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Thematische Bibliographien / Prolin catabolism

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Zeitschriftenartikel

Auswahl der wissenschaftlichen Literatur zum Thema „Prolin catabolism“

Autor: Grafiati

Veröffentlicht am 25. Mai 2024

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Zeitschriftenartikel zum Thema "Prolin catabolism"

1

Guerrier, Gilles. "Effect of salt-stress on proline metabolism in calli of Lycopersicon esculentum, Lycopersicon pennellii, and their interspecific hybrid." Canadian Journal of Botany 73, no. 12 (1995): 1939–46. http://dx.doi.org/10.1139/b95-206.

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Amino acid pools and enzyme activities of NH3-assimilation (glutamine synthetase, glutamate synthase), proline biosynthesis (pyrroline-5-carboxylate reductase), proline catabolism (proline dehydrogenase, proline oxidase), and ornithine transamination (ornithine transaminase) were determined in control and salinized (140 mM NaCl) calli from tomato roots. Three populations were used: the domestic salt-sensitive Lycopersicon esculentum Mill. cv. P-73, the wild salt-tolerant Lycopersicon pennellii (Correll) D'Arcy, accession PE-47, and their F1 interspecific cross, for which the relative growth ra

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2

Grantham, Barbara D., and J. Barrett. "Amino acid catabolism in the nematodes Heligmosomoides polygyrus and Panagrellus redivivus 2. Metabolism of the carbon skeleton." Parasitology 93, no. 3 (1986): 495–504. http://dx.doi.org/10.1017/s0031182000081208.

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SUMMARYAll of the enzymes of proline catabolism were present in Heligmosomoides polygyrus and Panagrellus redivivus and the activities were, in general, similar to those found in rat liver. Both nematodes were also shown to be able to catabolize the branched-chain amino acids leucine, isoleucine and valine, by pathways similar to those found in mammalian liver. There were no significant differences in amino acid catabolism between the animal-parasitic and free-living species of nematode.

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3

Phillips, Donald A., Eve S. Sande, J. A. C. Vriezen, Frans J. de Bruijn, Daniel Le Rudulier, and Cecillia M. Joseph. "A New Genetic Locus in Sinorhizobium meliloti Is Involved in Stachydrine Utilization." Applied and Environmental Microbiology 64, no. 10 (1998): 3954–60. http://dx.doi.org/10.1128/aem.64.10.3954-3960.1998.

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ABSTRACT Stachydrine, a betaine released by germinating alfalfa seeds, functions as an inducer of nodulation genes, a catabolite, and an osmoprotectant in Sinorhizobium meliloti. Two stachydrine-inducible genes were found in S. meliloti1021 by mutation with a Tn5-luxAB promoter probe. Both mutant strains (S10 and S11) formed effective alfalfa root nodules, but neither grew on stachydrine as the sole carbon and nitrogen source. When grown in the absence or presence of salt stress, S10 and S11 took up [14C]stachydrine as well as wild-type cells did, but neither used stachydrine effectively as an

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4

Diab, Farès, Théophile Bernard, Alexis Bazire, Dominique Haras, Carlos Blanco, and Mohamed Jebbar. "Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities." Microbiology 152, no. 5 (2006): 1395–406. http://dx.doi.org/10.1099/mic.0.28652-0.

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Glycine betaine (GB) and its immediate precursors choline and carnitine, dimethylsulfonioacetate, dimethylsulfoniopropionate, ectoine and proline were effective osmoprotectants for Pseudomonas aeruginosa, but pipecolate, trehalose and sucrose had no osmoprotective effect. GB was accumulated stably or transiently when succinate or glucose, respectively, was used as a carbon and energy source. The catabolite repression mediated by succinate occurred at both low and high salinities, and it did not involve the global regulators Vfr and Crc. A proteomic analysis showed that at least 21 proteins wer

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5

Tanner, John J. "Structural biology of proline catabolism." Amino Acids 35, no. 4 (2008): 719–30. http://dx.doi.org/10.1007/s00726-008-0062-5.

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6

Deutch, Charles E., James M. Hasler, Rochelle M. Houston, Manish Sharma, and Valerie J. Stone. "Nonspecific inhibition of proline dehydrogenase synthesis in Escherichia coli during osmotic stress." Canadian Journal of Microbiology 35, no. 8 (1989): 779–85. http://dx.doi.org/10.1139/m89-130.

