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            -Succinylated intermediates in an arginine catabolic pathway of Pseudomonas aeruginosa

Jann, Alfred; Stalon, Victor; Wauven, Corinne Vander; Leisinger, Thomas; Haas, Dieter

doi:10.1073/pnas.83.13.4937

Cited by 36 publications

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“…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).…”

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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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“…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).…”

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Arginine racemization by coupled catabolic and anabolic dehydrogenases

Lu²

2009

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

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“…1) is the major route for arginine catabolism under aerobic conditions in Pseudomonas aeruginosa, This pathway converts Larginine into L-glutamate with the concomitant release of three nitrogen moieties (11,13,14). Utilization of arginine as a carbon source entails deamination of glutamate to ␣-ketoglutarate, which is then channeled into the tricarboxylic acid (TCA) cycle.…”

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The Arginine Regulatory Protein Mediates Repression by Arginine of the Operons Encoding Glutamate Synthase and Anabolic Glutamate Dehydrogenase in Pseudomonas aeruginosa

et al. 2004

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The arginine regulatory protein of Pseudomonas aeruginosa, ArgR, is essential for induction of operons that encode enzymes of the arginine succinyltransferase (AST) pathway, which is the primary route for arginine utilization by this organism under aerobic conditions. ArgR also induces the operon that encodes a catabolic NAD ؉ -dependent glutamate dehydrogenase (GDH), which converts L-glutamate, the product of the AST pathway, in ␣-ketoglutarate. The studies reported here show that ArgR also participates in the regulation of other enzymes of glutamate metabolism. Exogenous arginine repressed the specific activities of glutamate synthase (GltBD) and anabolic NADP-dependent GDH (GdhA) in cell extracts of strain PAO1, and this repression was abolished in an argR mutant. The promoter regions of the gltBD operon, which encodes GltBD, and the gdhA gene, which encodes GdhA, were identified by primer extension experiments. Measurements of ␤-galactosidase expression from gltB::lacZ and gdhA::lacZ translational fusions confirmed the role of ArgR in mediating arginine repression. Gel retardation assays demonstrated the binding of homogeneous ArgR to DNA fragments carrying the regulatory regions for the gltBD and gdhA genes. DNase I footprinting experiments showed that ArgR protects DNA sequences in the control regions for these genes that are homologous to the consensus sequence of the ArgR binding site. In silica analysis of genomic information for P. fluorescens, P. putida, and P. stutzeri suggests that the findings reported here regarding ArgR regulation of operons that encode enzymes of glutamate biosynthesis in P. aeruginosa likely apply to other pseudomonads.The arginine succinyltransferase (AST) pathway (Fig. 1) is the major route for arginine catabolism under aerobic conditions in Pseudomonas aeruginosa, This pathway converts Larginine into L-glutamate with the concomitant release of three nitrogen moieties (11,13,14). Utilization of arginine as a carbon source entails deamination of glutamate to ␣-ketoglutarate, which is then channeled into the tricarboxylic acid (TCA) cycle. We have recently reported (18) the cloning and characterization of gdhB, which encodes a novel NAD ϩ -dependent glutamate dehydrogenase (NAD-GDH; GdhB). The expression of gdhB was shown to be inducible by exogenous arginine, and this induction was mediated by ArgR, the arginine regulatory protein. The activity of GdhB, a tetramer of equal 180-kDa subunits, was also found to be subject to allosteric activation by arginine. The induction of gdhB expression and the activation by arginine of the encoded enzyme clearly serve as mechanisms that coordinate aerobic utilization of arginine as a carbon source with glutamate utilization via the TCA cycle.The ArgR protein of P. aeruginosa does not exhibit any sequence homology to the arginine regulatory proteins from enteric bacteria (17,19) or Bacillus subtilis (5). Rather, ArgR of P. aeruginosa is a member of the AraC/XylS family of transcriptional regulators (27) and functions like other members of th...

