Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27070509
&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215
Statistical Mechanics of Allosteric Enzymes
#MMPMID27070509
Einav T
; Mazutis L
; Phillips R
J Phys Chem B
2016[Jul]; 120
(26
): 6021-37
PMID27070509
show ga
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.