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Catabolism of Arginine, Citrulline and Ornithine by Pseudomonas and Related Bacteria

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Catabolism of Arginine, Citrulline and Ornithine by Pseudomonas and Related Bacteria Journal of General Microbiology (1987), 133, 2487-2495. Printed in Great Britain 2487 Catabolism of Arginine, Citrulline and Ornithine by Pseudomonas and Related Bacteria By VICTOR STALON,l* CORINNE VANDER WAUVEN,2 PATRICIA MOMIN' AND CHRISTIANE LEGRAIN2 Laboratoire de Microbiologie, Universitk Libre de Bruxelles and Institut de Recherches du CERIA, I, avenue E. Gryson, B-1070 Brussels, Belgium (Received 5 January 1987; revised 13 April 1987) ~~ ~~ ~ ~ ~~ ~ The distribution of the arginine succinyltransferase pathway was examined in representative strains of Pseudomonas and related bacteria able to use arginine as the sole carbon and nitrogen source for growth. The arginine succinyltransferase pathway was induced in arginine-grown cells. The accumulation of succinylornithine following in vivo inhibition of succinylornithine transaminase activity by aminooxyacetic acid showed that this pathway is responsible for the dissimilation of the carbon skeleton of arginine. Catabolism of citrulline as a carbon source was restricted to relatively few of the organisms tested. In P. putida, P. cepacia and P. indigofera, ornithine was the main product of citrulline degradation. In most strains which possessed the arginine succinyltransferase pathway, the first step of ornithine utilization as a carbon source was the conversion of ornithine into succinylornithine through an ornithine succinyltransferase. However P. cepacia and P.putida used ornithine by a pathway which proceeded via proline as an intermediate and involved an ornithine cyclase activity. INTRODUCTION Bacterial species utilize arginine through various pathways (for a review see Cunin et al., 19863). The guanidino group of arginine is subject to either hydrolytic cleavage by arginase to form ornithine and urea or to deamination, producing citrulline and ammonia. Agmatine is formed through the action of arginine decarboxylase while the transamination or oxidation of the a-nitrogen atom of arginine results in synthesis of 2-oxoarginine. Succinylation of the amino group by succinyl CoA also initiates arginine catabolism in Pseudomonas cepacia (Vander Wauven & Stalon, 1985) and Pseudomonas aeruginosa (Jann et al., 1986) (Fig. 1). Multiple pathways may occur in the same organism. Pseudomonas putida has four arginine catabolic pathways while P. aeruginosa has at least three (Haaset al., 1984; Stalon, 1985; Jann etal., 1986). Ornithine, a biosynthetic precursor of arginine, is also susceptible to different modes of enzymic utilization. Transamination of ornithine to produce pyrroline-karboxylate has been reported in Bacillus species (De Hauwer et al., 1964; Baumberg & Harwood, 1979) as well as in Pseudomonas (Voellmy & Leisinger, 1975; Rahman et al., 1980) and Klebsiella (Friedrich et al., 1978). The decarboxylation of ornithine to produce putrescine, a polyamine precursor, is common in micro-organisms (see Tabor & Tabor, 1985; Cunin et al., 19863). Deamination of ornithine to proline by an ornithine cyclase occurs in Agrobacterium (Dessaux et al., 1986), Clostridium sticklandii (Costilow & Laycock, 1969) and Treponema denticola (Leschine & Canale- Parola, 1980). Little is known about citrulline utilization by bacteria; few species are able to use this substrate. as a carbon source (Stalon & Mercenier, 1984). Argininosuccinate synthetase and argininosuccinase, the enzymes catalysing the final step of arginine biosynthesis, seem to be involved in the utilization of citrulline by Bacillus species (Baumberg & Harwood, 1979). In the Pseudomonas strains of the fluorescent group which are able to use citrulline as a carbon source, 0001-3918 0 1987 SGM 2488 V. STALON AND OTHERS 4 / Putrescine a~u;~~CoA N'-Succinylarginine 0 OfH, v NADH ?H+ H J) Pyrroline-5-carboxylate N'-Succinylglutamate 0 .$'L+ H' Glutamate Succinate Carbon and nitrogen source Carbon source Fig. 1. Pathway of arginine, ornithine and citrulline utilization. Numbers designate enzymes : 1, arginine succinyltransferase (EC 2.3.1.-); 2, succinylarginine dihydrolase (EC 3.5.3.-); 3, succinylornithine transaminase (EC 2.6.1. -); 4, succinylglutamate semialdehyde dehydrogenase (EC 1.2.1.-); 5, succinylglutamate desuccinylase (EC 3.5.1.-); 6, ornithine succinyltransferase (EC 2.3.1.