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Chemical Compound Review

CHEMBL145114     (2S)-2-amino-4-(hydroxy- methyl...

Synonyms: CHEBI:339898, AC1L3MFS, C04650, 1fpy, 35597-44-5, ...
 
 
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Disease relevance of phosphinothricin

 

High impact information on phosphinothricin

  • Increased levels of AS polypeptides and transcripts were also transiently observed in nodules by inhibiting GS activity with phosphinothricin [6].
  • Resistance to PPT in transgenic crops has been reported by nuclear expression of a bar transgene encoding phosphinothricin acetyltransferase, a detoxifying enzyme [7].
  • We report here expression of a bacterial bar gene (b-bar1) in tobacco (Nicotiana tabacum cv Petit Havana) plastids that confers field-level tolerance to Liberty, an herbicide containing PPT [7].
  • Expression of a fusion protein between the amino terminal region of GR and phosphinothricin acetyl transferase resulted in targeting of the foreign protein to chloroplasts and mitochondria [8].
  • Plant material was bombarded with the plasmid pDB1 containing the beta-glucuronidase gene (uidA) under the control of the actin-1 promoter of rice, and the selectable marker gene bar (phosphinothricin acetyltransferase) under the control of the CaMV 35S promoter [9].
 

Chemical compound and disease context of phosphinothricin

 

Biological context of phosphinothricin

 

Associations of phosphinothricin with other chemical compounds

  • PEG-mediated transformation was done with two plasmid constructs containing either a CaMV 35S promoter/HPH chimaeric gene conferring resistance to hygromycin (Hg) or a CaMV 35S promoter/BAR chimaeric gene conferring resistance to a commercial herbicide (Basta) containing phosphinothricin (PPT) [17].
  • The selectivity, efficiency and lifetime of normal- and narrow-bore columns for high-performance liquid chromatography were investigated for the separation and quantification of amino acids and the amino acid-like antibiotics phosphinothricin and phosphinothricylalanylalanine in biological samples [18].
  • Proliferating SMCs were bombarded with a mixture of plasmids containing the sgfp(S65T) gene and one of three selectable marker genes, phosphinothricin acetyltransferase (bar), hygromycin phosphotransferase (hpt) and neomycin phosphotransferase (nptII) [19].
  • Among three possible conformations of phosphinothricin in the active site of GS, this compatible with binding mode of methionine sulfoximine, determined recently by crystallography, was found to be energetically favored [20].
  • The test proteins consisted of Ara h 2 (a peanut conglutin-like protein), beta-lactoglobulin, bovine serum albumin, concanavalin A, horseradish peroxidase, ovalbumin, ovomucoid, phosphinothricin acetyltransferase, ribulose diphosphate carboxylase, and soybean trypsin inhibitor [21].
 

Gene context of phosphinothricin

 

Analytical, diagnostic and therapeutic context of phosphinothricin

  • Transgenic L. japonicus plants resistant to PPT were positive upon PCR by bar gene-specific primers [27].
  • Addition of thiol-compounds during infection and co-culture with Agrobacterium and the choice of the bar gene for selection with phosphinothricin were also important [28].
  • Direct selection of bar resistant transformants was achieved by allowing a 24 h period of recovery of cells transformed by biolistic procedure, followed by growth of the cells for one week under standard condition prior to harvesting and plating on the solid medium containing 0.5 microg/mL of phosphinothricin (PPT) [29].
  • Polymerase chain reaction and genomic Southern blot analysis confirmed stable integration of the transgenes in the genome of the PPT-resistant plants [30].

