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EK. J. Wilson, W. Birchmeier, and P. Christen, Eur. J. Biochem. 41, 471 (1974). < 0 Z ~ o ¢; ~a <'-. ©~,, ~ ~N + ° o o • °~ 44 GENERAL METHODOLOGY ~] enzyme the rate of modification of Cys-390 is at a minimum. The rate increases as the enzyme passes through the consecutive enzyme-substrate intermediates and decreases again when the free pyridoxamine form is reached. The rate of Cys-390 modification is fastest when, in the presence of a substrate pair (glutamate plus 2-ketoglutarate or aspartate plus oxaloacetate), covalent enzyme-substrate intermediates are formed.
Chem. 234, 2517 (1958). ~R dehydrogenase ] H~,.. e. o. o- -ope| hh (CH2)2 NH~--C--COOH H a j. Everse, E. C. Zoll, L. Kahan, and N. O. Kaplan, Bioorg. Chem. 1, 207 (1971). b W. B. Noroa, A. D. Winer, A. J. Glaid, and G. W. Schwert, J. Biol. Chem. 234, 1143 (1959). c E. Racker, V. Klybas, and M. Schramm, J. Biol. Chem. 234, 2510 (1958). d A. L. Fluharty and C. E. Ballou, J. Biol. Chem. 234, 2517 (1958). • D. Northrop and H. G. Wood, J. Biol. Chem. 244, 5810 (1969). s G. H. Reed and S. D. Morgan, Biochemistry 13, 3537 (1974).
Chem. 250, 7120 (1975). ~*K. A. Koehler and G. E. Lienhard, Biochemistry 10, 2477 (1971). de inhibitors that may form adducts resembling tetrahedral intermediates in substrate hydrolysis, vary markedly but in parallel as the structure of the substrate (or inhibitor) is varied at points distant from the scissile bondJ ~ Cases of this kind are especially interesting in that they seem to imply the occurrence of conformation changes in the enzyme and/or the substrate during the catalytic process. In principle, such changes can be examined directly with transition-state analogs, using exact structural methods to compare atomic coordinates in complexes corresponding to various stages in the catalytic process.