-); 7, ornithine transaminase (EC 2.6.1.13); 8, pyrroline-5-carboxylate dehydrogenase (EC 1 .5.1.12); 9, arginine deiminase (EC 3.5.3.6); 10, catabolic ornithine carbamoyltransferase (EC 2.1.3.3); 1 1, ornithine cyclase (EC 4.1 .3.12); 12, proline dehydrogenase (EC 1 .5.99.8); 13, ornithine decarboxylase (EC 4.1.1.17); 14, anabolic ornithine carbamoyltransferase (EC 2.1.3.3). the catabolic ornithine carbamoyltransferase belonging to the arginine deiminase route was thought to participate in citrulline utilization (Ramos et af., 1967). The aim of the present study was to elucidate the relationships existing between ornithine, citrulline and arginine utilization pathways in Pseudomonas and related bacteria. METHODS Bacterial strains, media and growth. The strains and their origins are listed in Table 1. In addition Agrobacterium tumefaciens RlO, Bacillus lichen$ormis ATCC 14580 and Saccharomyces cerevisiae C 1278b were used as reference strains. They were routinely grown at 30 or 37 "C according to their optimum growth temperature. Nitrogen-free minimal medium 154 was used (Stalon et al., 1967). Substrates used as carbon and/or nitrogen source were added after separate sterilization by filtration. Unless otherwise stated the final concentration of metabolites was 20 mM when used as carbon source and 10 mM when utilized as nitrogen source. Strains were tested for the ability to grow at the expense of acyl derivatives. The tests were done in liquid media, where the yield could be determined quantitatively and where substrate consumption could be measured. To prepare inocula for substrate utilization studies, 3 ml of complex medium 853 (Cunin et al., 1986~)was inoculated from a slant and was incubated overnight. Cells were washed twice with NaCl (0.9%, w/v) and then used to inoculate 10 ml of standard salt medium 154 at lo7 cells ml-' . Bacterial growth was followed by measuring optical Arginine, citrulline and ornithine catabolism 2489 density at 660 nm with a Beckman photometer. For enzyme activity determinations, cultures were grown aerobically as 100 ml batches in 1 1 flasks on a rotary shaker. Cells were harvested in the middle of the exponential phase, washed twice with NaCl (0.9%) and stored at - 20 "C. Action ofaminooxyacetic acid. Cultures (10 ml) in the exponential phase of growth on 20 mM-amino acid were washed twice with 0.9% NaCl and resuspended in 2.0 ml50 mM-potassium phosphate buffer, pH 7.5, containing 10 mM each of succinate, amino acid and aminooxyacetic acid. After overnight incubation at the appropriate growth temperature with agitation, the centrifugation supernatant was analysed for excretion products using high voltage paper electrophoresis or amino acid analysis (Vander Wauven & Stalon, 1985). Enzyme assaj's. Cells were broken by sonication as described by Stalon & Mercenier (1984). All enzymes were assayed at 37 "C. Arginine deiminase (EC 3.5.3.6) and catabolic ornithine carbamoyltransferase (EC 2.1.3.3) were determined as described by Mercenier et al. (1980); arginine succinyltransferase (EC 2.3.1 . -), arginine succinylhydrolase (EC 3.5.3.-) and succinylglutamate desuccinylase (EC 3.5.1 . -) were determined according to Vander Wauven & Stalon (1985). Unless otherwise stated succinylornithine transaminase (EC 2.6.1 . -) and ornithine transaminase (EC 2.6.1 .13) were determined according to Vander Wauven & Stalon (1985) either by using 100 mM-Tris/HCl buffer, pH 8.5, or 100 mM-glycine/NaOH buffer, pH 9.0. Ornithine succinyltransferase (EC 2.3.1 .-) activity was assayed as for arginine succinyltransferase but substituting 100 mM-ornithine for arginine. Ornithine cyclase (EC 4.3.1 .12) was estimated by following the production of either proline or ammonium (Dessaux et al., 1986). Protein was determined by the Lowry method. Specific activity is defined as the amount of enzyme catalysing the formation of 1 pmol product h-' (mg protein)-'. Analytical methods. Arginine and acylarginine derivatives in culture media were determined by the method of Micklus &Stein (1973); citrulline and urea were determined by the method of Archibald (1944). Succinylornithine was identified by high voltage paper electrophoresis or amino acid analysis as described by Vander Wauven & Stalon (1985). Chemicals. Amino acids, putrescine, aminooxyacetic acid, guanidinobutyrate and succinate semialdehyde were obtained from Sigma. Succinylarginine, succinylcitrulline, succinylornithine and succinylglutamate were prepared as described by Vander Wauven & Stalon (1985). RESULTS AND DISCUSSION Catabolism of arginine Previous studies of arginine catabolism in P. cepacia (Vander Wauven & Stalon, 1985) and P. aeruginosa (Jann et al., 1986) suggested that the arginine succinyltransferase pathway may be responsible for the dissimilation of the arginine carbon skeleton in Pseudomonadaceae and related bacteria able to use this amino acid as sole carbon and nitrogen source. The strains listed in Table 1 were selected for their ability to use arginine as sole carbon source (Stalon & Mercenier, 1984). The doubling time of the various strains on arginine or related metabolites used either as carbon or nitrogen source are shown in Table 1. The presence of the pathway in a strain was established by comparing products excreted by arginine-grown cells incubated in the , presence
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