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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.41 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)

EC Number Crystallization (Comment) Organism
3.4.21.41 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.41 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 + ?
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?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.41 Homo sapiens P00736
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-

Posttranslational Modification

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.41 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.41 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 + ?
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?
3.4.21.41 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 + ?
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?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.41 C1r
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Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.41 8
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assay at Homo sapiens