The fundamental chemistry and mechanistic enzymology of methyl transfer processes will be studied with a view to determining individual transition-state structures and to developing predictive generalizations about such structures. The data should be useful in the design of transition-state analog enzyme inhibitors as drugs, which will affect the metabolism of catecholamines and other compounds. BIBLIOGRAPHIC REFERENCES: N. I. Nakano, M. Kise, E. E. Smissman, K. Widiger and R. L. Schowen, Transition-State Structure and Reactivity in the Acid-Base Catalyzed Hydrolysis of a Model Intermediate for Corn-Plant Herbicide Resistance, J. Org. Chem., 40, 2215 (1975); J. P. Elrod, R. D. Gandour, J. L. Hogg, M. Kise, G. M. Maggiora, R. L. Schowen and K. S. Venkatasubban, Proton Bridges in Enzyme Catalysis, Faraday Symposium No. 10, Stirling, Scotland, 8-10 Sept. 1975.