Biosynthesis and metabolism of arginine in bacteria.

Cunin, Raymond; Glansdorff, Nicolas; Pierard, André; Stalon, Victor

doi:10.1128/mmbr.50.3.314-352.1986

Cited by 517 publications

(352 citation statements)

References 261 publications

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“…Similar to NAGK-20 of L. hongkongensis, NAGK of Pseudomonas aeruginosa and Thermotoga maritima, which employ the cyclic pathway, can be inhibited by arginine as the rate-limiting enzyme for negative feedback control [34][35][36][37]. On the other hand, similar to NAGK-37 of L. hongkongensis, NAGK of E. coli, which employs the linear pathway, is not inhibited by arginine [35,36]. We speculate that L. hongkongensis can use different pathways with the two NAGK isoenzymes with differential importance at different temperatures of different habitats.…”

Section: Adaptability To Different Environmental Temperaturesmentioning

confidence: 99%

The Complete Genome and Proteome of Laribacter hongkongensis Reveal Potential Mechanisms for Adaptations to Different Temperatures and Habitats

et al. 2009

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Laribacter hongkongensis is a newly discovered Gram-negative bacillus of the Neisseriaceae family associated with freshwater fish–borne gastroenteritis and traveler's diarrhea. The complete genome sequence of L. hongkongensis HLHK9, recovered from an immunocompetent patient with severe gastroenteritis, consists of a 3,169-kb chromosome with G+C content of 62.35%. Genome analysis reveals different mechanisms potentially important for its adaptation to diverse habitats of human and freshwater fish intestines and freshwater environments. The gene contents support its phenotypic properties and suggest that amino acids and fatty acids can be used as carbon sources. The extensive variety of transporters, including multidrug efflux and heavy metal transporters as well as genes involved in chemotaxis, may enable L. hongkongensis to survive in different environmental niches. Genes encoding urease, bile salts efflux pump, adhesin, catalase, superoxide dismutase, and other putative virulence factors—such as hemolysins, RTX toxins, patatin-like proteins, phospholipase A1, and collagenases—are present. Proteomes of L. hongkongensis HLHK9 cultured at 37°C (human body temperature) and 20°C (freshwater habitat temperature) showed differential gene expression, including two homologous copies of argB, argB-20, and argB-37, which encode two isoenzymes of N-acetyl-L-glutamate kinase (NAGK)—NAGK-20 and NAGK-37—in the arginine biosynthesis pathway. NAGK-20 showed higher expression at 20°C, whereas NAGK-37 showed higher expression at 37°C. NAGK-20 also had a lower optimal temperature for enzymatic activities and was inhibited by arginine probably as negative-feedback control. Similar duplicated copies of argB are also observed in bacteria from hot springs such as Thermus thermophilus, Deinococcus geothermalis, Deinococcus radiodurans, and Roseiflexus castenholzii, suggesting that similar mechanisms for temperature adaptation may be employed by other bacteria. Genome and proteome analysis of L. hongkongensis revealed novel mechanisms for adaptations to survival at different temperatures and habitats.

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Section: Adaptability To Different Environmental Temperaturesmentioning

confidence: 99%

The Complete Genome and Proteome of Laribacter hongkongensis Reveal Potential Mechanisms for Adaptations to Different Temperatures and Habitats

et al. 2009

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“…The genes for the enzymes of the ADI pathway have been identified and described earlier together with a short regulatory gene product (arcR) and were found to be clustered in the arcRACB gene cluster [1]. The ADI pathway is found in several groups within the domain bacteria such as Pseudomonas, Mycoplasma, Bacillus and lactic bacteria [2]. In Pseudomonas aeruginosa an additional gene arcD was identified which codes for an arginine/ornithine antiporter [3].…”

Section: Introductionmentioning

confidence: 99%

Identification of the arginine/ornithine antiporter ArcD from Halobacterium salinarum

Wimmer¹,

Oberwinkler²,

Bisle³

et al. 2008

FEBS Letters

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This paper identifies the first arginine/ornithine antiporter ArcD from the domain of archea. The functional role of ArcD is demonstrated by transport assays with radioactive labelled arginine, by its necessity to enable arginine fermentation under anaerobic growth conditions and by the consumption of arginine from the medium during growth. All three experimentally observables are severely disturbed when the deletion strain DArcD is used. The isolated protein is verified by mass spectrometry and reconstituted in vesicles. The proteoliposomes are attached to a membrane and capacitive currents are recorded which appear upon initiation of the transport process by change from arginine-free to arginine-containing buffer. This clearly demonstrates that the purified 34 kD protein is the functional unit.

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“…3.5.3.1) are metal ion-activated enzymes which catalyse the hydrolysis of L-arginine to L-ornithine and urea. This reaction is part of the urea cycle in ureotelic animals, and is the initial step of arginine catabolism in certain aerobic bacteria [4]. Despite considerable research on trimeric eukaryotic arginases, notably from rat liver [5][6][7][8] and yeast [9][10][11], these enzymes remain very much a mechanistic and structural mystery.…”

Section: Introductionmentioning

confidence: 99%

The cloning, expression and crystallisation of a thermostable arginase

et al. 1996

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The gene for the thermostable arginase from the thermophilic bacterium 'Bacillus caldovelox" has been cloned and sequenced. Expression of recombinant arginase at high levels has been achieved in E. coil using an inducible T7 RNA polymerasebased system. A facile purification procedure incorporating a heat-treatment step yielded 0.2 g of recombinant arginase per litre of induced culture. The kinetic properties of the purified recombinant protein are essentially identical to the native enzyme. The recombinant protein has been crystaHised and one crystal form is isomorphous to crystals of the native protein.

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Biosynthesis and metabolism of arginine in bacteria.

Cited by 517 publications

References 261 publications

The Complete Genome and Proteome of Laribacter hongkongensis Reveal Potential Mechanisms for Adaptations to Different Temperatures and Habitats

The Complete Genome and Proteome of Laribacter hongkongensis Reveal Potential Mechanisms for Adaptations to Different Temperatures and Habitats

Identification of the arginine/ornithine antiporter ArcD from Halobacterium salinarum

The cloning, expression and crystallisation of a thermostable arginase

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