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Addition/Correction Cite This: ACS Omega 2018, 3, 8483−8483
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Correction to Effect of Substrate Number Fluctuations in Stochastic Enzyme Kinetics Divya Singh and Srabanti Chaudhury* ACS Omega 2018, 3 (5), 5574−5583. DOI: 10.1021/acsomega.8b00611
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few references were not included in the original publication. Grima, R. Investigating the robustness of the classical enzyme kinetic equations in small intracellular compartments. BMC Systems Biology 2009, 3, 101. Grima, R. Noise-Induced Breakdown of the Michaelis− Menten Equation in Steady-State Conditions. Phys. Rev. Lett. 2009, 102, 218103. Schnoerr, D.; Sanguinetti, G.; Grima, R. The complex chemical Langevin equation. J. Chem. Phys. 2014, 141, 024103. Also we would like to add a few points in our Conclusion section: Schnoerr et al. have derived an exact solution of the chemical master equation for the enzyme reaction system (Appendix G in J. Chem. Phys. 2014, 141, 024103) described by Figure 1 (a) in our manuscript. They have used the mathematical formulation as shown by Stefanini et al. (ref 17 in our original paper) to calculate the average number of substrate molecules and the variance in fluctuations in the average. In our work we have used the same mathematical method to obtain the reaction velocity and the variance. But we apply this theoretical approach not only for the scheme described in Figure 1 (a) but also for other catalytic reaction schemes that involve both substrate input and output from the intracellular compartment as well as reaction schemes with multiple intermediate states. In ref 17 the deviation from the MM equation was shown only for a simple catalytic reaction with substrate input (Figure 1(a)). In our work, we have extended this approach to a few more reaction schemes and also discussed the conditions where one can get back the MM like equation. We also study the coefficient of variation, which is a measure of the noise strength as a function of the mean substrate concentration for such reaction schemes where there is influx or/and outflux of substrate molecules. From our calculations, we compare the noise strength for both unidirectional and bidirectional transport of substrate molecules. We also compare the level of noise for enzymatic schemes with one and two intermediate states. The authors apologize for overlooking these references in the original paper.
Received: July 6, 2018 Published: August 1, 2018 © 2018 American Chemical Society
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DOI: 10.1021/acsomega.8b01556 ACS Omega 2018, 3, 8483−8483