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Journal articles on the topic 'EPSP-synthase'

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Published: 4 June 2021

Last updated: 7 February 2022

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1

Sutton, Kristin A., Jennifer Breen, Thomas A. Russo, L. Wayne Schultz, and Timothy C. Umland. "Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogenAcinetobacter baumannii." Acta Crystallographica Section F Structural Biology Communications 72, no. 3 (February 16, 2016): 179–87. http://dx.doi.org/10.1107/s2053230x16001114.

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The enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the sixth step of the seven-step shikimate pathway. Chorismate, the product of the pathway, is a precursor for the biosynthesis of aromatic amino acids, siderophores and metabolites such as folate, ubiquinone and vitamin K. The shikimate pathway is present in bacteria, fungi, algae, plants and apicomplexan parasites, but is absent in humans. The EPSP synthase enzyme produces 5-enolpyruvylshikimate 3-phosphate and phosphate from phosphoenolpyruvate and shikimate 3-phosphateviaa transferase reaction, and is the target of the herbicide glyphosate. TheAcinetobacter baumanniigene encoding EPSP synthase,aroA, has previously been demonstrated to be essential during host infection for the growth and survival of this clinically important drug-resistant ESKAPE pathogen. Prephenate dehydrogenase is also encoded by the bifunctionalA. baumannii aroAgene, but its activity is dependent upon EPSP synthase since it operates downstream of the shikimate pathway. As part of an effort to evaluate new antimicrobial targets, recombinantA. baumanniiEPSP (AbEPSP) synthase, comprising residues Ala301–Gln756 of thearoAgene product, was overexpressed inEscherichia coli, purified and crystallized. The crystal structure, determined to 2.37 Å resolution, is described in the context of a potential antimicrobial target and in comparison to EPSP synthases that are resistant or sensitive to the herbicide glyphosate.

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2

Lewis, Julian, Kenneth A. Johnson, and Karen S. Anderson. "The Catalytic Mechanism of EPSP Synthase Revisited†." Biochemistry 38, no. 22 (June 1999): 7372–79. http://dx.doi.org/10.1021/bi9830258.

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3

Lou, Meiyan, Steven K. Burger, Meghann E. Gilpin, Vivian Gawuga, Alfredo Capretta, and Paul J. Berti. "Transition State Analysis of Enolpyruvylshikimate 3-Phosphate (EPSP) Synthase (AroA)-Catalyzed EPSP Hydrolysis." Journal of the American Chemical Society 134, no. 31 (July 24, 2012): 12958–69. http://dx.doi.org/10.1021/ja304339h.

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4

Thompson, Gregory A., William R. Hiatt, Daniel Facciotti, David M. Stalker, and Luca Comai. "Expression in Plants of a Bacterial Gene Coding for Glyphosate Resistance." Weed Science 35, S1 (1987): 19–23. http://dx.doi.org/10.1017/s0043174500060999.

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The target site of glyphosate [N-(phosphonomethyl)glycine] inhibition in plants and bacteria is 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase. Our strategy for developing glyphosate-resistant crops has been to genetically engineer plants with a gene that codes for EPSP synthase with low sensitivity in glyphosate. We cloned such a gene from thearoAlocus of a glyphosate-resistant mutagenized strain ofSalmonella typhimurium.The enzyme encoded by this gene has a single amino acid change resulting in lower affinity for glyphosate and higher affinity for substrates than either plant or wild-type bacterial counterpart. A chimaeric gene containing the mutantaroAgene behind the octopine synthase promoter was constructed and integrated intoAgrobacteriumT-DNA vectors. Analysis of gall tissue fromBrassica campestrisL. (turnip rape) infected withA. tumefaciensK12 containing this chimaera showed mRNA and protein expressed from the bacterial gene; 50% of the total EPSP synthase activity present had kinetic properties of the mutant bacterial enzyme. Tobacco (Nicotiana tabacumL. ‘Xanthi′) plants have been regenerated from cocultivation withA. rhizogenescontaining the same construct; analysis indicates expression of the gene and enhanced tolerance to glyphosate.

