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Literature summary for 3.4.21.41 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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of activation of C1s and MASP-3 mutants, overview Homo sapiens
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
0.000062
-
MASP-3 K448Q zymogen pH 7.4, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
zymogen C1s + H2O Homo sapiens
-
active C1s protease + ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P00736
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
Homo sapiens
-

Substrates and Products (Substrate)

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

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

Synonyms

Synonyms Comment Organism
C1r
-
Homo sapiens
complement subcomponent 1r
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0021
-
MASP-3 K448Q zymogen pH 7.4, 37°C Homo sapiens
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

General Information Comment Organism
metabolism C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex Homo sapiens
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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
340
-
MASP-3 K448Q zymogen pH 7.4, 37°C Homo sapiens
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