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Structural requirements for pep binding To EPSP synthase |
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| Authors: | Mark C. Walker Joel E. Ream R. Douglas Sammons Eugene W. Logusch Marion H. O'Leary Ronald L. Somerville James A. Sikorski |
| Affiliation: | a New Products Division, Monsanto Agricultural Company, 800 N. Lindbergh Blvd., St. Louis, Missouri 63167 U.S.A. b Center for Biological Chemistry, University of Nebraska, Lincoln, Nebraska 68583 U.S.A. c Department of Biochemistry, Purdue University West Lafayette, Indiana 47907 U.S.A. |
| Abstract: | Evaluation of structural analogs of PEP as inhibitors ESPS synthase demonstrate that this enzyme displays a high degree of structural and ionic specificity for PEP binding. Both carboxyallenyl phosphate (1) and (Z)-3-fluoro-PEP (5) were surprisingly potent EPSP sythase inhibitors. |
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