3.4.21.42: complement subcomponent C1s
This is an abbreviated version!
For detailed information about complement subcomponent C1s, go to the full flat file.
Word Map on EC 3.4.21.42
-
3.4.21.42
-
angioedema
-
hereditary
-
lectin
-
c1-inh
-
edema
-
swell
-
mannose-binding
-
masp-1
-
mannan-binding
-
coagulation
-
kallikrein
-
airway
-
prophylaxis
-
abdominal
-
bradykinin
-
life-threatening
-
laryngeal
-
angioneurotic
-
lectin-associated
-
c1-inhibitor
-
danazol
-
prophylactic
-
ficolins
-
plasma-derived
-
urticaria
-
icatibant
-
antithrombin
-
submucosal
-
kinin
-
fibrinolysis
-
larynx
-
kallikrein-kinin
-
asphyxiation
-
antifibrinolytic
-
prekallikrein
-
2-antiplasmin
-
ecallantide
-
2-macroglobulin
-
tranexamic
-
kininogens
-
antihistamine
-
pharmacology
-
bradykinin-mediated
-
serping1
-
collectins
-
behring
-
c4d
-
medicine
-
collagen-like
-
drug development
-
tracheotomy
-
fibrinogen-like
-
stanozolol
- 3.4.21.42
- angioedema
- hereditary
- lectin
-
c1-inh
- edema
-
swell
-
mannose-binding
- masp-1
-
mannan-binding
-
coagulation
- kallikrein
-
airway
-
prophylaxis
- abdominal
- bradykinin
-
life-threatening
- laryngeal
-
angioneurotic
-
lectin-associated
- c1-inhibitor
- danazol
-
prophylactic
- ficolins
-
plasma-derived
- urticaria
- icatibant
- antithrombin
-
submucosal
- kinin
-
fibrinolysis
- larynx
-
kallikrein-kinin
-
asphyxiation
-
antifibrinolytic
- prekallikrein
-
2-antiplasmin
- ecallantide
-
2-macroglobulin
-
tranexamic
- kininogens
-
antihistamine
- pharmacology
-
bradykinin-mediated
-
serping1
-
collectins
-
behring
- c4d
- medicine
-
collagen-like
- drug development
-
tracheotomy
-
fibrinogen-like
-
stanozolol
Reaction
Cleavage of Arg-/-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-/-Lys bond in complement component C2 to form C2a and C2b: the "classical" pathway C3 convertase =
Synonyms
activated complement C1s, C1 esterase, C1-esterase, C1g, C1s, C1s protease, C1s serine protease, complement 1s, complement C.hivin. 1s, complement C1s, complement C1s, activated, complement component 1 s, complement component 1 subcomponent s, complement component C1s, complement protease, complement protease C1s, complement subcomponent 1s, complement subcomponent C1sbar, esterase, C1, mannan-binding lectin-associated serine protease-2, MASP-2, MBL-associated serine protease-2, multiprotein complex C1, protease C1s, serine protease C1s
ECTree
3.4.21.42 complement subcomponent C1sAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.42 - complement subcomponent C1s
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-GLQRALEI-Lys(dinitrophenol)-NH2 + H2O
?
the Abz-GLQRALEI-Lys(Dnp)fluorescence quenched peptide representing the P4-P4' sequence of complement C4
-
-
?
2-aminobenzoyl-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Gly-Leu-Gln-Arg + Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2
2-aminobenzoyl-Gly-Tyr-Leu-Gly-Arg-Ser-Tyr-Lys-Val-Gly-Lys(dinitrophenyl)-Asp-OH + H2O
2-aminobenzoyl-Gly-Tyr-Leu-Gly-Arg + Ser-Tyr-Lys-Val-Gly-Lys(dinitrophenyl)-Asp-OH + H2O
-
substrate obtained from phage display analysis, 4.7fold higher procession than the natural C1s protease substrate (SLGRKIQI)
-
-
?
2-aminobenzoyl-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Leu-Gly-Arg + Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2
2-aminobenzoyl-Ser-Val-Ala-Arg-Thr-Leu-Leu-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Val-Ala-Arg + Thr-Leu-Leu-Lys(dinitrophenyl)-NH2 + H2O
-
-
-
-
?
Ac-Ala-P3-P2-P1-7-amino-4-carbamoylmethylcoumarin + H2O
?