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5

Walker, Mark C., Joel E. Ream, R. Douglas Sammons, Eugene W. Logusch, Marion H. O'Leary, Ronald L. Somerville, and James A. Sikorski. "Structural requirements for pep binding To EPSP synthase." Bioorganic & Medicinal Chemistry Letters 1, no. 12 (January 1991): 683–88. http://dx.doi.org/10.1016/s0960-894x(01)81048-9.

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6

Saunders, J. E., E. P. Carpenter, P. Vaithanomsat, J. R. Coggins, and K. A. Brown. "Structure-function studies of EPSP synthase fromPseudomonas aeruginosa." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c112. http://dx.doi.org/10.1107/s0108767302089511.

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7

ALBERG, D. G., C. T. LAUHON, R. NYFELER, A. FAESSLER, and P. A. BARTLETT. "ChemInform Abstract: Inhibition of EPSP Synthase by Analogues of the Tetrahedral Intermediate and of EPSP." ChemInform 23, no. 34 (August 21, 2010): no. http://dx.doi.org/10.1002/chin.199234302.

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8

Fonseca, Emily C. M., Kauê S. da Costa, Jerônimo Lameira, Cláudio Nahum Alves, and Anderson H. Lima. "Investigation of the target-site resistance of EPSP synthase mutants P106T and T102I/P106S against glyphosate." RSC Advances 10, no. 72 (2020): 44352–60. http://dx.doi.org/10.1039/d0ra09061a.

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9

Seto, Christopher T., and Paul A. Bartlett. "(Z)-9-Fluoro-EPSP Is Not a Substrate for EPSP Synthase: Implications for the Enzyme Mechanism." Journal of Organic Chemistry 59, no. 23 (November 1994): 7130–32. http://dx.doi.org/10.1021/jo00102a046.

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10

Pereira, José Henrique, Fernanda Canduri, Jaim Simões de Oliveira, Nelson José Freitas da Silveira, Luiz Augusto Basso, Mário Sérgio Palma, Walter Filgueira de Azevedo, and Diógenes Santiago Santos. "Structural bioinformatics study of EPSP synthase from Mycobacterium tuberculosis." Biochemical and Biophysical Research Communications 312, no. 3 (December 2003): 608–14. http://dx.doi.org/10.1016/j.bbrc.2003.10.175.

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11

Sammons, R. Douglas, Kenneth J. Gruys, Karen S. Anderson, Kenneth A. Johnson, and James A. Sikorski. "Reevaluating Glyphosate as a Transition-State Inhibitor of EPSP Synthase: Identification of an EPSP Synthase.cntdot.EPSP.cntdot.Glyphosate Ternary Complex." Biochemistry 34, no. 19 (May 16, 1995): 6433–40. http://dx.doi.org/10.1021/bi00019a024.

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12

Alberg, David G., Charles T. Lauhon, Robert Nyfeler, Alex Faessler, and Paul A. Bartlett. "Inhibition of 5-enolpyruvoylshikimate 3-phosphate (EPSP) synthase by analogs of the tetrahedral intermediate and of EPSP." Journal of the American Chemical Society 114, no. 9 (April 1992): 3535–46. http://dx.doi.org/10.1021/ja00035a058.

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13

Pansegrau, Paul D., Karen S. Anderson, Theodore Widlanski, Joel E. Ream, R. Douglas Sammons, James A. Sikorski, and Jeremy R. Knowles. "Synthesis and evaluation of two new inhibitors of EPSP synthase." Tetrahedron Letters 32, no. 23 (June 1991): 2589–92. http://dx.doi.org/10.1016/s0040-4039(00)78792-2.

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14

Miller, Michael J., Joel E. Ream, Mark C. Walker, and James A. Sikorski. "Functionalized 3,5-dihydroxybenzoates as potent novel inhibitors of EPSP synthase." Bioorganic & Medicinal Chemistry 2, no. 5 (May 1994): 331–38. http://dx.doi.org/10.1016/s0968-0896(00)82189-6.

