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Relevant bibliographies by topics / Enzyme inhibition; Phosphinothricin

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Academic literature on the topic 'Enzyme inhibition; Phosphinothricin'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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Journal articles on the topic "Enzyme inhibition; Phosphinothricin"

1

Forlani, Giuseppe, Barbara Lejczak, and Pawel Kafarski. "The herbicidally active compound N-2-(5-chloro-pyridyl) aminomethylene bisphosphonic acid acts by inhibiting both glutamine and aromatic amino acid biosynthesis." Functional Plant Biology 27, no. 7 (2000): 677. http://dx.doi.org/10.1071/pp00011.

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The effect of the herbicidally active compound N-2-(5-chloro-pyridyl)aminomethylene bisphosphonic acid (Cl-pyr-AMBPA), previously found in vitro to inhibit the activity of the first enzyme in the shikimate pathway 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, was investigated in vivo on suspension cultured cells of Nicotiana plumbaginifolia Viviani. Amino acid pool measurement showed an actual reduction of tyrosine, tryptophan and phenylalanine level following the addition of the compound to the growth medium. However, an even stronger effect was noticed for other amino acids, mainly g

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2

Wild, Aloysius, and Christine Ziegler. "The Effect of Bialaphos on Ammonium-Assimilation and Photosynthesis I. Effect on the Enzymes of Ammonium-Assimilation." Zeitschrift für Naturforschung C 44, no. 1-2 (1989): 97–102. http://dx.doi.org/10.1515/znc-1989-1-217.

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Abstract In this investigation, the effect of bialaphos (phosphinothricyl-alanyl-alanine) on the enzymes involved in NH4+-assimilation - glutamine synthetase, glutamine-2-oxoglutarate aminotransferase, glutamate dehydrogenase - is examined and compared to the effect of phosphinothricin (glufosinate) on the same enzymes. Bialaphos was given to whole plants (in vivo) and to leaf homogenate (in vitro). The investigation showed that bialaphos has an inhibiting effect on glutamine synthetase in vivo, but not in vitro. In contrast to this, phosphinothricin inhibits glutamine synthetase in vitro as w

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3

Seabra, Ana R., Patrícia A. Pereira, Jörg D. Becker, and Helena G. Carvalho. "Inhibition of Glutamine Synthetase by Phosphinothricin Leads to Transcriptome Reprograming in Root Nodules of Medicago truncatula." Molecular Plant-Microbe Interactions® 25, no. 7 (2012): 976–92. http://dx.doi.org/10.1094/mpmi-12-11-0322.

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Glutamine synthetase (GS) is a vital enzyme for the assimilation of ammonia into amino acids in higher plants. In legumes, GS plays a crucial role in the assimilation of the ammonium released by nitrogen-fixing bacteria in root nodules, constituting an important metabolic knob controlling the nitrogen (N) assimilatory pathways. To identify new regulators of nodule metabolism, we profiled the transcriptome of Medicago truncatula nodules impaired in N assimilation by specifically inhibiting GS activity using phosphinothricin (PPT). Global transcript expression of nodules collected before and aft

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4

Mahan, James R., Peter A. Dotray, Ginger G. Light, and Kristy R. Dawson. "Thermal dependence of bioengineered glufosinate tolerance in cotton." Weed Science 54, no. 1 (2006): 1–5. http://dx.doi.org/10.1614/ws-05-042r.1.

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Tolerance to glufosinate has been bioengineered into cotton through the expression of a gene encoding the enzyme phosphinothricin acetyl transferase (PAT). Studies were conducted to determine thermal limitations on herbicide efficacy in bioengineered cotton. The 50% inhibition (I50) of glufosinate of the target-site enzyme glutamine synthetase was thermally dependent with the lowest values between 25 and 35 C. Larger values of I50were measured above and below the 25 to 35 C range. The apparent Michaelis constant KMof the enzyme PAT was relatively stable from 15 to 30 C and increased more rapid

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5

Wild, Aloysius, and Christine Wendler. "Inhibitory Action of Glufosinate on Photosynthesis." Zeitschrift für Naturforschung C 48, no. 3-4 (1993): 369–73. http://dx.doi.org/10.1515/znc-1993-3-441.

