SUMMARY: Pseudomonas aeruginosapaci 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. aeruginosapac586, 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-piperideine → 5-aminovalerate → glutarate semialdehyde → glutarate. Evidence for this pathway is based on the characterization of the pathway reactions and the induction of the corresponding enzymes by growth on l-lysine. The first three enzymes were also induced by growth on cadaverine and to a lesser extent by 5-aminovalerate. No evidence was obtained for the presence of pathways involving l-lysine 2-monooxygenase or l-pipecolate dehydrogenase, but another potential route for l-lysine catabolism initiated by l-lysine 6-aminotrans-ferase was detected. Studies with mutants unable to grow on l-lysine supported the existence of more than one catabolic pathway for l-lysine in this organism and indicated that all routes converge on a pathway for glutarate catabolism which generates acetyl-CoA. Pipecolate catabolism also appeared to converge on the glutarate pathway in P. aeruginosa. The results suggested that the growth rate of the parental strain is limited by the rate of transport and/or decarboxylation of l-lysine. The cadaverine pathway was present, but not so highly induced, in the parental strain P. aeruginosapaci. Pseudomonas fluorescens contained enzymes of both the cadaverine (decarboxylase) and oxygenase pathways, strains of P. putida (biotypes a and b) contained enzymes of the oxygenase pathway but not the decarboxylase pathway and P. multivorans appeared deficient in both. All these species possessed l-lysine aminotransferase activity.
BaginskyM.L., RodwellV.W.1966; Metabolism of pipecolic acid in a Pseudomonas species. IV. Electron transport particle of Pseudomonas putida.. Journal of Bacteriology 92:424–432
CalvertA.F., RodwellV.W.1966; Metabolism of pipecolic acid in a Pseudomonas species. III. l-α-Amino adipate-δ-semialdehyde :NADoxidoreductase.. Journal of Biological Chemistry 241:409–414
HartlineR.A., RodwellV.W.1971; Metabolism of pipecolic acid in a Pseudomonas species. VI. Precursors of glutamic acid.. Archives of Biochemistry and Biophysics 142:32–39
HolmstedtB., LarssonL., ThamB.1961; Further studies of a spectrophotometric method for the determination of diamine oxidase activity.. Biochimica et biophysica acta 48:182–186
KennedyI.R., DilworthM.J.1963; Activation of isocitratelyase and triosephosphate dehydrogenase in Azotobacter vinelandii extracts.. Biochimica et biophysica acta 67:226–239
MillerD.L., RodwellV.W.1971a; Metabolism of basic amino acids in Pseudomonas putida.Catabolism of lysine by cyclic and acyclic intermediates.. Journal of Biological Chemistry 246:2758–2764
MillerD.L., RodwellV.W.1971b; Metabolism of basic amino acids in Pseudomonas putida: intermediates in l-arginine catabolism.. Journal of Biological Chemistry 246:5053–5058
NumaS., IshimuraY., NakazawaD., OkazakiT., HayaishiO.1964; Enzymic studies on the metabolism of glutarate in Pseudomonas.. Journal of Biological Chemistry 239:3915–3926
SamuelsS.B., MossC.W., WeaverR.E.1973; The fatty acids of Pseudomonas multivorans (Pseudomonas cepacia) and Pseudomonas kingii.. Journal of General Microbiology 74:275–279
SodaK., MisonoH., YamamotoT.1968; l-Lysine-α-ketoglutarate aminotransferase. I. Identification of a product, Δ′-piperideine-6-carboxylic acid.. Biochemistry 7:4102–4109
TakedaH., YamamotoS., KojimaY., HayaishiO.1969; Studies on monooxygenases.I. General properties of crystalline l-lysine monooxygenase.. Journal of Biological Chemistry 244:2935–2941
VandecasteeleJ-P., HermannM.1972; Regulation of a catabolic pathway: lysine degradation in Pseudomonas putida.. European Journal of Biochemistry 31:80–85
WyngaardenJ.B., AshtonD.M.1959; The regulation of activity of phosphoribosylpyrophosphateamidotransferase by purine ribonucleotides: a potential feedback control of purine biosynthesis.. Journal of Biological Chemistry 234:1492–1496
ZolgW., OttowJ.C.G.1974; Thin-layer chromatography of arginine, lysine and ornithine decarboxylase activity among Pseudomonas spp. and Enterobacteriaceae.. Microbios 10:225–231