Arginine degradation in Pseudomonas aeruginosa mutants blocked in two arginine catabolic pathways

Haas, Dieter; Matsui, Hideki; Moretti, Paola; Stalon, Victor; Mercenier, Annick

doi:10.1007/bf00382081

Cited by 43 publications

(45 citation statements)

References 41 publications

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“…Assay of D-arginine dehydrogenase P. aeruginosa P A 0 grew on D-arginine as the only carbon and nitrogen source, albeit more slowly (doubling time about 2 h) than on L-arginine (doubling time 1.3 h; Haas et al, 1984). Cells grown on D-arginine contained D-arginine dehydrogenase activity ( Table 2).…”

Section: Resultsmentioning

confidence: 99%

The Fourth Arginine Catabolic Pathway of Pseudomonas aeruginosa

Jann¹,

Matsumoto²,

Haas³

1988

Microbiology

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D-Arginine dehydrogenase activity was discovered in Pseudomonas aeruginosa. This enzyme was inducible by its substrate, D-arginine, as well as by its product, 2-ketoarginine, but not by L-arginine. The enzyme activity was measured in uitro, in the presence of artificial electron acceptors (phenazine methosulphate and iodonitrotetrazolium chloride). 2-Ketoarginine was catabolized further to 4-guanidinobutyraldehyde, 4-guanidinobutyrate and 4-aminobutyrate. Two enzymes involved, 4-guanidinobutyraldehyde dehydrogenase and guanidinobutyrase, were inducible by 2-ketoarginine ; the latter enzyme was also strongly induced by 4-guanidinobutyrate. An arginine racemase activity was detected by an in vivo test. D-Arginine had the potential to be catabolized via the D-arginine dehydrogenase pathway and, after racemization, via the three L-arginine catabolic pathways previously demonstrated in P. aeruginosa. In mutants blocked in the L-arginine succinyltransferase pathway, but not in the wild-type, L-arginine was channelled partially into the D-arginine dehydrogenase pathway. Mutations in the kauB locus abolished growth of P. aeruginosa on 2-ketoarginine, agmatine and putrescine, and led to loss of 4-guanidino bu t yralde h yde de h ydrogenase and 4-amino bu tyralde hyde de hydrogenase activities.Thus, these two activities appear to be due to one enzyme in P. aeruginosa. The kauB locus was mapped on the chromosome between 1ysA and argB and was not linked to known genes involved in the three L-arginine catabolic pathways. The existence of four arginine catabolic pathways illustrates the metabolic versatility of P. aeruginosa. I N T R O D U C T I O NThree arginine catabolic pathways are known in Pseudomonas aeruginosa P A 0 (Fig. 1). (I) The arginine deiminase pathway converts L-arginine to L-ornithine, with the formation of ATP. The enzymes of this pathway are inducible by energy depletion and by the presence of L-arginine. Mutants which are defective in one of the three enzymes involved (arcA, B, C mutants) cannot grow anaerobically with L-arginine as the energy source (Mercenier et al., 19806,1982;Vander Wauven et al., 1984). (11) The arginine succinyltransferase pathway is used for aerobic L-arginine degradation. The products are L-glutamate and succinate, and L-arginine induces all enzymes of this route. Mutants blocked in the arginine succinyltransferase pathway (aru mutants) grow very poorly if at all on L-arginine as the only carbon and nitrogen source (Jann et al., 1986). (111) The arginine decarboxylase pathway produces putrescine, which can be converted to spermidine, and permits good growth on agmatine and putrescine. The first enzyme, L-arginine decarboxylase (enzyme 12 in Fig. l), is induced by L-arginine. The synthesis of agmatine deiminase and N-carbamoylputrescine hydrolase (enzymes 13 and 14 in Fig. 1) is switched on by agmatine. Putrescine is further catabolized to succinate and ammonia (Jakoby & Fredericks, 1959;Voellmy & Leisinger, 1976; Mercenier et al., 1980a

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Section: Resultsmentioning

confidence: 99%

The Fourth Arginine Catabolic Pathway of Pseudomonas aeruginosa

Jann¹,

Matsumoto²,

Haas³

1988

Microbiology

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“…In most cases, D-amino acid oxidase or dehydrogenase catalyzes the oxidative deamination as the first step in catabolism. Pseudomonas aeruginosa, an opportunistic human pathogen with an enormous catabolic capacity, is capable of growing on D-arginine as the sole source of carbon and nitrogen (5). The presence of an inducible D-arginine dehydrogenase activity in this organism was initially reported by Haas and coworkers (6), and 2-ketoarginine derived from this reaction could be converged into the arginine transaminase (ATA) pathway (7,8), 1 of the 4 pathways for L-arginine catabolism in pseudomonads (Fig.…”

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confidence: 97%

Arginine racemization by coupled catabolic and anabolic dehydrogenases

Lu²

2009

Proc. Natl. Acad. Sci. U.S.A.

