Aminopeptidase
From Proteopedia
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Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide. | Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide. | ||
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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. | ||
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| + | The active site 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. | ||
Revision as of 18:07, 14 November 2007
Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide.
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 active site 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.
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, David Canner, Joel L. Sussman, Eran Hodis
