Carboxypeptidase A: Difference between revisions

As previously stated, <scene name='69/694222/1cpx_default/3'>CPA</scene> from ''B. taurus'' has the ability to bind two Zn²⁺ ions in its active site.  The binding of only one Zn²⁺ ion is [http://en.wikipedia.org/wiki/Catalysis catalytic], while the binding of a second is [http://en.wikipedia.org/wiki/Reaction_inhibitor inhibitory].  These Zn²⁺ ions are connected to each other via a hydroxy-bridge (Figure 4) with a distance of 3.48 [http://en.wikipedia.org/wiki/%C3%85ngstr%C3%B6m Å].<ref name="CPA1" />    In the CPA structure containing only the catalytic Zn²⁺ ion (3CPA), a water molecule complexed to the zinc is able to be deprotonated by <scene name='69/694222/3cpas1subsiteglu270/3'>Glu270</scene> to allow for normal initiation of hydrolysis.  Again, this water molecule was not crystallized in the structure of 3CPA, but it is shown in Figure 3.  However, when <scene name='69/694222/Glu270wiz/8'>the inhibitory zinc ion</scene> is also present ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1cpx 1CPX]), it occupies the physical space that would normally be occupied by the water molecule.  Thus, the inhibitory Zn²⁺ ion interacts with the carboxylate group of Glu270.  The Glu270 (shown in yellow) now simply stabilizes the second Zn²⁺ and is unable to perform its usual base catalyst role while the catalytic Zn²⁺ ion (shown in cyan) is still being stabilized in place by His69, Glu72, and His196 (shown in orange). <ref name=“Binding”>Hirose, J., Noji, M., Kidani, Y., Wilkins, R. 1985. Interaction of zinc ions with arsanilazotyrosine-248 carboxypeptidase A.''Biochemistry''. 24(14):3495-3502. [http://pubs.acs.org/doi/abs/10.1021/bi00335a016 DOI:10.1021/bi00335a016]</ref>