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15

Caetano, Melissa Soares, Matheus P. Freitas, Elaine F. F. da Cunha, and Teodorico C. Ramalho. "Construction and assessment of reaction models of Class I EPSP synthase. Part II: investigation of the EPSP ketal." Journal of Biomolecular Structure and Dynamics 31, no. 4 (April 2013): 393–402. http://dx.doi.org/10.1080/07391102.2012.703066.

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16

MACHEROUX, Peter, Ernst SCHÖNBRUNN, Dmitri I. SVERGUN, Vladimir V. VOLKOV, Michel H. J. KOCH, Stephen BORNEMANN, and Roger N. F. THORNELEY. "Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding." Biochemical Journal 335, no. 2 (October 15, 1998): 319–27. http://dx.doi.org/10.1042/bj3350319.

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Chorismate synthase (EC 4.6.1.4) catalyses the conversion of 5-enolpyruvylshikimate 3-phosphate (EPSP) into chorismate, and requires reduced FMN as a cofactor. The enzyme can bind first oxidized FMN and then EPSP to form a stable ternary complex which does not undergo turnover. This complex can be considered to be a model of the ternary complex between enzyme, EPSP and reduced FMN immediately before catalysis commences. It is shown that the binding of oxidized FMN and EPSP to chorismate synthase affects the properties and structure of the protein. Changes in small-angle X-ray scattering data, decreased susceptibility to tryptic digestion and altered Fourier-transform (FT)-IR spectra provide the first strong evidence for major structural changes in the protein. The tetrameric enzyme undergoes correlated screw movements leading to a more overall compact shape, with no change in oligomerization state. The changes in the FT-IR spectrum appear to reflect changes in the environment of the secondary-structural elements rather than alterations in their distribution, because the far-UV CD spectrum changes very little. Changes in the mobility of the protein during non-denaturing PAGE indicate that the ternary complex may exhibit less conformational flexibility than the apoprotein. Increased enzyme solubility and decreased tryptophan fluorescence are discussed in the light of the observed structural changes. The secondary structure of the enzyme was investigated using far-UV CD spectroscopy, and the tertiary structure was predicted to be an α–β-barrel using discrete state-space modelling.

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17

Kishore, Ganesh M., Stephen R. Padgette, and Robert T. Fraley. "History of Herbicide-Tolerant Crops, Methods of Development and Current State of the Art – Emphasis on Glyphosate Tolerance." Weed Technology 6, no. 3 (September 1992): 626–34. http://dx.doi.org/10.1017/s0890037x00035934.

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Weed management is an integral part of agriculture; weeds lower both productivity and quality of agricultural products. A combination of mechanical, chemical, biological, and cultural methods is expected to deliver a sustainable weed management program for the next two decades. While chemical methods offer the most cost effective means of weed management, crop selectivity has hampered the use of the best chemicals for weed management. Recent progress in gene technology has facilitated the introduction and expression of genes to confer a wide range of traits to crop plants. Application of this technology has resulted in the development of crop plant genotypes that are resistant to a specific herbicide. This article describes the progress that has been made by our group toward the introduction of glyphosate tolerance to crop plants. Glyphosate [N-(phosphonomethyl)glycine] kills plants due to inhibition of the biosynthesis of aromatic compounds via the shikimate pathway. Our approach for introduction of glyphosate tolerance is based on insertion and expression in plants of a gene encoding a glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase, a key enzyme of the shikimate pathway. The wild type enzyme present in plants is susceptible to inhibition glyphosate; variants of EPSP synthase have been produced that are less susceptible to inhibition by glyphosate. Expression of genes encoding these variants has been shown to confer glyphosate tolerance to plants. The degree of glyphosate tolerance is related to the tolerance characteristics of the EPSP synthase variant, its substrate activity, targeting to the plastid, and the level of expression of the variant gene. The tissue specificity of expression of the variant EPSP synthase has also been shown to be critical since glyphosate is a systemic herbicide and is translocated to many growing points within the plant. Our studies on glyphosate tolerance have substantially enhanced our understanding of the mode-of-action of glyphosate, the shikimate pathway, and protein sorting within plant cells, as well as developmental and tissue specific expression of genes in plants. Commercial use of glyphosate tolerance technology is expected to affect positively, the weed management arsenal available to the farmers, the sustainability of farm land and groundwater, and promote the use of a “soft” herbicide.

