What does the allosteric site of an enzyme do?
allosteric site. The place on an enzyme where a molecule that is not a substrate may bind, thus changing the shape of the enzyme and influencing its ability to be active.
Enzymes speed up chemical reactions that are used to build structures in your cells or break them down. The substrate is the name for the substance an enzyme works on. The substrate binds to the active site, or the place on the enzyme that actually does the work.
- The regulation of 1-phosphofructokinase occurs primarily by allosteric effectors, and is based on the cell's energy needs. There are two ATP binding sites; a substrate site where the phosphate transfer occurs, and an allosteric site where allosteric regulation occurs.
- Allosteric enzymes. Effectors are small molecules which modulate the enzyme activity; they function through reversible, non-covalent binding of a regulatory metabolite in the allosteric site (which is not the active site).
- An allosteric enzyme is an enzyme that contains a region to which small, regulatory molecules ("effectors") may bind in addition to and separate from the substrate binding site and thereby affect the catalytic activity.
Allosteric enzymes are enzymes that change their conformational ensemble upon binding of an effector, which results in an apparent change in binding affinity at a different ligand binding site. The site to which the effector binds is termed the allosteric site.
- Cooperativity, in enzymology, a phenomenon in which the shape of one subunit of an enzyme consisting of several subunits is altered by the substrate (the substance upon which an enzyme acts to form a product) or some other molecule so as to change the shape of a neighbouring subunit.
- In biochemistry and pharmacology, an allosteric modulator (allo- from the Greek meaning "other") is a substance which indirectly influences (modulates) the effects of a primary ligand that directly activates or deactivates the function of a target protein.
- Isozyme. Isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. These enzymes usually display different kinetic parameters (e.g. different KM values), or different regulatory properties.
allosteric effect The binding of a ligand to one site on a protein molecule in such a way that the properties of another site on the same protein are affected. Some enzymes are allosteric proteins, and their activity is regulated through the binding of an effector to an allosteric site. "allosteric effect."
- Definition of allosteric. : of, relating to, undergoing, or being a change in the shape and activity of a protein (such as an enzyme) that results from combination with another substance at a point other than the chemically active site.
- Covalent modifications are enzyme-catalysed alterations of synthesised proteins and include the addition or removal of chemical groups. Modifications can target a single type of amino acid or multiple amino acids and will change the chemical properties of the site.
- Reversible covalent modification is the making and breaking of a covalent bond between a non-protein group and an enzyme molecule. The most common reversible modification is the addition and removal of phosphate groups through the processes of phosphorylation and dephosphorylation.
Updated: 21st November 2019