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Free energies and equilibria of peptide bond hydrolysis and formation.
Abstract
The utility of the average Boltzmann factor around the active site of an enzyme as the predictor of the electrostatic enhancement of the substrate binding rate is tested on a set of data on wild-type acetylcholinesterase and 18 charge mutants recently obtained by Brownian dynamics simulations. A good correlation between the average Boltzmann factors and the substrate binding rate constants is found. The effects of single charge mutations on both the Boltzmann factor and the substrate binding rate constant are modest, i.e., < 5 fold increase or decrease. This is consistent with the experimental results of Shafferman et al. but does not support their suggestion that the overall rate of the catalytic reaction is not limited by the diffusional encounter of acetylcholinesterase and its substrate.
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“Hydrolyzing peptides inside the cell might allow the bacterium to capture the energy released by the hydrolysis, and for the longer peptides, this might result in a net gain of energy as the energy released can exceed the energy required to re-phosphorylate two moles of ATP (Martin, 1998; Bergman et al., 2010).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Martin, 1998
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- Authors
- Martin, R. B.
- Venue
- Biopolymers
- Published
- 1998
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- Martin, R. B. (1998). Free energies and equilibria of peptide bond hydrolysis and formation. Biopolymers. https://doi.org/10.1002/(sici)1097-0282(19980415)45%3A5
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