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18

Anderson, Karen S., and Kenneth A. Johnson. "Kinetic and structural analysis of enzyme intermediates: lessons from EPSP synthase." Chemical Reviews 90, no. 7 (November 1990): 1131–49. http://dx.doi.org/10.1021/cr00105a004.

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19

dos Santos, Alberto M., Anderson H. Lima, Cláudio Nahum Alves, and Jerônimo Lameira. "Unraveling the Addition–Elimination Mechanism of EPSP Synthase through Computer Modeling." Journal of Physical Chemistry B 121, no. 37 (September 8, 2017): 8626–37. http://dx.doi.org/10.1021/acs.jpcb.7b05063.

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20

Leo, Gregory C., James A. Sikorski, and R. Douglas Sammons. "Novel product from EPSP (5-enolpyruvoylshikimate 3-phosphate) synthase at equilibrium." Journal of the American Chemical Society 112, no. 4 (February 1990): 1653–54. http://dx.doi.org/10.1021/ja00160a068.

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21

Bakhsh, Allah, Tahira Hussain, Ilhom Rahamkulov, Ufuk Demirel, and Mehmet Emin Çalışkan. "Transgenic potato lines expressing CP4-EPSP synthase exhibit resistance against glyphosate." Plant Cell, Tissue and Organ Culture (PCTOC) 140, no. 1 (October 8, 2019): 23–34. http://dx.doi.org/10.1007/s11240-019-01708-1.

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22

Bartlett, Paul A., Uday Maitra, and Paul M. Chouinard. "Synthesis of "iso-EPSP" and evaluation of its interaction with chorismate synthase." Journal of the American Chemical Society 108, no. 25 (December 1986): 8068–71. http://dx.doi.org/10.1021/ja00285a031.

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23

Vaithanomsat, Pilanee, and Katherine A. Brown. "Isolation and mutation of recombinant EPSP synthase from pathogenic bacteria Pseudomonas aeruginosa." Process Biochemistry 42, no. 4 (April 2007): 592–98. http://dx.doi.org/10.1016/j.procbio.2006.11.006.

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24

XU, Junwang. "The first intron of rice EPSP synthase enhances expression of foreign gene." Science in China Series C 46, no. 6 (2003): 561. http://dx.doi.org/10.1360/02yc0120.

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25

Sikorski, James A., Mark L. Peterson, Susan D. Corey, Jose L. Font, and Mark C. Walker. "New 4-(α-Hetero-Phosphonomethyl) Pyrrole 2-Carboxylates are EPSP Synthase Inhibitors." Phosphorus, Sulfur, and Silicon and the Related Elements 144, no. 1 (January 1, 1999): 617–20. http://dx.doi.org/10.1080/10426509908546320.

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26

Arnaud, L., A. Sailland, M. Lebrun, K. Pallett, P. Ravanel, F. Nurit, and M. Tissut. "Physiological Behavior of Two Tobacco Lines Expressing EPSP Synthase Resistant to Glyphosate." Pesticide Biochemistry and Physiology 62, no. 1 (October 1998): 27–39. http://dx.doi.org/10.1006/pest.1998.2363.

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27

de Oliveira, Maycon D., Jéssica de O. Araújo, João M. P. Galúcio, Kauê Santana, and Anderson H. Lima. "Targeting shikimate pathway: In silico analysis of phosphoenolpyruvate derivatives as inhibitors of EPSP synthase and DAHP synthase." Journal of Molecular Graphics and Modelling 101 (December 2020): 107735. http://dx.doi.org/10.1016/j.jmgm.2020.107735.

