The Catabolism of Arginine by Pseudomonas aeruginosa

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Abstract
Mutants isolated from P. aeruginosa strain PAO1632 (Hut-Ami-) were unable to utilize L-arginine or L-ornithine as the C source for growth. Arginine deaminase (AD), catabolic ornithine carbamoyltransferase (cOTC) and N2-acetylornithine 5-aminotransferase (ACOAT) were present in the mutants but these enzymes were not induced to higher levels by exogenous L-arginine. One group of mutants could utilize L-ornithine but not L-arginine and in these strains L-arginine induced the synthesis of ACOAT but not AD or cOTC. The mutations of the arginine utilization-negative mutants were all in genes of the same transductional linkage group and mapped in the 45-50 min region of the chromosome. Revertants isolated on L-arginine or L-ornithine plates were derepressed for the synthesis of ACOAT. It is suggested that L-arginine is normally catabolized by the wild-type strain via the arginine deaminase pathway and requires a threshold level of ACOAT. The regulatory factors controlling the functioning of the divergent arginine deaminase and arginine carboxylase pathways was discussed.

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