User:John S. de Banzie/Sandbox 2

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The enzyme has <scene name='59/590622/4cpacartoon/2'>mixed secondary structure</scene>. A <scene name='59/590622/4cpacartoonzn/3'>zinc ion</scene> is present. The ion is involved in binding and catalysis.
The enzyme has <scene name='59/590622/4cpacartoon/2'>mixed secondary structure</scene>. A <scene name='59/590622/4cpacartoonzn/3'>zinc ion</scene> is present. The ion is involved in binding and catalysis.
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Three interactions hold the substrate in the active site.
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Substrate binding involves three interactions between the substrate and the active site.
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1. <scene name='59/590622/4cpabindone/3'>Between the carbonyl group of the penultimate residue in the substrate and the zinc ion and an arginine in the enzyme</scene>.
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1. <scene name='59/590622/4cpabindone/3'>Between the carbonyl group of the penultimate residue in the substrate and the zinc ion and an arginyl residue in the enzyme</scene>.
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2. <scene name='59/590622/4cpabindtwo/1'>Between the C-terminal carboxyl group and asparagine, arginine, and tyrosine residues in the enzyme</scene>.
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2. <scene name='59/590622/4cpabindtwo/2'>Between the C-terminal carboxyl group and asparaginyl, arginyl, and tyrosyl residues in the enzyme</scene>.
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3. <scene name='59/590622/4cpabindthree/1'>Between the C-terminal R group and a hydrophobic pocket in the enzyme</scene>.
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3. <scene name='59/590622/4cpabindthree/2'>Between the C-terminal R group and a hydrophobic pocket in the enzyme</scene>.
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Catalysis involves <scene name='59/590622/4cpacatalysis/1'>electron withdrawal from the carbonyl of the penultimate residue by the zinc ion and an arginyl residue, and nucleophilic attack on that same group by a glutamyl residue</scene>.

Revision as of 22:28, 12 June 2014

Carboxypeptidase A

Carboxypeptidase A, 4cpa

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References

Proteopedia Page Contributors and Editors (what is this?)

John S. de Banzie

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