Aminopeptidase
From Proteopedia
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===Additional Resources=== | ===Additional Resources=== | ||
| - | For additional information, see: [[ | + | For additional information, see: [[Amino Acid Synthesis & Metabolism]] |
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Revision as of 10:17, 1 October 2010
Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide.
S. griseus aminopeptidase
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S. griseus aminopeptidase (SGAP) cleaves the N-terminal amino acid from a peptide or protein, and is specific for larger hydrophobic acids, especially leucine. No cleavage occurs if the next residue is proline.
The of the enzyme contains two Zn2+ ions with His85 and Asp160 as ligands for one ion, and Glu132 and His247 as ligands for the second ion. Asp97 is a common ligand to both ions. What appears to be a phosphate anion is bound to both zinc atoms, replacing the water molecule/hydroxide ion normally found in this class of enzyme.
Additional Resources
For additional information, see: Amino Acid Synthesis & Metabolism
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