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 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