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Pyruvate-phosphate dikinase (PPDK) was targeted for inhibitor design because of its central role in C 4 -type photosynthetic carbon metabolism and its relative absence in C 3 -type plants and organisms of the animal kingdom. Compounds were tested for their activities as reversible and irreversible inhibitors of PPDK isolated from maize. The relative activity of the test compounds against phosphoenolpvruvate carboxylase (PEPCase), isolated from wheat, was used as a measure of the specificity of the inhibitors for the targeted enzyme. PPDK. An ideal compound for successful herbicide design should be an inhibitor which is specific toward the targeted enzyme and either effectively inhibits enzyme activity at very low concentrations or inactivates the enzyme through an irreversible mechanism. Using results obtained with commercially purchased compounds. the discussion will emphasize the difficulty of obtaining specific inhibitors toward PPDK. Another report from this laboratory (A. L. Lawyer. S. R. Kelley, and J. I. Allen, in: Proc. Seventh Internat. Congr. Photosynth. (J. Biggins, ed.), in press) emphasizes other results obtained from the targeting of PPDK for herbicide activity.

Use of Pyruvate-Phosphate Dikinase as a Target for Herbicide Design: Analysis of Inhibitor Specificity