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Kinetic and Magnetic Resonance Studies of the Pyruvate Kinase Reaction
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SUMMARY A correlation between the kinetics of the pyruvate kinase reaction and the enhancements of the relaxation rate of the nuclear spins of water protons in the ternary enzyme-manganese-substrate (E-Mn-S) complexes, et, has revealed certain salient features of the pathway of the reaction and the structure of the ternary intermediates. The rate equation for initial velocities of the forward reaction was derived by assuming (a) rapid simultaneous equilibria of enzyme with divalent metal ion, adenosine diphosphate, manganese adenosine diphosphate, and phosphoenolpyruvate, (b) random order of combination, and (c) phosphoryl transfer as the rate-determining step. This formulation permitted the calculation of the dissociation constants KS of the ES complexes and KB of the EiWS complexes for ADP and phosphoenolpyruvate. The values of KS for E-Mn-ADP and E-Mn-phosphoenolpyruvate were determined directly by equilibrium experiments with proton relaxation rate (PRR) with the use of et as the parameter which characterized the ternary complexes. The values of KS for E-phosphoenolpyruvate and E-ADP were determined directly by equilibrium experiments
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Kinetic and Magnetic Resonance Studies of the Pyruvate Kinase Reaction
Mildvan, A. S., & Cohn, M. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96818-3 · Cited by 282
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Metadata
- Authors
- Mildvan, A. S., & Cohn, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1965-01
- Volume
- 240
- Issue
- 1
- Pages
- 238-246
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W49918647
- Cited by
- 200
- References
- 0
- FWCI
- 10.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
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