In biochemistry, allosteric regulation is the regulation of an enzyme or other protein by binding an effector molecule at the protein's allosteric site (that is, a site other than the protein's active site). Effectors that enhance the protein's activity are referred to as allosteric activators, whereas those that decrease the protein's activity are called allosteric inhibitors. The term allostery comes from the Greek allos (ἄλλος), other, and stereos (στερεὀς), solid (object), in reference to the fact that the regulatory site of an allosteric protein is physically distinct from its active site. Allosteric regulations are a natural example of control loops, such as feedback from downstream products or feedforward from upstream substrates. Long-range allostery is especially important in cell signaling.
The allosteric site of the enzyme plays an important role in the activity of an enzyme. The questions in this quiz will ask you to define the allosteric site and related terms, like allosteric. . Re:Need Explanations to NBME 19! #3372070: blessedalways - 09/10/18 12:01: Hey, for # 14 I finally figured out that AMP is an allosteric activator because it binds to the y-subunit of AMPK, resulting in the activation of catabolic pathways and the inhibition of anabolic pathways to.