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Glufosinate (phosphinothricin) irreversibly blocks the glutamine synthetase which subsequently gives rise to an accumulation of ammonium and to a strong decrease in some amino acids, especially glutamine and glutamate.Under atmospheric conditions (400 ppm CO2, 21% O2) glufosinate causes a rapid inhibition of photosynthesis, too. H ow ever, under non-photo respiratory conditions (1000 ppm CO2, 2% O2) only a slight inhibition of photosynthesis occurs with glufosinate. Since under both conditions an accumulation of ammonium occurs, it is concluded that inhibition of photosynthesis is not induced

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MONTANINI, Barbara, Marco BETTI, Antonio J. MÁRQUEZ, Raffaella BALESTRINI, Paola BONFANTE, and Simone OTTONELLO. "Distinctive properties and expression profiles of glutamine synthetase from a plant symbiotic fungus." Biochemical Journal 373, no. 2 (2003): 357–68. http://dx.doi.org/10.1042/bj20030152.

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Nitrogen retrieval and assimilation by symbiotic ectomycorrhizal fungi is thought to play a central role in the mutualistic interaction between these organisms and their plant hosts. Here we report on the molecular characterization of the key N-assimilation enzyme glutamine synthetase from the mycorrhizal ascomycete Tuber borchii (TbGS). TbGS displayed a strong positive co-operativity (n=1.7±0.29) and an unusually high S0.5 value (54±16 mM; S0.5 is the substrate concentration value at which v=½Vmax) for glutamate, and a correspondingly low sensitivity towards inhibition by the glutamate analog

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7

Logusch, Eugene W., Daniel M. Walker, John F. McDonald, and John E. Franz. "Substrate variability as a factor in enzyme inhibitor design: inhibition of ovine brain glutamine synthetase by .alpha.- and .gamma.-substituted phosphinothricins." Biochemistry 28, no. 7 (1989): 3043–51. http://dx.doi.org/10.1021/bi00433a046.

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8

Nerland, Audun Helge, Per Brandtzæg, Merethe Aasmo Finne, et al. "Environmental Risk Assessment of Glufosinate-Tolerant Genetically Modified Oilseed Rape MS8, RF3 and MS8 x RF3 for Import, Processing and Feed Uses under Directive 2001/18/EC (Notification C/BE/96/01)." European Journal of Nutrition & Food Safety, November 19, 2019, 51–55. http://dx.doi.org/10.9734/ejnfs/2019/v11i130130.

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In preparation for a legal implementation of EU-regulation 1829/2003, the Norwegian Scientific Committee for Food Safety (VKM) has been requested by the Norwegian Directorate for Nature Management to conduct final environmental risk assessments for all genetically modified organisms (GMOs) and products containing or consisting of GMOs that are authorized in the European Union under Directive 2001/18/EC or Regulation 1829/2003/EC. The request covers scope(s) relevant to the Gene Technology Act. The request does not cover GMOs that VKM already has conducted its final risk assessments on. However

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9

Andreassen, Åshild, Per Brandtzæg, Merethe Aasmo Finne, et al. "Food/Feed and Environmental Risk Assessment of Genetically Modified Glufosinate-tolerant Oilseed Rape MS8, RF3 and MS8 x RF3 for Import, Processing and Feed Uses under Directive 2001/18/EC (Notification C/BE/96/01)." European Journal of Nutrition & Food Safety, April 15, 2020, 5–9. http://dx.doi.org/10.9734/ejnfs/2020/v12i330199.

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In preparation for a legal implementation of EU-regulation 1829/2003, the Norwegian Environment Agency (former Norwegian Directorate for Nature Management) has requested the Norwegian Food Safety Authority (NFSA) to give final opinions on all genetically modified organisms (GMOs) and products containing or consisting of GMOs that are authorized in the European Union under Directive 2001/18/EC or Regulation 1829/2003/EC within the Authority’s sectoral responsibility. The Norwegian Food Safety Authority has therefore, by letter dated 13 February 2013 (ref. 2012/150202), requested the Norwegian S

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Dissertations / Theses on the topic "Enzyme inhibition; Phosphinothricin"

1

Varley, Denise Joyce. "Novel inhibitors of glutamine synthase." Thesis, University of Oxford, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.308650.

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