65288a64fe These electrophilic groups are able to react with amino acid side chains to form covalent adducts. An active site is the part of an enzyme that directly binds to a substrate and carries a reaction. Once the shape is changed, the substrate is unbound to the enzyme, which ultimately changes the shape of the enzyme. The arrangement of atoms in the active site is crucial for binding spectificity. After the products of the reaction move away from the enzyme, the active site returns to its initial shape. Most reversible inhibitors follow the classic Michaelis-Menten scheme, where an enzyme (E) binds to its substrate(S) to form an enzyme-substrate complex (ES). Non-competitive inhibitors have identical affinities for E and ES. References[edit]. Binding site[edit]. Proteolytic enzymes are targets for some drugs, such as protease inhibitors, which include drugs against AIDS and hypertension.[6] These protease inhibitors bind to an enzyme's active site and block interaction with natural substrates.[7] An important factor in drug design is the strength of binding between the active site and an enzyme inhibitor.[8].
In addition, some reversible inhibitors can form irreversible products by binding so tightly to their target enzyme. This involves description of the size of an active site and the number and properties of sub-sites, such as details of the binding interaction.[6] Modern database technology called CPASS (Comparison of Protein Active Site Structures) however allows us to compare active sites in more detail and to look at structural similarity using software.[9]. Reversible Inhibitors[edit]. Induced fit hypothesis[edit]. Notes[edit]. ^ a b Sullivan SM (2008). 15: 379.
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