Publications

• Biosynthesis and metabolism of arginine in bacteria.

  Cunin R., Glansdorff N., Pierard A., Stalon V.

  Microbiol Rev 50:314-352(1986) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria.

  Stalon V., Vander Wauven C., Momin P., Legrain C.

  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 accumula ... >> More

  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. << Less

  J Gen Microbiol 133:2487-2495(1987) [PubMed] [EuropePMC]

• Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia.

  Vander Wauven C., Stalon V.

  Pseudomonas cepacia NCTC 10743 utilizes arginine as the sole source of carbon and nitrogen for growth. Arginine is degraded to glutamate via succinyl derivatives. The catabolic sequence in this pathway is L-arginine----N2-succinylarginine----N2-succinylornithine----N2-succinylglutamate semialdehyd ... >> More

  Pseudomonas cepacia NCTC 10743 utilizes arginine as the sole source of carbon and nitrogen for growth. Arginine is degraded to glutamate via succinyl derivatives. The catabolic sequence in this pathway is L-arginine----N2-succinylarginine----N2-succinylornithine----N2-succinylglutamate semialdehyde----N2-succinylglutamate----glutamate + succinate. The formation of the enzymes responsible for arginine degradation is regulated not only by induction but also by both carbon and nitrogen catabolite repression. << Less

  J Bacteriol 164:882-886(1985) [PubMed] [EuropePMC]

  This publication is cited by 3 other entries.

• Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.

  Schneider B.L., Kiupakis A.K., Reitzer L.J.

  Arginine catabolism produces ammonia without transferring nitrogen to another compound, yet the only known pathway of arginine catabolism in Escherichia coli (through arginine decarboxylase) does not produce ammonia. Our aims were to find the ammonia-producing pathway of arginine catabolism in E. ... >> More

  Arginine catabolism produces ammonia without transferring nitrogen to another compound, yet the only known pathway of arginine catabolism in Escherichia coli (through arginine decarboxylase) does not produce ammonia. Our aims were to find the ammonia-producing pathway of arginine catabolism in E. coli and to examine its function. We showed that the only previously described pathway of arginine catabolism, which does not produce ammonia, accounted for only 3% of the arginine consumed. A search for another arginine catabolic pathway led to discovery of the ammonia-producing arginine succinyltransferase (AST) pathway in E. coli. Nitrogen limitation induced this pathway in both E. coli and Klebsiella aerogenes, but the mechanisms of activation clearly differed in these two organisms. We identified the E. coli gene for succinylornithine aminotransferase, the third enzyme of the AST pathway, which appears to be the first of an astCADBE operon. Its disruption prevented arginine catabolism, impaired ornithine utilization, and affected the synthesis of all the enzymes of the AST pathway. Disruption of astB eliminated succinylarginine dihydrolase activity and prevented arginine utilization but did not impair ornithine catabolism. Overproduction of AST enzymes resulted in faster growth with arginine and aspartate. We conclude that the AST pathway is necessary for aerobic arginine catabolism in E. coli and that at least one enzyme of this pathway contributes to ornithine catabolism. << Less

  J. Bacteriol. 180:4278-4286(1998) [PubMed] [EuropePMC]

  This publication is cited by 4 other entries.

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

  Itoh Y.

  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 clone ... >> More

  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, N2-succinylornithine 5-aminotransferase, N-succinylglutamate 5-semialdehyde dehydrogenase, N2-succinylarginine dihydrolase, and N-succinylglutamate desuccinylase, respectively, and the aruF and aruG genes encode the subunits (AruAI and AruAII) of arginine and ornithine N2-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. << Less

  J. Bacteriol. 179:7280-7290(1997) [PubMed] [EuropePMC]

  This publication is cited by 5 other entries.