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amino acid ͉ arginine dehydrogenase ͉ racemase A lthough L-amino acids are the predominant amino acids in protein synthesis, D-amino acids serve as specialized components of many types of machineries in living organisms. In mammals, D-serine and D-aspartate are associated with cell aging and neural signaling (1, 2). In bacteria, some D-amino acids are essential ingredients of cell wall synthesis (3). Endogenous D-amino acids are produced by racemization from the prevalent L-amino acids through the action of racemases. Amino acid racemases are classified into 2 groups: pyridoxal 5Ј phosphate-dependent and phosphate-independent enzymes (4). Completely different reaction mechanisms have been proposed for these 2 groups of enzymes for the spatial rearrangement of ␣-hydrogen in the corresponding amino acids. Nevertheless, racemization of amino acids reported so far is catalyzed by a single enzyme.When provided in excess, some D-amino acids can be used as nutrients to support growth by bacteria. In most cases, D-amino acid oxidase or dehydrogenase catalyzes the oxidative deamination as the first step in catabolism. Pseudomonas aeruginosa, an opportunistic human pathogen with an enormous catabolic capacity, is capable of growing on D-arginine as the sole source of carbon and nitrogen (5). The presence of an inducible D-arginine dehydrogenase activity in this organism was initially reported by Haas and coworkers (6), and 2-ketoarginine derived from this reaction could be converged into the arginine transaminase (ATA) pathway (7,8), 1 of the 4 pathways for L-arginine catabolism in pseudomonads (Fig. 1). In fact, it has been proposed that L-arginine might be converted into D-arginine via racemization (6), reminiscent of L-alanine utilization through a catabolic alanine racemase and D-alanine dehydrogenase in Escherichia coli and many bacteria (9, 10). Existence of an arginine racemase in P. aeruginosa was supported by growth complementation of arginine auxotrophs with D-arginine (6). However, the activity of P. aeruginosa arginine racemase has never been demonstrated in vitro, presumably because of the instant decomposition of both L-and D-arginine in extracts.Under aerobic conditions, L-arginine is preferentially catabolized by the arginine succinyltransferase (AST) pathway, followed by the ATA pathway (7,11). Enzymes of the AST pathway are encoded by the aruCFGDBE operon (12), which is induced by exogenous L-arginine in the presence of a functional arginine regulator, ArgR (13). The ArgR protein belongs to the AraC family of transcriptional regulators. Depending on the location of its binding sites, ArgR serves as a repressor or activator of ArgR regulon in arginine and glutamate metabolism. Thus, when the AST pathway is absent or remains uninduced (e.g., in the argR mutant), the ATA pathway then takes charge as the auxiliary route of L-arginine utilization.

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“…Formation of putrescine from agmatine via N-carbamoylputrescine has also been reported in Streptococcus faecalis (Roon & Barker, 1972) and in Pseudomonas aeruginosa (Haas et al, 1984).…”

Section: Introductionmentioning

confidence: 63%

A probable new pathway for the biosynthesis of putrescine in Escherichia coli

Cataldi¹,

Algranati²

1986

Biochemical Journal

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Some cultures of Escherichia coli BGA8, a mutant unable to synthesize putrescine, showed a change of behaviour and could grow almost equally well in either the absence or the presence of polyamines after repeated periods of polyamine starvation. Experiments in vivo with radioactive precursors showed that the bacteria which evaded the polyamine requirement had recovered their ability to synthesize putrescine from glucose or glutamic acid, but not from ornithine or arginine. These results are in agreement with the fact that the polyamine-independent cells were still deficient in the enzymes ornithine decarboxylase and agmatinase. Our findings seem to indicate the existence of a new pathway to synthesize putrescine which does not involve ornithine or arginine as intermediates.

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Arginine degradation in Pseudomonas aeruginosa mutants blocked in two arginine catabolic pathways

Cited by 43 publications

References 41 publications

The Fourth Arginine Catabolic Pathway of Pseudomonas aeruginosa

The Fourth Arginine Catabolic Pathway of Pseudomonas aeruginosa

Arginine racemization by coupled catabolic and anabolic dehydrogenases

A probable new pathway for the biosynthesis of putrescine in Escherichia coli

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