Abstract:
:Theory for enzyme-catalyzed reactions is developed for the dependence on product concentration of deuterium isotope effects on V and V/K. Generally, a product that decreases the off-rate for a second product to zero causes the isotope effect on V/K to decrease to DKeq and that on V to decrease to a value between 1 and DKeq. If the second product off-rate is decreased to a finite value, DV and D(V/K) will decrease to a value greater than DKeq, while if there is no effect on the off-rate for the second product, DV and D(V/K) will not change. Interestingly, for a ping-pong mechanism, the presence of the product that provides a reversible connection between the isotope-sensitive step and the isotope-insensitive half-reaction will give an isotope effect on V/K for the latter. (In the absence of the product, the isotope effect on V/K for the isotope-insensitive half-reaction will be unity.) Theory is supported with data for alcohol and lactate dehydrogenases. For lactate dehydrogenase, D(V/Kpyruvate) decreases from 1.93 +/- 0.02 at zero to 1.16 +/- 0.02 at infinite lactate concentration, while DV decreases from a value of 1.75 +/- 0.03 at zero to a value of 0.93 +/- 0.05 at infinite lactate concentration. Thus, it appears that the pathway in which lactate is released first is greatly preferred, but the pathway in which NAD+ is released before lactate is observed at high lactate concentration.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Biochemistryjournal_title
Biochemistryauthors
Cook PF,Yoon MY,Hara S,McClure GD Jrdoi
10.1021/bi00058a013subject
Has Abstractpub_date
1993-02-23 00:00:00pages
1795-802issue
7eissn
0006-2960issn
1520-4995journal_volume
32pub_type
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