Arginine Catabolism and the Arginine Succinyltransferase Pathway in
            <i>Escherichia coli</i>

Schneider, Barbara L.; Kiupakis, Alexandros K.; Reitzer, Larry

doi:10.1128/jb.180.16.4278-4286.1998

Cited by 132 publications

(73 citation statements)

References 36 publications

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“…Arginine repressed argD about 10-fold, and nitrogen limitation activated expression of astC expression. These results confirm previously reported results (Glansdorff, 1996;Schneider et al, 1998;Kiupakis and Reitzer, 2002), and show that the fusions were responding appropriately. Finally, growth in LB repressed argD and serC, but activated astC.…”

Section: Expression Of the Major Sdap-at Isozymessupporting

confidence: 93%

“…A possible candidate for the alternate ACOAT is AstC. AstC is an enzyme of arginine catabolism that has 60% amino acid identity with ArgD (Schneider et al, 1998). A phylogenetic tree of all aminotransferases in E. coli shows that AstC is most closely related to ArgD (Fig.…”

Section: Genetics Of N-acetylornithine Synthesis: Four Acoat Isozymesmentioning

confidence: 99%

“…The major E. coli enzymes with either SDAP-AT or ACOAT activity are promiscuous. ArgD and AstC synthesize SDAP and N-acetylornithine, and degrade N-succinylornithine (this article) (Schneider et al, 1998;Ledwidge and Blanchard, 1999). GabT and PuuE degrade γ-aminobutyrate and can synthesize Nacetylornithine (this article) .…”

Section: The Broad Specificity Of Aminotransferasesmentioning

confidence: 99%

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The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli

Lal

Schneider

et al. 2014

Molecular Microbiology

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SummaryAminotransferases can be redundant or promiscuous, but the extent and significance of these properties is not known in any organism, even in Escherichia coli. To determine the extent of redundancy, it was first necessary to identify the redundant aminotransferases in arginine and lysine synthesis, and then complement all aminotransferase-deficient mutants with genes for all aminotransferases. The enzymes with N-acetylornithine aminotransferase (ACOAT) activity in arginine synthesis were ArgD, AstC, GabT and PuuE; the major anaerobic ACOAT was ArgD. The major enzymes with N-succinyl-L,L-diaminopimelate aminotransferase (SDAP-AT) activity in lysine synthesis were ArgD, AstC, and SerC. Seven other aminotransferases, when overproduced, complemented the defect in a triple mutant. Lysine availability did not regulate synthesis of the major SDAP-ATs. Complementation analysis of mutants lacking aminotransferases showed that the SDAP-ATs and alanine aminotransferases were exceptionally redundant, and it is proposed that this redundancy may ensure peptidoglycan synthesis. An overview of all aminotransferase reactions indicates that redundancy and broad specificity are common properties of aminotransferases.

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Section: Expression Of the Major Sdap-at Isozymessupporting

confidence: 93%

Section: Genetics Of N-acetylornithine Synthesis: Four Acoat Isozymesmentioning

confidence: 99%

Section: The Broad Specificity Of Aminotransferasesmentioning

confidence: 99%

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The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli

Lal

Schneider

et al. 2014

Molecular Microbiology

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“…The 'ast' gene locus has not been identified or characterized (Blattner et al, 1997;Keseler et al, 2013), and it can be speculated that ast corresponds to dcuA. The 'ast' genes in Kay (1971) should not be confused with the ast genes encoding the arginine succinyl-transferase (AST) pathway of arginine catabolism (Schneider et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

DcuA of aerobically grown Escherichia coli serves as a nitrogen shuttle (L‐aspartate/fumarate) for nitrogen uptake

Strecker

Schubert

Zedler

et al. 2018

Molecular Microbiology

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DcuA of Escherichia coli is known as an alternative C -dicarboxylate transporter for the main anaerobic C -dicarboxylate transporter DcuB. Since dcuA is expressed constitutively under aerobic and anaerobic conditions, DcuA was suggested to serve aerobically as a backup for the aerobic (DctA) transporter, or for the anabolic uptake of C -dicarboxylates. In this work, it is shown that DcuA is required for aerobic growth with L-aspartate as a nitrogen source, whereas for growth with L-aspartate as a carbon source, DctA was needed. Strains with DcuA catalyzed L-aspartate and C -dicarboxylate uptake (like DctA), or an L-aspartate/C -dicarboxylate antiport (unlike DctA). DcuA preferred L-aspartate to succinate in transport (K = 43 and 844 µM, respectively), whereas DctA has higher affinity for C -dicarboxylates like succinate compared to L-aspartate. When L-aspartate was supplied as the sole nitrogen source together with glycerol as the carbon source, L-aspartate was taken up by the bacteria and fumarate (or L-malate) was excreted in equimolar amounts. Both reactions depended on DcuA. L-Aspartate was taken up in amounts required for nitrogen metabolism but not for carbon metabolism. Therefore, DcuA catalyzes an L-aspartate/C -dicarboxylate antiport serving as a nitrogen shuttle for nitrogen supply without net carbon supply.

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“…Arginine can also be catabolized through the arginine succinyl pathway, which leads to the production of NH 3 , CO 2 , glutamate and succinate. This last metabolite then enters the citric acid cycle [82]. The presence of argininosuccinate synthetase in all the tissues of Riftia raises the possibility that this catabolic pathway is operative in the worm (Fig.…”

Section: Arginine Catabolism Via the Arginine And Ornithine Decarboxymentioning

confidence: 99%

Biochemical and enzymological aspects of the symbiosis between the deep‐sea tubeworm Riftia pachyptila and its bacterial endosymbiont

Minić

Hervé

2004

European Journal of Biochemistry

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Riftia pachyptila (Vestimentifera) is a giant tubeworm living around the volcanic deep-sea vents of the East Pacific Rise. This animal is devoid of a digestive tract and lives in an intimate symbiosis with a sulfur-oxidizing chemoautotrophic bacterium. This bacterial endosymbiont is localized in the cells of a richly vascularized organ of the worm: the trophosome. These organisms are adapted to their extreme environment and take advantage of the particular composition of the mixed volcanic and sea waters to extract and assimilate inorganic metabolites, especially carbon, nitrogen, oxygen and sulfur. The high molecular mass hemoglobin of the worm is the transporter for both oxygen and sulfide. This last compound is delivered to the bacterium which possesses the sulfur oxidizing respiratory system, which produces the metabolic energy for the two partners. CO 2 is also delivered to the bacterium where it enters the Calvin-Benson cycle.Some of the resulting small carbonated organic molecules are thus provided to the worm for its own metabolism. As far as nitrogen assimilation is concerned, NH 3 can be used by the two partners but nitrate can be used only by the bacterium. This very intimate symbiosis applies also to the organization of metabolic pathways such as those of pyrimidine nucleotides and arginine. In particular, the worm lacks the first three enzymes of the de novo pyrimidine biosynthetic pathways as well as some enzymes involved in the biosynthesis of polyamines. The bacterium lacks the enzymes of the pyrimidine salvage pathway. This symbiotic organization constitutes a very interesting system to study the molecular and metabolic basis of biological adaptation.

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Arginine Catabolism and the Arginine Succinyltransferase Pathway in Escherichia coli

Cited by 132 publications

References 36 publications

The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli

The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli

DcuA of aerobically grown Escherichia coli serves as a nitrogen shuttle (L‐aspartate/fumarate) for nitrogen uptake

Biochemical and enzymological aspects of the symbiosis between the deep‐sea tubeworm Riftia pachyptila and its bacterial endosymbiont

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