate catabolism) activity has been reported in crude extracts of P. aeruginosa (Fothergill & Guest, 1977). However, none of the genes for glutarate catabolism and its regulation have been characterized in Pseudomonas.…”
Section: Introductionmentioning
confidence: 99%
“…P. aeruginosa does not possess the lysine racemase; however, L-Lys catabolism can potentially be connected to the D-Lys pathway via an arginine-pyruvate transaminase AruH (Chou et al, 2010;Yang & Lu, 2007a). One early report suggested the presence of another route through L-lysine 6-amino transferase to make L-pipecolate, which again could possibly convert into glutarate (Fothergill & Guest, 1977). In P. aeruginosa, the alpha amino group of D-Lys can be deaminated by the FAD-dependent D-amino acid dehydrogenase DauA (Li & Lu, 2009a).…”
Section: Introductionmentioning
confidence: 99%