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“…1). Therefore, this pathway can serve as a common catabolic route for both arginine and ornithine utilization in P. aeruginosa (4, 8,17,34) (Fig. 1).…”

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“…SOAT, the aruC product of P. aeruginosa PAO1, transaminates both N 2 -succinylornithine and N 2 -acetylornithine with comparable catalytic parameters (17). Therefore, it has been postulated that this enzyme also participates in arginine anabolism as an N 2 -acetylornithine 5-aminotransferase (ACOAT) (4, 8,17,37). It is also known that 4-aminobutyrate aminotransferase, which is involved in the utilization of 4-aminobutyrate, a common intermediate in the arginine decarboxylase and arginine oxidase pathways (4, 8), has ACOAT and ornithine aminotransferase activities (38).…”

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Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa

Itoh

1997

J Bacteriol

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The arginine succinyltransferase (AST) pathway is the major arginine and ornithine utilization (aru) pathway under aerobic conditions in Pseudomonas aeruginosa. A 26-kb DNA fragment of the P. aeruginosa PAO1 chromosome carrying the regulatory argR gene and the aru structural gene cluster was cloned. Complementation tests and nucleotide sequence data established the locations of the argR, aruC, aruF, aruG, aruD, aruB, and aruE genes, in that order. The aruR, aruC, aruD, aruB, and aruE genes specify the ArgR regulatory protein, N 2 -succinylornithine 5-aminotransferase, N-succinylglutamate 5-semialdehyde dehydrogenase, N 2 -succinylarginine dihydrolase, and N-succinylglutamate desuccinylase, respectively, and the aruF and aruG genes encode the subunits (AruAI and AruAII) of arginine and ornithine N 2 -succinyltransferases. Furthermore, in vivo analysis of transcriptional aru fusions and of polar insertion mutations located at different sites in the aru cluster indicated the presence of three transcriptional units which are controlled by ArgR. The aruCFGDB genes appear to form an operon transcribed from a promoter upstream of aruC, whereas aruE has its own promoter. The argR gene, which is located upstream of the aruCFGDB operon, is a member of another (aot) operon coding for arginine transport genes. The deduced amino acid sequences of the AST enzymes were compared to those of homologous proteins of Escherichia coli specified by the ast genes lying in the chromosome region from 39.2 to 39.5 min (Kohara clone 327; GenBank/EMBL/DDJB accession no. D90818). The overall organization of the aru and ast genes in both organisms is similar, with the exception that E. coli appears to have a single AST gene.The arginine succinyltransferase (AST) pathway consists of five arginine catabolic enzymes: arginine succinyltransferase (AST; encoded by aruA), N 2 -succinylarginine dihydrolase (SADH; aruB), N 2 -succinylornithine 5-aminotransferase (SOAT; aruC), N-succinylglutamate 5-semialdehyde dehydrogenase (SGSD; aruD), and N-succinylglutamate desuccinylase (SGDS; aruE) (for a review, see references 4 and 8; Fig. 1). The AST pathway was first established in Pseudomonas spp. and also occurs in Aeromonas formicans, Klebsiella aerogenes, Salmonella typhimurium, and Escherichia coli (17,27,34,35). The pathway is initiated with the succinyl-coenzyme Adependent succinylation of L-arginine and converts arginine to L-glutamate and succinate, with the concomitant liberation of ammonia and carbon dioxide (Fig. 1). In Pseudomonas aeruginosa, arginine and ornithine N 2 -succinyltransferase (AOST; aruF and aruG) catalyzes the succinylation of both L-arginine and L-ornithine (33). Ornithine succinyltransferase activity of AOST results in the formation of N 2 -succinylornithine (33, 34), which is an intermediate of the AST pathway (Fig. 1). Therefore, this pathway can serve as a common catabolic route for both arginine and ornithine utilization in P. aeruginosa (4, 8,17,34) (Fig. 1). The aru genes of P. aeruginosa are clustered in a locus origina...

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N ² -Succinylated intermediates in an arginine catabolic pathway of Pseudomonas aeruginosa

Cited by 36 publications

References 20 publications

Arginine racemization by coupled catabolic and anabolic dehydrogenases

Arginine racemization by coupled catabolic and anabolic dehydrogenases

The Arginine Regulatory Protein Mediates Repression by Arginine of the Operons Encoding Glutamate Synthase and Anabolic Glutamate Dehydrogenase in Pseudomonas aeruginosa

Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa

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N 2 -Succinylated intermediates in an arginine catabolic pathway of Pseudomonas aeruginosa

Cited by 36 publications

References 20 publications

Arginine racemization by coupled catabolic and anabolic dehydrogenases

Arginine racemization by coupled catabolic and anabolic dehydrogenases

The Arginine Regulatory Protein Mediates Repression by Arginine of the Operons Encoding Glutamate Synthase and Anabolic Glutamate Dehydrogenase in Pseudomonas aeruginosa

Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa

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N ² -Succinylated intermediates in an arginine catabolic pathway of Pseudomonas aeruginosa