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L-Proline, which is accumulated by Escherichia coli during growth in media of high osmolality, also induces the synthesis of the enzyme degrading it to glutamate. To determine if proline catabolism is inhibited during osmotic stress, proline utilization and the formation of proline dehydrogenase were examined in varying concentrations of NaCl and sucrose. Although the specific growth rate of E. coli with proline as the sole nitrogen source diminished as the solute osmolality increased, a comparable reduction in growth rate occurred with ammonium as the primary nitrogen source. Proline cataboli

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7

Pallag, Gergely, Sara Nazarian, Dora Ravasz, et al. "Proline Oxidation Supports Mitochondrial ATP Production When Complex I Is Inhibited." International Journal of Molecular Sciences 23, no. 9 (2022): 5111. http://dx.doi.org/10.3390/ijms23095111.

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The oxidation of proline to pyrroline-5-carboxylate (P5C) leads to the transfer of electrons to ubiquinone in mitochondria that express proline dehydrogenase (ProDH). This electron transfer supports Complexes CIII and CIV, thus generating the protonmotive force. Further catabolism of P5C forms glutamate, which fuels the citric acid cycle that yields the reducing equivalents that sustain oxidative phosphorylation. However, P5C and glutamate catabolism depend on CI activity due to NAD+ requirements. NextGen-O2k (Oroboros Instruments) was used to measure proline oxidation in isolated mitochondria

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8

Belitsky, Boris R., and Abraham L. Sonenshein. "Modulation of Activity of Bacillus subtilis Regulatory Proteins GltC and TnrA by Glutamate Dehydrogenase." Journal of Bacteriology 186, no. 11 (2004): 3399–407. http://dx.doi.org/10.1128/jb.186.11.3399-3407.2004.

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ABSTRACT The Bacillus subtilis gltAB operon, encoding glutamate synthase, requires a specific positive regulator, GltC, for its expression and is repressed by the global regulatory protein TnrA. The factor that controls TnrA activity, a complex of glutamine synthetase and a feedback inhibitor, such as glutamine, is known, but the signal for modulation of GltC activity has remained elusive. GltC-dependent gltAB expression was drastically reduced when cells were grown in media containing arginine or ornithine or proline, all of which are inducers and substrates of the Roc catabolic pathway. Anal

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9

Cruz-Leite, Vanessa Rafaela Milhomem, André Luís Elias Moreira, Lana O’Hara Souza Silva, et al. "Proteomics of Paracoccidioides lutzii: Overview of Changes Triggered by Nitrogen Catabolite Repression." Journal of Fungi 9, no. 11 (2023): 1102. http://dx.doi.org/10.3390/jof9111102.

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Members of the Paracoccidioides complex are the causative agents of Paracoccidioidomycosis (PCM), a human systemic mycosis endemic in Latin America. Upon initial contact with the host, the pathogen needs to uptake micronutrients. Nitrogen is an essential source for biosynthetic pathways. Adaptation to nutritional stress is a key feature of fungi in host tissues. Fungi utilize nitrogen sources through Nitrogen Catabolite Repression (NCR). NCR ensures the scavenging, uptake and catabolism of alternative nitrogen sources, when preferential ones, such as glutamine or ammonium, are unavailable. The

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10

Chen, Siyun, Catharine E. White, George C. diCenzo, et al. "l-Hydroxyproline and d-Proline Catabolism in Sinorhizobium meliloti." Journal of Bacteriology 198, no. 7 (2016): 1171–81. http://dx.doi.org/10.1128/jb.00961-15.

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ABSTRACTSinorhizobium melilotiforms N2-fixing root nodules on alfalfa, and as a free-living bacterium, it can grow on a very broad range of substrates, includingl-proline and several related compounds, such as proline betaine,trans-4-hydroxy-l-proline (trans-4-l-Hyp), andcis-4-hydroxy-d-proline (cis-4-d-Hyp). Fourteenhypgenes are induced upon growth ofS. melilotiontrans-4-l-Hyp, and of those,hypMNPQencodes an ABC-typetrans-4-l-Hyp transporter andhypREencodes an epimerase that convertstrans-4-l-Hyp tocis-4-d-Hyp in the bacterial cytoplasm. Here, we present evidence that the HypO, HypD, and HypH

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