Literature summary for 3.4.21.41 extracted from

Thielens, N.M.; Illy, C.; Bally, I.M.; Arlaud, G.J.
Activation of human complement serine-proteinase C1r is down-regulated by a Ca(2+)-dependent intramolecular control that is released in the C1 complex through a signal transmitted by C1q (1994), Biochem. J., 301, 509-516.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic 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	Homo sapiens

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Release 2023.1 (January 2023)