| Literature DB >> 27070509 |
Tal Einav1, Linas Mazutis2, Rob Phillips3.
Abstract
The concept of allostery in which macromolecules switch between two different conformations is a central theme in biological processes ranging from gene regulation to cell signaling to enzymology. Allosteric enzymes pervade metabolic processes, yet a simple and unified treatment of the effects of allostery in enzymes has been lacking. In this work, we take a step toward this goal by modeling allosteric enzymes and their interaction with two key molecular players-allosteric regulators and competitive inhibitors. We then apply this model to characterize existing data on enzyme activity, comment on how enzyme parameters (such as substrate binding affinity) can be experimentally tuned, and make novel predictions on how to control phenomena such as substrate inhibition.Entities:
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Year: 2016 PMID: 27070509 PMCID: PMC5452729 DOI: 10.1021/acs.jpcb.6b01911
Source DB: PubMed Journal: J Phys Chem B ISSN: 1520-5207 Impact factor: 2.991