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dc.contributor.authorBanerjee, Kinshuk
Kolomeisky, Anatoly B.
Igoshin, Oleg A.
dc.date.accessioned 2017-08-02T14:52:15Z
dc.date.available 2017-08-02T14:52:15Z
dc.date.issued 2017
dc.identifier.citation Banerjee, Kinshuk, Kolomeisky, Anatoly B. and Igoshin, Oleg A.. "Accuracy of Substrate Selection by Enzymes Is Controlled by Kinetic Discrimination." The Journal of Physical Chemistry Letters, 8, no. 7 (2017) American Chemical Society: 1552-1556. https://doi.org/10.1021/acs.jpclett.7b00441.
dc.identifier.urihttps://hdl.handle.net/1911/96170
dc.description.abstract Enzymes have the remarkable ability to select the correct substrate from the pool of chemically similar molecules. The accuracy of such a selection is determined by differences in the free-energy profiles for the right and wrong reaction pathways. Here, we investigate which features of the free-energy landscape govern the variation and minimization of selectivity error. It is generally believed that minimal error is affected by both kinetic (activation barrier heights) and thermodynamic (binding stability) factors. In contrast, using first-passage theoretical analysis, we show that the steady-state selectivity error is determined only by the differences in transition-state energies between the pathways and is independent of the energies of the stable complexes. The results are illustrated for two common catalytic mechanisms: (i) the Michaelis–Menten scheme and (ii) an error-correcting kinetic proofreading scheme with tRNA selection and DNA replication as guiding biological examples. Our theoretical analysis therefore suggests that the selectivity mechanisms are always kinetically controlled.
dc.language.iso eng
dc.publisher American Chemical Society
dc.rights This is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by the American Chemical Society.
dc.title Accuracy of Substrate Selection by Enzymes Is Controlled by Kinetic Discrimination
dc.type Journal article
dc.citation.journalTitle The Journal of Physical Chemistry Letters
dc.contributor.org Center for Theoretical Biological Physics
dc.citation.volumeNumber 8
dc.citation.issueNumber 7
dc.identifier.digital kinetic-regulation-enzymatic
dc.type.dcmi Text
dc.identifier.doihttps://doi.org/10.1021/acs.jpclett.7b00441
dc.identifier.pmid 28322561
dc.type.publication post-print
dc.citation.firstpage 1552
dc.citation.lastpage 1556


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