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User:John S. de Banzie/Sandbox 2

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<scene name='59/590622/3cpacatalysis/1'>Catalysis</scene><ref name="quiocho"/> involves electron withdrawal from the carbonyl of the penultimate residue (in this case, Gly) by the zinc ion and an arginyl residue, and acid-base catalysis by a glutamyl residue of a nucleophilic attack on that same group.
<scene name='59/590622/3cpacatalysis/1'>Catalysis</scene><ref name="quiocho"/> involves electron withdrawal from the carbonyl of the penultimate residue (in this case, Gly) by the zinc ion and an arginyl residue, and acid-base catalysis by a glutamyl residue of a nucleophilic attack on that same group.
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(X-ray crystallography with intact substrate was possible because Gly-Tyr is hydrolyzed very slowly and because X-ray crystallography was carried out at -9° C.)
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(X-ray crystallography with intact substrate was possible because Gly-Tyr is hydrolyzed very slowly and because X-ray crystallography was carried out at -9°C.)
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 15:03, 13 June 2014

Carboxypeptidase A with Substrate

Carboxypeptidase A with the dipeptide Gly-Tyr in the active site, 3cpa

Drag the structure with the mouse to rotate

References

  1. 1.0 1.1 Quiocho, F. A. and W. N. Lipscomb (1971). "Carboxypeptidase A: a protein and an enzyme." Adv Protein Chem 25: 1-78.

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John S. de Banzie

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