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28

Shah, Ajit, Jose L. Font, Michael J. Miller, Joel E. Ream, Mark C. Walker, and James A. Sikorski. "New aromatic inhibitors of EPSP synthase incorporating hydroxymalonates as novel 3-phosphate replacements." Bioorganic & Medicinal Chemistry 5, no. 2 (February 1997): 323–34. http://dx.doi.org/10.1016/s0968-0896(96)00239-8.

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29

Anderson, Karen S., James A. Sikorski, and Kenneth A. Johnson. "A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics." Biochemistry 27, no. 19 (September 1988): 7395–406. http://dx.doi.org/10.1021/bi00419a034.

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30

Bartlett, Paul, Uday Maitra, and Paul Chouinard. "Correction. Synthesis of "Iso-EPSP" and Evaluation of Its Interaction with Chorismate Synthase." Journal of the American Chemical Society 109, no. 9 (April 1987): 2861. http://dx.doi.org/10.1021/ja00243a606.

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31

Sikorski, James A., Douglas R. Sammons, Kenneth J. Gruys, and Mark C. Walker. "Insights from 31P NMR Studies of Substrate and Inhibitor Complexes with EPSP Synthase." Phosphorus, Sulfur, and Silicon and the Related Elements 144, no. 1 (January 1, 1999): 293–96. http://dx.doi.org/10.1080/10426509908546239.

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32

Vicini, John L., William R. Reeves, John T. Swarthout, and Katherine A. Karberg. "Glyphosate in livestock: feed residues and animal health1." Journal of Animal Science 97, no. 11 (September 9, 2019): 4509–18. http://dx.doi.org/10.1093/jas/skz295.

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Abstract Glyphosate is a nonselective systemic herbicide used in agriculture since 1974. It inhibits 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase, an enzyme in the shikimate pathway present in cells of plants and some microorganisms but not human or other animal cells. Glyphosate-tolerant crops have been commercialized for more than 20 yr using a transgene from a resistant bacterial EPSP synthase that renders the crops insensitive to glyphosate. Much of the forage or grain from these crops are consumed by farm animals. Glyphosate protects crop yields, lowers the cost of feed production, and reduces CO2 emissions attributable to agriculture by reducing tillage and fuel usage. Despite these benefits and even though global regulatory agencies continue to reaffirm its safety, the public hears conflicting information about glyphosate's safety. The U.S. Environmental Protection Agency determines for every agricultural chemical a maximum daily allowable human exposure (called the reference dose, RfD). The RfD is based on amounts that are 1/100th (for sensitive populations) to 1/1,000th (for children) the no observed adverse effects level (NOAEL) identified through a comprehensive battery of animal toxicology studies. Recent surveys for residues have indicated that amounts of glyphosate in food/feed are at or below established tolerances and actual intakes for humans or livestock are much lower than these conservative exposure limits. While the EPSP synthase of some bacteria is sensitive to glyphosate, in vivo or in vitro dynamic culture systems with mixed bacteria and media that resembles rumen digesta have not demonstrated an impact on microbial function from adding glyphosate. Moreover, one chemical characteristic of glyphosate cited as a reason for concern is that it is a tridentate chelating ligand for divalent and trivalent metals; however, other more potent chelators are ubiquitous in livestock diets, such as certain amino acids. Regulatory testing identifies potential hazards, but risks of these hazards need to be evaluated in the context of realistic exposures and conditions. Conclusions about safety should be based on empirical results within the limitations of model systems or experimental design. This review summarizes how pesticide residues, particularly glyphosate, in food and feed are quantified, and how their safety is determined by regulatory agencies to establish safe use levels.

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33

Anderson, Karen S., James A. Sikorski, Alan J. Benesi, and Kenneth A. Johnson. "Isolation and structural elucidation of the tetrahedral intermediate in the EPSP synthase enzymic pathway." Journal of the American Chemical Society 110, no. 19 (September 1988): 6577–79. http://dx.doi.org/10.1021/ja00227a056.

