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M for the catalyst-first substrate complex in the presence or absence of complexed other substrate. α =1 means no dependence. See Segel, I.H.; Enzyme Kinetics; John Wiley & Sons, New York, 1975, pp 273-283.
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note
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2O, detection by UV at 250 nm).
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36
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0039495743
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note
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R(11) = 15.2 min and 19.2 min. The enantioselectivity is corrected for the racemic background reaction.
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0024298964
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Here we cite a paragraph on the issue of substrate binding in enzymatic catalysis: "Why is there a Michaelis-Menten complex? The existence of an ES complex is postulated to account for the phenomenon of substrate saturation in steady-state kinetics." And later: "Probably the ES complex represents binding of a Boltzmann distribution of substrate molecules in states preceding the transition-state bottleneck. That these bound states are well populated may be due simply to the inevitable fact that the transition-state of the usual substrate molecule does not look very different from its ground state."
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Kraut, J. Science 1988, 242, 533. Here we cite a paragraph on the issue of substrate binding in enzymatic catalysis: "Why is there a Michaelis-Menten complex? The existence of an ES complex is postulated to account for the phenomenon of substrate saturation in steady-state kinetics." And later: "Probably the ES complex represents binding of a Boltzmann distribution of substrate molecules in states preceding the transition-state bottleneck. That these bound states are well populated may be due simply to the inevitable fact that the transition-state of the usual substrate molecule does not look very different from its ground state."
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Science
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Kraut, J.1
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42
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0029018511
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uncat. This leads to a classification of all catalyzed reactions as either uni-or bimolecular, so that higher-order processes like those discussed here cannot be analyzed
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uncat. This leads to a classification of all catalyzed reactions as either uni-or bimolecular, so that higher-order processes like those discussed here cannot be analyzed.
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Nature
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Stewart, J.D.1
Benkovic, S.J.2
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