User:John S. de Banzie/Sandbox 2
From Proteopedia
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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. | ||
- | + | Substrate binding involves three interactions between the substrate and the active site. | |
- | 1. <scene name='59/590622/4cpabindone/3'>Between the carbonyl group of the penultimate residue in the substrate and the zinc ion and an | + | 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>. |
- | 2. <scene name='59/590622/4cpabindtwo/ | + | 2. <scene name='59/590622/4cpabindtwo/2'>Between the C-terminal carboxyl group and asparaginyl, arginyl, and tyrosyl residues in the enzyme</scene>. |
- | 3. <scene name='59/590622/4cpabindthree/ | + | 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
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