Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Wijeyewickrema, L.C.; Yongqing, T.; Tran, T.P.; Thompson, P.E.; Viljoen, J.E.; Coetzer, T.H.; Duncan, R.C.; Kass, I.; Buckle, A.M.; Pike, R.N.
    Molecular determinants of the substrate specificity of the complement-initiating protease, C1r (2013), J. Biol. Chem., 288, 15571-15580.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.41 additional information
-
 additional information kinetics of activation of C1s and MASP-3 mutants, overview Homo sapiens
3.4.21.41 0.000022
-
 zymogen C1s pH 7.4, 37°C, substrate is a fragment consisting of complement control protein domains, CCP1 and CCP2, plus serine Homo sapiens
3.4.21.41 0.000062
-
 MASP-3 K448Q zymogen pH 7.4, 37°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.41 extracellular
-
 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 zymogen C1s + H2O Homo sapiens
-
 active C1s protease + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.41 Homo sapiens P00736
-
-
3.4.21.42 Homo sapiens P09871
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.41 blood plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.41 MASP-3 K448Q zymogen + H2O poor activity with the wild-type MASP-3 Homo sapiens active MASP-3 protein + ?
-
 ?
3.4.21.41 additional information 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 Homo sapiens ?
-
 ?
3.4.21.41 zymogen C1s + H2O
-
 Homo sapiens active C1s protease + ?
-
 ?
3.4.21.41 zymogen C1s + H2O 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 Homo sapiens active C1s protease + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.41 More C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex Homo sapiens
3.4.21.42 More C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.4.21.41 C1r
-
 Homo sapiens
3.4.21.41 complement subcomponent 1r
-
 Homo sapiens
3.4.21.42 C1s
-
 Homo sapiens
3.4.21.42 complement subcomponent 1s
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.41 0.0021
-
 MASP-3 K448Q zymogen pH 7.4, 37°C Homo sapiens
3.4.21.41 0.0645
-
 zymogen C1s pH 7.4, 37°C, substrate is a fragment consisting of complement control protein domains, CCP1 and CCP2, plus serine Homo sapiens

General Information

EC Number General Information Comment Organism
3.4.21.41 metabolism C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex Homo sapiens
3.4.21.41 additional information subsite profiling of human C1r using a phage display library with a fixed P1 arginine, specificity determinants, overview. Gln and Ile residues at P2 and P1', respectively, are important for cleavage of phage displayed substrates, the enzyme displays considerable specificity at every position apart from P4, P3', and P4' Homo sapiens
3.4.21.42 metabolism C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex. Zymogen C1s is cleaved by the C1r protease resulting in C1s activation, kinetics of activation of C1s by C1r protease, overview Homo sapiens
3.4.21.42 additional information synthesis of a series of fluorescence-quenched peptide substrates, comprising residues from the cleavage site in C1s and some peptides found among the phage-displayed peptides, very high concentrations of C1r are required to cleave such peptides Homo sapiens
3.4.21.42 physiological function enzyme C1r 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, C1s mutant Q462N/I464A gives very low activity as substrate for C1r Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.21.41 340
-
 MASP-3 K448Q zymogen pH 7.4, 37°C Homo sapiens
3.4.21.41 2900
-
 zymogen C1s pH 7.4, 37°C, substrate is a fragment consisting of complement control protein domains, CCP1 and CCP2, plus serine Homo sapiens