EC Number |
Reaction |
Reference |
---|
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline |
exopeptidase that cleaves dipeptides from the N-terminus of oligo- and polypeptides with the penultimate residue being proline or alanine |
649276 |
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline |
prefers Pro or Ala at position P1, substrate recognition involves the negatively charged active site residues E205 and E206, reaction mechanism, active site structure and substrate binding |
653811 |
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline |
proline specific serine protease |
649285 |
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline |
reaction mechanism |
651150 |
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline |
serine protease |
649281, 649615, 653506 |
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline |
serine protease, catalytic triad Ser630, Asp708, His740, active site architecture |
649200 |
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline |
specific for hydrolysis of peptide bond on the carboxylic side of proline residues which are penultimate from the amino terminus |
651515 |