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User:John S. de Banzie/Sandbox 2
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The enzyme has <scene name='59/590622/3cpacartoon/1'>mixed secondary structure</scene>. A zinc ion (violet) is present. The ion is involved in binding and catalysis. | The enzyme has <scene name='59/590622/3cpacartoon/1'>mixed secondary structure</scene>. A zinc ion (violet) is present. The ion is involved in binding and catalysis. | ||
| - | Substrate binding involves three interactions between the substrate and the active site. | + | Substrate binding involves three interactions between the substrate and the active site<ref name="quiocho">Quiocho, F. A. and W. N. Lipscomb (1971). "Carboxypeptidase A: a protein and an enzyme." Adv Protein Chem 25: 1-78.</ref>. |
1. <scene name='59/590622/3cpabindone/1'>Between the carbonyl group of the penultimate residue in the substrate (in this case, Gly) and the zinc ion and an arginyl residue in the enzyme</scene>. | 1. <scene name='59/590622/3cpabindone/1'>Between the carbonyl group of the penultimate residue in the substrate (in this case, Gly) and the zinc ion and an arginyl residue in the enzyme</scene>. | ||
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3. <scene name='59/590622/3cpabindthree/1'>Between the C-terminal R group and a hydrophobic pocket in the enzyme</scene>. | 3. <scene name='59/590622/3cpabindthree/1'>Between the C-terminal R group and a hydrophobic pocket in the enzyme</scene>. | ||
| - | <scene name='59/590622/3cpacatalysis/1'>Catalysis</scene> 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. |
(The substrate remained intact because Gly-Tyr is hydrolyzed very slowly and because X-ray crystallography was carried out at -9° C.) | (The substrate remained intact because Gly-Tyr is hydrolyzed very slowly and because X-ray crystallography was carried out at -9° C.) | ||
Revision as of 14:58, 13 June 2014
Carboxypeptidase A with Substrate
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