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E. , Biochem. , in press. ~sK. D. Collins, J. Biol. Chem. 49, 136 (1974). ~"G. E. Lienhard and I. I. Secemski, J. Biol. Chem. 248, 1121 (1973). 28 Although binding ratios as large as 105-106 are found in some cases, it should be emphasized that true Ks values are not often known for productive ES complexes, and may be higher or lower than the observed K~ values on which the apparent binding ratios are based. In addition, it seems probable that calculations according to expressions such as Scheme 2 provide only an upper limiting value for KTx, in the likely event that the enzymic and nonenzymic reactions differ in the detailed structure of the altered substrate in the transition state2 Affinity Labeling with Transition State Analogs The possibility of combining the features of a transition state analog with those of an affinity labeling agent remains to be explored in detail, but it appears to have been realized unexpectedly in two cases.

Spoonhower, and R. Cookingham, Science 189, 384 (1975). 13D. A. Matthews, R. A. Alden, J. J. Birktoft, S. T. Freer, and J. Kraut, J. Biol. 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.

J. M. Manning, N. E. Merrifield, W. M. Jones, and E. C. Gotschlich, Proc. Natl. Acad. Sci. A. 71, 417 (1974). ~0L. J. Fowler and R. A. John, Biochem. J. 130, 569 (1972). 2, R. A. John and P. Fasella, Biochemistry 8, 4477 (1969). = P. Fasella, in "Pyridoxal Catalysis: Enzymes and Model Systems" (E. ), p. 1. Wiley, New York, 1968. 25C. T. Walsh, A. Schonbrunn, and R. H. Abeles, J. Biol. Chem. 246, 6855 (1971). ,/'~-NI-I+~ ~] /Cl cis- 3-Chloroallylamine 2-Chloroallylamine flavin-linked monoamine oxidase and 2-chloroallylamine is an irreversible inhibit~r and nonflavin-linked monoamine oxidase.

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