BRENDA - Enzyme Database
show all sequences of 3.4.21.41

Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r

Kardos, J.; Harmat, V.; Pallo, A.; Barabas, O.; Szilagyi, K.; Graf, L.; Naray-Szabo, G.; Goto, Y.; Zavodszky, P.; Gal, P.; Mol. Immunol. 45, 1752-1760 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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)
Crystallization
Organism
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)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P00736
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
proteolytic modification
autoactivation of C1r as part of the C1 complex, modeling, overview
Homo sapiens
Purification (Commentary)
Commentary
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
683889
Homo sapiens
activated complement component C1s + ?
-
-
-
?
complement component C1s + H2O
C1r cleaves proenzyme C1s at an Arg-Ile bond in the serine domain, enzyme-product binding structure, overview
683889
Homo sapiens
activated complement component C1s + ?
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
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) (protein specific)
Crystallization
Organism
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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 + ?
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
proteolytic modification
autoactivation of C1r as part of the C1 complex, modeling, overview
Homo sapiens
Purification (Commentary) (protein specific)
Commentary
Organism
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
683889
Homo sapiens
activated complement component C1s + ?
-
-
-
?
complement component C1s + H2O
C1r cleaves proenzyme C1s at an Arg-Ile bond in the serine domain, enzyme-product binding structure, overview
683889
Homo sapiens
activated complement component C1s + ?
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
Other publictions for EC 3.4.21.41
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732102
Wijeyewickrema
Molecular determinants of the ...
Homo sapiens
J. Biol. Chem.
288
15571-15580
2013
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732820
Venkatraman Girija
Structural basis of the C1q/C1 ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
110
13916-13920
2013
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3
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732824
Bally
Expression of recombinant huma ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
110
8650-8655
2013
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732889
Beveridge
A molecular dynamics study of ...
Homo sapiens
Proteins
80
1987-1997
2012
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3
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717587
Lang
Intermodule cooperativity in t ...
Homo sapiens
FEBS J.
277
3986-3998
2010
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1
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717603
Lang
Interaction between separated ...
Homo sapiens
FEBS Lett.
584
4565-4569
2010
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717786
Major
Calcium-dependent conformation ...
Homo sapiens
J. Biol. Chem.
285
11863-11869
2010
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717805
Brier
Mapping surface accessibility ...
Homo sapiens
J. Biol. Chem.
285
32251-32263
2010
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718116
Valck
Molecular mechanisms involved ...
Homo sapiens
Mol. Immunol.
47
1516-1521
2010
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718117
Kaplan
The plasma bradykinin-forming ...
Homo sapiens
Mol. Immunol.
47
2161-2169
2010
-
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1
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683195
Duncan
The initiating proteases of th ...
Homo sapiens
Biochimie
90
387-395
2008
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683889
Kardos
Revisiting the mechanism of th ...
Homo sapiens
Mol. Immunol.
45
1752-1760
2008
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696932
Gaultier
Regulation of tumor necrosis f ...
Mus musculus
Blood
111
5316-5325
2008
1
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697529
Goesswein
Mutational spectrum of the C1I ...
Homo sapiens
Cytogenet. Genome Res.
121
181-188
2008
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698805
Geach
Molecular determinants of Xoll ...
Xenopus laevis
J. Biol. Chem.
283
27057-27063
2008
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700245
Davis
Biological activities of C1 in ...
Homo sapiens
Mol. Immunol.
45
4057-4063
2008
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1
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683530
Biro
Studies on the interactions be ...
Homo sapiens
Immunology
121
40-50
2007
1
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650989
Budayova-Spano
The crystal structure of the z ...
Homo sapiens
EMBO J.
21
231-239
2002
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653898
Budayova-Spano
Monomeric structures of the zy ...
Homo sapiens
Structure
10
1509-1519
2002
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652176
Lacroix
Assembly and enzymatic propert ...
Homo sapiens
J. Biol. Chem.
276
36233-36240
2001
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1
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652680
Kardos
The role of the individual dom ...
Homo sapiens
J. Immunol.
167
5202-5208
2001
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1
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1
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1
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81405
Dobo
One active C1r subunit is suff ...
Homo sapiens
J. Immunol.
162
1108-1112
1999
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81391
Gal
Structure and function of the ...
Homo sapiens
Immunobiology
199
317-326
1998
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1
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81388
Thielens
Activation of human complement ...
Homo sapiens
Biochem. J.
301
509-516
1994
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81390
Illy
Chemical characterization and ...
Homo sapiens
J. Protein Chem.
12
771-781
1993
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1
1
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81400
Katz
Regulation of synthesis of com ...
Homo sapiens
Clin. Immunol. Immunopathol.
67
117-123
1993
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1
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1
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81401
Zavodszky
Protein engineering studies on ...
Homo sapiens
Behring Inst. Mitt.
93
103-114
1993
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1
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81402
Gulati
Regulation of the synthesis of ...
Homo sapiens
Behring Inst. Mitt.
93
196-203
1993
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1
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5
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5
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81403
Arlaud
Human complement serine protea ...
Homo sapiens
Methods Enzymol.
223
61-82
1993
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1
6
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1
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2
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1
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1
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4
1
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1
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1
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6
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1
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1
1
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1
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4
1
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1
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1
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81404
Kam
Substituted isocoumarins as in ...
Homo sapiens
J. Immunol.
149
163-168
1992
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3
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81399
Thielens
Ca2+ binding properties and Ca ...
Homo sapiens
J. Biol. Chem.
265
14469-14475
1990
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81386
Busby
Calcium-sensitive thermal tran ...
Homo sapiens
Biochemistry
26
5564-5571
1987
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2
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1
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81387
Journet
Cloning and sequencing of full ...
Homo sapiens
Biochem. J.
240
783-787
1986
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81397
Reboul
Characteristics of complement ...
Homo sapiens
Biochem. J.
233
559-564
1986
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81389
Loos
-
C1rbar-esterase ...
Homo sapiens
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
514-527
1984
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81396
Nilsson
Kinetics of the reaction betwe ...
Homo sapiens
Eur. J. Biochem.
129
663-667
1983
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81395
Sim
The human complement system se ...
Homo sapiens
Methods Enzymol.
80
26-42
1981
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5
1
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2
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5
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2
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81394
Sim
Kinetics of reaction of human ...
Homo sapiens
Biochim. Biophys. Acta
612
433-449
1980
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81398
Arlaud
Purified proenzyme C1r. Some c ...
Homo sapiens
Biochim. Biophys. Acta
616
116-129
1980
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1
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81392
Andrews
The enzymatic nature of human ...
Homo sapiens
J. Immunol.
123
1403-1408
1979
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81393
Sim
The structure and enzymic acti ...
Homo sapiens
Biochem. J.
163
219-227
1977
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