Bon Lester L.

Lamparero BS ChE-IV
2, 2016
ChE 171 Introduction to Biochemical Engineering

March

Allosteric Regulation
Enzymes are not only important in digestion, but many other bodily and cellular functions as well, like
respiration. Therefore, it's also important that they are properly regulated. An unregulated enzyme may make too much
of something or nothing at all, both of which cases can have profound effects on how your body performs.. There are
many processes occurring inside the cell at any one time, and they must coexist in proper balance. This balance is where
allosteric enzymes come into play.
Every enzyme contains an active site, the location on the enzyme where it catalyses its specific reaction. Allosteric
enzymes contain a second type of site, called an allosteric site. The allosteric site, through its binding of a nonsubstrate
molecule, influences (enhances or impairs) the activity of the enzyme. The word "allosteric" is derived from two Greek
words: allos, meaning other, and stereos, meaning site. Another important feature of allosteric enzymes is that they consist
of multiple polypeptide chains, with multiple active and allosteric sites.
Allosteric enzyme regulation therefore is when a molecule binds a site other than the active site and changes the
behavior of the enzyme by changing its conformation. Instead of binding a substrate, an allosteric site binds another
molecule that affects the enzyme's regulation. When a molecule binds an allosteric site, it alters the enzyme's shape, or
conformation, which then changes how the enzyme functions.

Allosteric inhibitors and activators

Allosteric inhibitors modify the active site of the enzyme so that substrate binding is reduced or prevented. In

In noncompetitive allosteric inhibition, inhibitor molecules bind to an enzyme at the allosteric site. Their binding
induces a conformational change that reduces the affinity of the enzyme's active site for its substrate. The binding of this
allosteric inhibitor changes the conformation of the enzyme and its active site, so the substrate is not able to bind. This
prevents the enzyme from lowering the activation energy of the reaction, and the reaction rate is reduced.

However, allosteric inhibitors are not the only molecules that bind to allosteric sites. Allosteric activators can
increase reaction rates. They bind to an allosteric site which induces a conformational change that increases the affinity of
the enzyme's active site for its substrate. This increases the reaction rate.
Sources:
Boundless. Control of Metabolism Through Enzyme Regulation. Boundless Biology. Boundless, 25 Jan. 2016. Retrieved
02 Mar. 2016 from https://www.boundless.com/biology/textbooks/boundless-biology-textbook/metabolism6/enzymes-72/control-of-metabolism-through-enzyme-regulation-351-11577/
Chemistryexplained.com,. (2016). Allosteric Enzymes - Chemistry Encyclopedia - reaction, proteins, molecule. Retrieved 2
March 2016, from http://www.chemistryexplained.com/A-Ar/Allosteric-Enzymes.html
Middleschoolchemistry.com,. (2016). Multimedia: DensitySink and Float for Liquids | Chapter 3, Lesson 5 | Middle
School Chemistry. Retrieved 25 February 2016, from
http://www.middleschoolchemistry.com/multimedia/chapter3/lesson5