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 ==
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| - | <applet load='1xjo' size='500' frame='true' align='right' caption='1xjo' />
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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.
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Revision as of 21:44, 4 February 2008
Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide.
