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Results 1 - 10 of 17 > >>
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline - -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.14.5release 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
Results 1 - 10 of 17 > >>