Carboxypeptidase A: Difference between revisions

The active site of bovine pancreatic CPA is embedded within a <scene name='69/694222/3cpadeeppocket/1'>deep pocket</scene> (shown in orange); the deep pocket's opening is located on the surface of the protein.  Kinetics experiments have indicated that the binding region of the active site is actually capable of extending over five amino acids of the substrate.<ref name="CPA2" />  When no polypeptide substrate is bound in the active site, the pocket is open. However, the pocket is <scene name='69/694222/3cpadeeppocket2/2'>"capped" by a tyrosine residue (Tyr248)</scene> (see section titled "Important Tyr248 Residue") when a substrate or [http://en.wikipedia.org/wiki/Enzyme_inhibitor inhibitor] molecule binds.<ref name="CPA2" />  In this view, the  Tyr248 is shown in purple.  The active site contains two separate subsites, labeled S1' and S1, each of which contain several pertinent residues that serve important roles during the catalyzed hydrolysis reaction.