3.4.21.41: complement subcomponent C1r
This is an abbreviated version!
For detailed information about complement subcomponent C1r, go to the full flat file.
Reaction
Selective cleavage of Lys(or Arg)-/-Ile bond in complement subcomponent C1s to form C_overbar_1s_ (EC 3.4.21.42) =
Synonyms
activated complement C1r, C1r, C1r protease, C1r serine protease, C1r-LP, C1rbar-esterase, complement C1r subcomponent-like protein, complement C1r, activated, complement protease C1r, complement subcomponent 1r, CUB, multiprotein complex C1, proteases C1r, serine protease C1r, Xld, xolloid
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.41 - complement subcomponent C1r
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REACTION DIAGRAM
benzyloxycarbonyl-Lys-thiobenzyl ester + H2O
benzyloxycarbonyl-Lys + phenylmethanethiol
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?
chordin + H2O
?
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C-terminal domains CUB1 and CUB2 are required for the ventralizing activity of Xld and for its ability to cleave chordin
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-
?
MASP-3 K448Q zymogen + H2O
active MASP-3 protein + ?
poor activity with the wild-type MASP-3
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-
?
N-acetyl-Gly-Lys methyl ester + H2O
N-acetyl-Gly-Lys + methanol
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-
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?
N-carbobenzoxy-Lys-p-nitrophenyl ester + H2O
N-carbobenzoxy-Lys + 4-nitrophenyl
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-
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?
N-carbobenzoxy-Tyr-p-nitrophenyl ester + H2O
N-carbobenzoxy-Tyr + 4-nitrophenol
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-
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?
prohaptoglobin + H2O
haptoglobin + ?
the enzyme cleaves prohaptoglobin after arginine R102 in variants Hp1F and Hp1S or after R161 in variant Hp2FS
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?
complement C1q zymogen + H2O
active complement C1q + ?
no or reduced activity with substrate mutants K59A, K61A, K58A, and K58A/K59A/K61A
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?
complement component C1s
?
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binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar, which in turn activates C1s, thereby initiating the classical pathway of complement
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?
complement component C1s
?
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activates the proenzyme form of C1s by limited proteolysis
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?
activated complement component C1s + ?
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?
complement component C1s + H2O
activated complement component C1s + ?
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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
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?
complement component C1s + H2O
activated complement component C1s + ?
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
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?
complement component C1s + H2O
activated complement component C1s + ?
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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, interaction anaylsis of the C1 complex and regulatory proteins, overview
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?
complement component C1s + H2O
activated complement component C1s + ?
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C1r cleaves proenzyme C1s at an Arg-Ile bond in the serine domain
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?
complement component C1s + H2O
activated complement component C1s + ?
C1r cleaves proenzyme C1s at an Arg-Ile bond in the serine domain, enzyme-product binding structure, overview
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?
complement component C1s + H2O
activated complement component C1s + ?
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?
complement component C1s + H2O
activated complement component C1s + ?
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?
complement component C1s + H2O
complement component C1sbar
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cleavage of a single Arg-Ile or Lys-Ile bond in C1s
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?
complement component C1s + H2O
complement component C1sbar
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cleavage of a single Arg-Ile bond in the sequence Lys-Gln-Arg-Ile-Ile-Gly
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?
complement component C1s + H2O
complement component C1sbar
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C1rbar does not hydrolyze any amino acid ester tested nor any protein substrate except subcomponent C1s
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?
complement component C1s + H2O
complement component C1sbar
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C1R and its activated fragments all cleave C1s, in the order of increasing efficiency: C21r, CCP1/2-SP, CCP2-SP. CCP1 is not involved in C1s recognition
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?
zymogen C1s + H2O
active C1s protease + ?
the enzyme is active with the substrate fragment consisting of complement control protein domains, CCP1 and CCP2, plus serine protease domain of wild-type and mutant Q462N, Q462G, I464A, and Q462N/I464A forms of C1s, mutant Q462N/I464A substrate gives very low activity
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?
?
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the ability of autoactivation of C1r and C1s cleavage activity is an inherent property of the SP domain
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?
additional information
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the enzyme recognizes the a short collagen-like peptide containing the sequence Hyp-Gly-Lys-Leu-Gly-Pro
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?
additional information
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the residues found in the activation loop of the zymogens capable of being activated by enzyme C1r play a major role in recognition of the active site of enzyme C1r
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?