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.
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 + ? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.41 |
Homo sapiens |
P00736 |
- |
- |
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 + ? |
- |
? |
|
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 + ? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.21.41 |
C1r |
- |
Homo sapiens |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.4.21.41 |
8 |
- |
assay at |
Homo sapiens |