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34

Sikorski, James A., Michael J. Miller, Diane S. Braccolino, Darryl G. Cleary, Susan D. Corey, Jose' L. Font, Kenneth J. Gruys, et al. "EPSP Synthase: The Design and Synthesis of Bisubstrate Inhibitors Incorporating Novel 3-Phosphate Mimics." Phosphorus, Sulfur, and Silicon and the Related Elements 76, no. 1-4 (March 1993): 115–18. http://dx.doi.org/10.1080/10426509308032372.

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35

Sikorski, James A., Mark L. Peterson, Susan D. Corey, Jose L. Font, and Mark C. Walker. "ChemInform Abstract: New 4-(α-Hetero-phosphonomethyl)pyrrole 2-Carboxylates Are EPSP Synthase Inhibitors." ChemInform 31, no. 9 (June 10, 2010): no. http://dx.doi.org/10.1002/chin.200009274.

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36

Gribkoff, V. K., and J. T. Lum-Ragan. "Evidence for nitric oxide synthase inhibitor-sensitive and insensitive hippocampal synaptic potentiation." Journal of Neurophysiology 68, no. 2 (August 1, 1992): 639–42. http://dx.doi.org/10.1152/jn.1992.68.2.639.

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1. Nitric oxide (NO) has been proposed as a retrograde messenger, mediating the postsynaptic to presynaptic transfer of the effects of conditioning stimulation, responsible for the initiation of hippocampal long-term potentiation (LTP). To further test this hypothesis, we inhibited nitric oxide synthase (NOS) to determine whether synaptic potentiation produced by different conditioning stimulus patterns and intensities was differentially affected by reduction of stimulation-dependent NO production. 2. Synaptic potentiation was produced in hippocampal slices from young F-344 rats by two different conditioning stimulation protocols. Conditioning stimuli were delivered to the Schaffer-collateral commissural system, and moderate levels of potentiation of the population excitatory postsynaptic potential (EPSP) in area CA1 were produced by a single 100 Hz, 1-s conditioning train delivered at half-maximal stimulus intensity. Higher levels of potentiation of the population EPSP were obtained by delivering two 100 Hz, 1-s conditioning stimulus trains, with a 60-s intertrain interval, at high stimulus currents. 3. Application of the nitric oxide synthase inhibitors NG-nitro-L-arginine (NOARG; 0.1-200 microM) and NG-monomethyl-L-arginine (NMMA; 100 microM) produced no significant direct effects on synaptic responses. 4. In slices that received a single conditioning stimulus train, both NOARG and NMMA were ineffective in blocking or reducing potentiation at concentrations between 0.1 and 200 microM. In slices receiving the more intense pair of conditioning stimulus trains, levels of potentiation in control slices were higher, and there was a very significant reduction by both NOARG (50 and 100 microM) and NMMA (100 microM).(ABSTRACT TRUNCATED AT 250 WORDS)

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37

Gruys, Kenneth J., Mark C. Walker, and James A. Sikorski. "Substrate synergism and the steady-state kinetic reaction mechanism for EPSP synthase from Escherichia coli." Biochemistry 31, no. 24 (June 1992): 5534–44. http://dx.doi.org/10.1021/bi00139a016.

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38

Marzabadi, Mohammad R., Kenneth J. Gruys, Paul D. Pansegrau, Mark C. Walker, Henry K. Yuen, and James A. Sikorski. "An EPSP Synthase Inhibitor Joining Shikimate 3-Phosphate with Glyphosate: Synthesis and Ligand Binding Studies." Biochemistry 35, no. 13 (January 1996): 4199–210. http://dx.doi.org/10.1021/bi9521349.

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39

Sikorski, James A., and Kenneth J. Gruys. "Understanding Glyphosate's Molecular Mode of Action with EPSP Synthase: Evidence Favoring an Allosteric Inhibitor Model." Accounts of Chemical Research 30, no. 1 (January 1997): 2–8. http://dx.doi.org/10.1021/ar950122.

