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 |
- |
- |
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 |
active site structure and accessibility |
647177 |
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 |
active site structure modeling and reaction mechanism |
649278 |
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 |
active site structure, containing the catalytic triad Ser630, Asp708, and His740, is located in a large cavity at the interface of the 2 domains, substrate binding and catalytic mechanism, serine exopeptidase |
653913 |
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 |
catalytic domain structure, active site and substrate recognition study |
653593 |
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 |
cleaves dipeptides containing proline or alanine or one of several other amino acids at the penultimate position from the amino termini of substrates, contains a Ser-His-Asp catalytic triad, active site structure, the Glu-Glu motif is necessary for amino dipeptide selection |
650930 |
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 |
conserved residues Ser624, Asp702, and His734 form a catalytic triad and are involved in the catalytic reaction, Ser593 is likely to be the catalytic serine of the serine protease |
651478 |
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 |
enzyme is a serine protease, catalytic and substrate binding mechanism, active site structure, catalytic triad Ser630, Asp708, His740 |
653298 |
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 |
enzyme is an ectopeptidase |
652293 |
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 |
enzyme prefers Ala in P1 position, reduced activity is observed with Ser, Gly, or Val at the P1 position, modeling of reaction mechanism and substrate binding at the catalytic site |
649284 |