Literature summary for 3.4.21.41 extracted from

Kardos, J.; Harmat, V.; Pallo, A.; Barabas, O.; Szilagyi, K.; Graf, L.; Naray-Szabo, G.; Goto, Y.; Zavodszky, P.; Gal, P.
Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r (2008), Mol. Immunol., 45, 1752-1760.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of the isolated active catalytic region, containing the C-terminal serine protease domain, and two preceding complement control protein modules, of C1r in Escherichia coli strain BL21(DE3)	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant isolated active catalytic region forming a dimer in a head-to-tail fashion, complex of enzyme and product, hanging drop vapour diffusion method, 15°C, mixing of 0.008 ml protein solution, containing 0.2 mg/ml protein, 20 mM Tris-HCl, pH 7.4, and 130 mM NaC, with 0.008 ml reservoir solution containing 14% w/v PEG 6000, 0.2 M NaCl, 10% v/v glycerol, and 0.1 M Tris-HCl, pH 7.4, cryoprotection of crystals in 20% glycerol, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement	Homo sapiens

Crystallization (Comment)

Organism

purified recombinant isolated active catalytic region forming a dimer in a head-to-tail fashion, complex of enzyme and product, hanging drop vapour diffusion method, 15°C, mixing of 0.008 ml protein solution, containing 0.2 mg/ml protein, 20 mM Tris-HCl, pH 7.4, and 130 mM NaC, with 0.008 ml reservoir solution containing 14% w/v PEG 6000, 0.2 M NaCl, 10% v/v glycerol, and 0.1 M Tris-HCl, pH 7.4, cryoprotection of crystals in 20% glycerol, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement

Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
complement component C1s + H2O	Homo sapiens	the enzyme is part of the Ca2+-dependent tetramer C1s-C1r-C1r-C1s, termed as C1 complex, which is associated with the recognition molecule C1q, autoactivation of C1r, which then activates proenzyme C1s through cleavage at an Arg-Ile bond in the serine domain, C1r is active in the classical pathway of the complement system	activated complement component C1s + ?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00736	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	autoactivation of C1r as part of the C1 complex, modeling, overview	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
recombinant active catalytic region of C1r from Escherichia coli strain BL21(DE3) by ion exchange chromatography and gel filtration	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
complement component C1s + H2O	the enzyme is part of the Ca2+-dependent tetramer C1s-C1r-C1r-C1s, termed as C1 complex, which is associated with the recognition molecule C1q, autoactivation of C1r, which then activates proenzyme C1s through cleavage at an Arg-Ile bond in the serine domain, C1r is active in the classical pathway of the complement system	Homo sapiens	activated complement component C1s + ?	-	?
complement component C1s + H2O	C1r cleaves proenzyme C1s at an Arg-Ile bond in the serine domain, enzyme-product binding structure, overview	Homo sapiens	activated complement component C1s + ?	-	?

Synonyms

Synonyms	Comment	Organism
C1r	-	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Homo sapiens