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40

Kahrizi, Danial. "Reduction of EPSP synthase in transgenic wild turnip (Brassica rapa) weed via suppression of aroA." Molecular Biology Reports 41, no. 12 (September 5, 2014): 8177–84. http://dx.doi.org/10.1007/s11033-014-3718-0.

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41

Cross, Robert B., Lambert B. McCarty, Nishanth Tharayil, J. Scott McElroy, Shu Chen, Patrick E. McCullough, Brian A. Powell, and William C. Bridges. "A Pro106to Ala Substitution is Associated with Resistance to Glyphosate in Annual Bluegrass (Poa annua)." Weed Science 63, no. 3 (September 2015): 613–22. http://dx.doi.org/10.1614/ws-d-15-00033.1.

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Glyphosate is used in the transition zone to control annual bluegrass in fully dormant warm-season grasses. A suspected resistant (R) biotype of annual bluegrass was identified on a golf course in South Carolina after at least 10 consecutive years of glyphosate application. Greenhouse bioassays revealed the R biotype was 4.4-fold resistant to glyphosate compared with a standard susceptible (S) biotype. Further studies were conducted to investigate the mechanism conferring glyphosate resistance in the R biotype. Leaf discs of both biotypes accumulated shikimate in response to increasing glyphosate concentration, but the glyphosate concentration resulting in 50% EPSP synthase inhibition as a result of shikimate accumulation (I50) was 4.2-fold higher in the R biotype compared with the S biotype. At the whole plant level, similar levels of shikimate accumulation were observed between biotypes at 6 and 24 h after treatment (HAT) with glyphosate, but greater shikimate accumulation occurred in the S biotype at 72, 120, and 168 HAT. Shikimate levels decreased in the R biotype after 72 HAT. There were no differences in14C-glyphosate absorption between biotypes. However, more14C-glyphosate translocated out of the treated leaf in the R biotype and into root tissues over time compared with the S biotype. Partial sequencing of the EPSP synthase gene revealed a point mutation that resulted in an Ala substitution at Pro106. Although other mechanisms may contribute to glyphosate resistance, these results confirm a Pro106to Ala substitution is associated with resistance to glyphosate in the R annual bluegrass biotype.

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42

Corey, Susan D., Paul D. Pansegrau, Mark C. Walker, and James A. Sikorski. "EPSP synthase inhibitor deisgn III. Synthesis & evaluation of a new 5-oxamic acid analog of EPSP which incorporates a malonate ether as a 3-phosphate mimic." Bioorganic & Medicinal Chemistry Letters 3, no. 12 (December 1993): 2857–62. http://dx.doi.org/10.1016/s0960-894x(01)80779-4.

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43

SIKORSKI, J. A., M. J. MILLER, D. S. BRACCOLINO, D. G. CLEARY, S. D. COREY, J. L. FONT, K. J. GRUYS, et al. "ChemInform Abstract: EPSP Synthase: The Design and Synthesis of Bisubstrate Inhibitors Incorporating Novel 3-Phosphate Mimics." ChemInform 24, no. 35 (August 31, 2010): no. http://dx.doi.org/10.1002/chin.199335301.

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44

Donahue, Raymon A., Tim D. Davis, Charles H. Michler, Don E. Riemenschneider, Doug R. Carter, Paula E. Marquardt, Narendra Sankhla, Daksha Sankhla, Bruce E. Haissig, and J. G. Isebrands. "Growth, photosynthesis, and herbicide tolerance of genetically modified hybrid poplar." Canadian Journal of Forest Research 24, no. 12 (December 1, 1994): 2377–83. http://dx.doi.org/10.1139/x94-306.

