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Results 1 - 10 of 16 > >>
EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41glycoprotein - 683195
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41glycoprotein carbohydrate content of C1r fragments 652176
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification - 81389
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification activation of C1r involves cleavage of a single peptide bond which converts the proenzyme into active enzyme. Activation of the serine-proteinase domain of C1r is controlled by a Ca2+-dependent intramolecular mechanism involving the Ca2+-binding alpha-region. This control is released in C1 by a signal originating in C1q and transmitted through the C1q/C1r interface 81388
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification activation of the proenzyme C1r can be mimicked under certain conditions by digestion of C1r with trypsin or plasmin 81395
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification autoactivation of C1r as part of the C1 complex 683195
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification autoactivation of C1r as part of the C1 complex, modeling, overview 683889
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification autolytic proteolysis involves cleavage of the Arg279-Gly280 bond in the sequence Asp-Ser-Arg-Gly-Trp-Lys 81403
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar 81390
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.41proteolytic modification the proenzyme C1r is not autoactivatable but undergoes proteolysis by exogenous C1rbar 81397
Results 1 - 10 of 16 > >>