References

  1. Phosphinothricin tripeptide synthetases in Streptomyces viridochromogenes Tü494. Schwartz, D., Grammel, N., Heinzelmann, E., Keller, U., Wohlleben, W. Antimicrob. Agents Chemother. (2005) [Pubmed]
  2. Investigation of the mechanism of phosphinothricin inactivation of Escherichia coli glutamine synthetase using rapid quench kinetic technique. Abell, L.M., Villafranca, J.J. Biochemistry (1991) [Pubmed]
  3. The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Gill, H.S., Eisenberg, D. Biochemistry (2001) [Pubmed]
  4. Survival in soils of an herbicide-resistant Pseudomonas putida strain bearing a recombinant TOL plasmid. Ramos, J.L., Duque, E., Ramos-Gonzalez, M.I. Appl. Environ. Microbiol. (1991) [Pubmed]
  5. Development of Bean pod mottle virus-based vectors for stable protein expression and sequence-specific virus-induced gene silencing in soybean. Zhang, C., Ghabrial, S.A. Virology (2006) [Pubmed]
  6. Nodule-specific modulation of glutamine synthetase in transgenic Medicago truncatula leads to inverse alterations in asparagine synthetase expression. Carvalho, H.G., Lopes-Cardoso, I.A., Lima, L.M., Melo, P.M., Cullimore, J.V. Plant Physiol. (2003) [Pubmed]
  7. Expression of bar in the plastid genome confers herbicide resistance. Lutz, K.A., Knapp, J.E., Maliga, P. Plant Physiol. (2001) [Pubmed]
  8. Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco. Creissen, G., Reynolds, H., Xue, Y., Mullineaux, P. Plant J. (1995) [Pubmed]
  9. Fertile transgenic wheat from microprojectile bombardment of scutellar tissue. Becker, D., Brettschneider, R., Lörz, H. Plant J. (1994) [Pubmed]
  10. Stereospecific production of the herbicide phosphinothricin (glufosinate) by transamination: isolation and characterization of a phosphinothricin-specific transaminase from Escherichia coli. Schulz, A., Taggeselle, P., Tripier, D., Bartsch, K. Appl. Environ. Microbiol. (1990) [Pubmed]
  11. Conversion of bialaphos to other oligopeptides containing phosphinothricin by Streptomyces hygroscopicus. Kumada, Y., Imai, S., Nagaoka, K. J. Antibiot. (1991) [Pubmed]
  12. Agrobacterium-mediated genetic transformation and development of herbicide-resistant sugarcane (Saccharum species hybrids) using axillary buds. Manickavasagam, M., Ganapathi, A., Anbazhagan, V.R., Sudhakar, B., Selvaraj, N., Vasudevan, A., Kasthurirengan, S. Plant Cell Rep. (2004) [Pubmed]
  13. Isolation and characterization of the PEP-phosphomutase and the phosphonopyruvate decarboxylase genes from the phosphinothricin tripeptide producer Streptomyces viridochromogenes Tü494. Schwartz, D., Recktenwald, J., Pelzer, S., Wohlleben, W. FEMS Microbiol. Lett. (1998) [Pubmed]
  14. Peas (Pisum sativum L.). Grant, J., Cooper, P. Methods Mol. Biol. (2006) [Pubmed]
  15. Molecular cloning, sequence analysis, and heterologous expression of the phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces viridochromogenes DSM 40736. Blodgett, J.A., Zhang, J.K., Metcalf, W.W. Antimicrob. Agents Chemother. (2005) [Pubmed]
  16. Vectors based on maize streak virus can replicate to high copy numbers in maize plants. Shen, W.H., Hohn, B. J. Gen. Virol. (1995) [Pubmed]
  17. Herbicide-resistant Indica rice plants from IRRI breeding line IR72 after PEG-mediated transformation of protoplasts. Datta, S.K., Datta, K., Soltanifar, N., Donn, G., Potrykus, I. Plant Mol. Biol. (1992) [Pubmed]
  18. Separation of amino acids and antibiotics by narrow-bore and normal-bore high-performance liquid chromatography with pre-column derivatization. Fiedler, H.P., Plaga, A. J. Chromatogr. (1987) [Pubmed]
  19. Expression of green fluorescent protein and its inheritance in transgenic oat plants generated from shoot meristematic cultures. Cho, M.J., Choi, H.W., Okamoto, D., Zhang, S., Lemaux, P.G. Plant Cell Rep. (2003) [Pubmed]
  20. Computer-aided analysis of the interactions of glutamine synthetase with its inhibitors. Berlicki, L., Kafarski, P. Bioorg. Med. Chem. (2006) [Pubmed]
  21. A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins. Thomas, K., Aalbers, M., Bannon, G.A., Bartels, M., Dearman, R.J., Esdaile, D.J., Fu, T.J., Glatt, C.M., Hadfield, N., Hatzos, C., Hefle, S.L., Heylings, J.R., Goodman, R.E., Henry, B., Herouet, C., Holsapple, M., Ladics, G.S., Landry, T.D., MacIntosh, S.C., Rice, E.A., Privalle, L.S., Steiner, H.Y., Teshima, R., Van Ree, R., Woolhiser, M., Zawodny, J. Regulatory toxicology and pharmacology : RTP. (2004) [Pubmed]
  22. Inhibition of Escherichia coli glutamine synthetase by alpha- and gamma-substituted phosphinothricins. Logusch, E.W., Walker, D.M., McDonald, J.F., Franz, J.E., Villafranca, J.J., DiIanni, C.L., Colanduoni, J.A., Li, B., Schineller, J.B. Biochemistry (1990) [Pubmed]
  23. Stereospecific production of the herbicide phosphinothricin (glufosinate): purification of aspartate transaminase from Bacillus stearothermophilus, cloning of the corresponding gene, aspC, and application in a coupled transaminase process. Bartsch, K., Schneider, R., Schulz, A. Appl. Environ. Microbiol. (1996) [Pubmed]
  24. Design, synthesis, and activity of analogues of phosphinothricin as inhibitors of glutamine synthetase. Berlicki, Ł., Obojska, A., Forlani, G., Kafarski, P. J. Med. Chem. (2005) [Pubmed]
  25. Nucleotide sequence analysis reveals linked N-acetyl hydrolase, thioesterase, transport, and regulatory genes encoded by the bialaphos biosynthetic gene cluster of Streptomyces hygroscopicus. Raibaud, A., Zalacain, M., Holt, T.G., Tizard, R., Thompson, C.J. J. Bacteriol. (1991) [Pubmed]
  26. Phosphinothricin induces epileptic activity via nitric oxide production through NMDA receptor activation in adult mice. Lapouble, E., Montécot, C., Sevestre, A., Pichon, J. Brain Res. (2002) [Pubmed]
  27. Transformation of Lotus japonicus using the herbicide resistance bar gene as a selectable marker. Lohar, D.P., Schuller, K., Buzas, D.M., Gresshoff, P.M., Stiller, J. J. Exp. Bot. (2001) [Pubmed]
  28. Genetic transformation of cowpea (Vigna unguiculata L.) and stable transmission of the transgenes to progeny. Popelka, J.C., Gollasch, S., Moore, A., Molvig, L., Higgins, T.J. Plant Cell Rep. (2006) [Pubmed]
  29. The actin gene promoter-driven bar as a dominant selectable marker for nuclear transformation of Dunaliella salina. Jiang, G.Z., Lü, Y.M., Niu, X.L., Xue, L.X. Yi Chuan Xue Bao (2005) [Pubmed]
  30. A multi-needle-assisted transformation of soybean cotyledonary node cells. Xue, R.G., Xie, H.F., Zhang, B. Biotechnol. Lett. (2006) [Pubmed]
 
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