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They also form stable, reversible compounds with dehydrogenases. An oxidation reduction reaction between a dehydrogenase (excluding those with flavin prosthetic groups) and a coenzyme, in the complete absence of the other substrate, has never been demonstrated. There is no reliable evidence, therefore, for an enzyme-substitution (ping-pong) mechanism; indeed, for many dehydrogenases this mechanism has been excluded simply by the results of initial rate measurements. It is reasonable to suppose that the enzyme-coenzyme compounds are intermediates in the overall catalytic reaction.
Chim. Biol. 49, 1563 (1967). K. Dalziel and F. M. Dickinson, BJ 100, 34 (1966). 1. 13 KINETICS AND MECHANISM tive substrate B were used, since 4 . ~is a function of ka, k--4, k , and k’ as well as kl. The relations in Eq. (8) should hold, however. This mechanism in which reactant coenzyme may “leak” from the ternary complex was first suggested for liver alcohol dehydrogenase to reconcile the results of initial rate studies with primary and secondary alcohols as substrates and isotope exchange experiments (39),and it has also been proposed for yeast alcohol dehydrogenase (40) and a-glycerophosphate dehydrogenase from rabbit muscle (41).
Wolfe, Biochemistry 1, 1112 (1962). 55. M. Caasman and S. Englard, JBC 241, 787 and 793 (1966). 56. A. D. Winer and G. W. Schwert, JBC 231,1065 (1958). 57. G. W. Schwert, B. R. Miller, and R. J. Peanasky, JBC 242, 3245 (1967). 58. V. Zewe and H. J. Fromm, JBC 237, 1668 (1962). 59. V. Zewe and H. J. Fromm, Biochemistry 4, 782 (1965). TABLE 111 TESTSO F MAXIMUM RATERELATIONS [EQ. O 7. 8 +p~'$o Ref. o 54 55 41 56,57 58,59 a The original data have been corrected, where necessary, to express the rates as moles substrate per mole enzyme active center.