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Hybrid poplar clone NC–5339 (Populusalba × Populusgrandidentata cv. Crandon) was genetically modified for glyphosate (N-(phosphonomethyl)glycine) tolerance by Agrobacterium-mediated transformation with genetic constructs (pPMG 85/587 and pCGN 1107) that included the mutant aroA gene for 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase (EC 2.5.1.19) and the neomycin phosphotransferase selectable marker gene. pCGN 1107 also harbored the coding sequence for a chloroplast transit peptide and the CaMV 35S promoter fused to the mutant aroA gene. Transformants were selected for kanamycin tolerance, and integration of the aroA gene was verified by Southern blot analysis. Cuttings of NC-5339 and the derived transformants were rooted and grown in glasshouses at separate locations, with maximum photosynthetic photon flux density of 1600 and 750 μmol•m−2•s−1. Productivity was assessed by growth studies and photosynthesis measurements at both locations. Glyphosate tolerance was tested by (i) measurement of chlorophyll concentration in herbicide-treated leaf discs and (ii) whole-plant spray tests. Plants transformed with construct pCGN 1107 were the most herbicide tolerant. Perhaps high-level expression of the aroA gene by the CaMV 35S promoter, transport of mutant EPSP synthase into the chloroplasts, or both facilitated glyphosate tolerance. Plants grown at higher photosynthetic photon flux densities (1600 vs. 750 μmol•m−2•s−1) had significantly higher maximum net photosynthesis (19.8 vs. 16.2 μmol•m−2•s−1) and more biomass accumulation (47.6 vs. 33.7 g). However, there were no significant differences between NC-5339 and transformants within location for net photosynthesis or any growth parameter. Genetic modification of hybrid poplar NC-5339 for glyphosate tolerance did not adversely affect plant productivity at either location.

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Miller, Michael J., Diane S. Braccolino, Darryl G. Clearly, Joel E. Ream, Mark C. Walker, and James A. Sikorski. "EPSP synthase inhibitor design IV. New aromatic substrate analogs and symmetrical inhibitors containing novel 3-phosphate mimics." Bioorganic & Medicinal Chemistry Letters 4, no. 21 (November 1994): 2605–8. http://dx.doi.org/10.1016/s0960-894x(01)80293-6.

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Knowles, William S., Karen S. Anderson, Steven S. Andrew, Dennis P. Phillion, Joel E. Ream, Kenneth A. Johnson, and James A. Sikorski. "Synthesis & characterization of N-amino-glyphosate as a potent analog inhibitor of E. coli EPSP synthase." Bioorganic & Medicinal Chemistry Letters 3, no. 12 (December 1993): 2863–68. http://dx.doi.org/10.1016/s0960-894x(01)80780-0.

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Anderson, Karen S., R. Douglas Sammons, Gregory C. Leo, James A. Sikorski, Alan J. Benesi, and Kenneth A. Johnson. "Observation by carbon-13 NMR of the EPSP synthase tetrahedral intermediate bound to the enzyme active site." Biochemistry 29, no. 6 (February 1990): 1460–65. http://dx.doi.org/10.1021/bi00458a017.

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Shuttleworth, Wendy A., and Jeremy N. S. Evans. "Site-Directed Mutagenesis and NMR Studies of Histidine 385 Mutants of 5-Enolpyruvylshikimate-3-phosphate (EPSP) Synthase." Biochemistry 33, no. 23 (June 1994): 7062–68. http://dx.doi.org/10.1021/bi00189a007.

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Wibbenmeyer, Jamie, Lorna Brundage, Stephen R. Padgette, John J. Likos, and Ganesh M. Kishore. "Mechanism of the EPSP synthase catalyzed reaction: Evidence for the lack of a covalent carboxyvinyl intermediate in catalysis." Biochemical and Biophysical Research Communications 153, no. 2 (June 1988): 760–66. http://dx.doi.org/10.1016/s0006-291x(88)81160-4.

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SIKORSKI, J. A., and K. J. GRUYS. "ChemInform Abstract: Understanding Glyphosate′s Molecular Mode of Action with EPSP Synthase: Evidence Favoring an Allosteric Inhibitor Model." ChemInform 28, no. 19 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199719303.

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