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Enzyme
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=== Allosteric modulation === {{main|Allosteric regulation}} Allosteric sites are pockets on the enzyme, distinct from the active site, that bind to molecules in the cellular environment. These molecules then cause a change in the conformation or dynamics of the enzyme that is transduced to the active site and thus affects the reaction rate of the enzyme.<ref>{{cite journal | vauthors = Tsai CJ, Del Sol A, Nussinov R | title = Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms | journal = Molecular BioSystems | volume = 5 | issue = 3 | pages = 207β216 | date = March 2009 | pmid = 19225609 | pmc = 2898650 | doi = 10.1039/b819720b }}</ref> In this way, allosteric interactions can either inhibit or activate enzymes. Allosteric interactions with metabolites upstream or downstream in an enzyme's metabolic pathway cause [[feedback]] regulation, altering the activity of the enzyme according to the [[Flux (metabolism)|flux]] through the rest of the pathway.<ref>{{cite journal | vauthors = Changeux JP, Edelstein SJ | title = Allosteric mechanisms of signal transduction | journal = Science | volume = 308 | issue = 5727 | pages = 1424β1428 | date = June 2005 | pmid = 15933191 | doi = 10.1126/science.1108595 | s2cid = 10621930 | bibcode = 2005Sci...308.1424C }}</ref>
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