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EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Preferential cleavage: Glu-/-, Asp-/- - -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Preferential cleavage: Glu-/-, Asp-/- absolutely specific for cleavage sites Glu-/-Xaa and Asp-/-Xaa, cleavage exclusively at the carboxylic side, active site Ser169 649239
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Preferential cleavage: Glu-/-, Asp-/- catalytic tetrad of His213, Asp102, Ser195, and Trp214, computer modeling of S1 and S'1 sites of the enzyme's active site -, 653874
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Preferential cleavage: Glu-/-, Asp-/- catalytic triad of His, Asp, and Ser 653874
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Preferential cleavage: Glu-/-, Asp-/- catalytic triad of His, Asp, and Ser, computer modeling of active site structure, S1-substrate binding site, and substrate binding mechanism 653874
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Preferential cleavage: Glu-/-, Asp-/- catalytic triad of His, Asp, and Ser, substrate binding mechanism and structure 653874
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.19Preferential cleavage: Glu-/-, Asp-/- specific for cleavage on the carboxylic site of glutamic acid, catalytic site are His47 and Ser171, the N-terminus is involved in formation of the substrate binding pocket, a direct structural relation between zymogen activation and substrate charge compensation exists 650241
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