-
a 722-member substrate library with combinations of all proteogenic amino acids at positions P3 and P2 was screened for cleavage, C1s preferred the small polar residues Ser, Ala and Gly at the P2 position and had a broad specificity at P3 position
-
-
?
benzoyl-beta-Ala-Gly-L-Arg 4-nitroanilide + H2O
benzoyl-beta-Ala-Gly-L-Arg + 4-nitroaniline
-
-
-
?
benzoyl-L-Pro-L-Phe-L-Arg 4-nitroanilide + H2O
benzoyl-L-Pro-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
benzoyl-L-Val-Gly-L-Arg 4-nitroaniline + H2O
benzoyl-L-Val-Gly-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-D-Ala-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-Gly-D-Ala-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-Leu-Gln-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Leu-Gln-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Lys 4-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Lys-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Lys-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Tyr-L-Lys-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Tyr-L-Lys-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Val-Gly-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Val-Gly-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ser-Leu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Ser-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
butyloxycarbonyl-L-Leu-Gly-L-Arg 4-nitroanilide + H2O
butyloxycarbonyl-L-Leu-Gly-L-Arg + 4-nitroaniline
-
-
-
?
butyloxycarbonyl-O-benzoyl-L-Ser-Gly-Arg 4-nitroanilide + H2O
butyloxycarbonyl-O-benzoyl-L-Ser-Gly-Arg + 4-nitroaniline
-
-
-
?
C2H5CO-Lys-(epsilon-Cbz)-Gly-Arg-4-nitroanilide + H2O
C2H5CO-Lys-(epsilon-Cbz)-Gly-Arg + 4-nitroaniline
-
-
-
?
complement C1q zymogen + H2O
?
C1s-C1q Collagen interface, the three collagen-like peptides form a right-handed helix with a characteristic one residue stagger between adjacent strands, overview
-
-
?
complement C4-bound C2 zymogen + H2O
C4a + C2b
-
the fragments associate to form a C3 convertase enzyme
-
?
D-CHG-L-Pro-L-Arg 4-nitroanilide + H2O
D-CHG-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
D-Ile-L-Phe-L-Lys 4-nitroanilide + H2O
D-Ile-L-Phe-L-Lys + 4-nitroaniline
-
-
-
?
D-Ile-L-Pro-L-Arg 4-nitroanilide + H2O
D-Ile-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
D-Pro-L-hexahydrotyrosine-L-Arg 4-nitroanilide + H2O
D-Pro-L-hexahydrotyrosine-L-Arg + 4-nitroaniline
-
-
-
?
D-Pro-L-Phe-L-Arg 4-nitroanilide + H2O
D-Pro-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
D-Val-L-cyclohexylalanine-L-Arg 4-nitroanilide + H2O
D-Val-L-cyclohexylalanine-L-Arg + 4-nitroaniline
-
-
-
?
D-Val-L-Leu-L-Arg 4-nitroanilide + H2O
D-Val-L-Leu-L-Arg + 4-nitroaniline
-
-
-
?
D-Val-L-Leu-L-Lys 4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
-
-
-
?
D-Val-L-Phe-L-Lys 4-nitroanilide + H2O
D-Val-L-Phe-L-Lys + 4-nitroaniline
-
-
-
?
insulin-like growth factor-I binding protein-5 + H2O
?
-
C1s accounts for the proteolytic activity in human osteoarthritis fluid for insulin-like growth factor-I binding protein-5
-
-
?
L-Glu-Gly-L-Arg 4-nitroanilide + H2O
L-Glu-Gly-L-Arg + 4-nitroaniline
-
-
-
?
L-Glu-L-Pro-L-Arg 4-nitroanilide + H2O
L-Glu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
methyloxycarbonyl-D-L-hexahydrotyrosine-Gly-L-Arg 4-nitroaniline + H2O
methyloxycarbonyl-D-L-hexahydrotyrosine-Gly-L-Arg + 4-nitroaniline
-
-
-
?
methyloxycarbonyl-D-Nle-Gly-L-Arg 4-nitroaniline + H2O
methyloxycarbonyl-D-Nle-Gly-L-Arg + 4-nitroaniline
-
-
-
?
methyloxycarbonyl-L-cyclohexylglycine-Gly-L-Arg 4-nitroaniline + H2O
methyloxycarbonyl-L-cyclohexylglycine-Gly-L-Arg + 4-nitroaniline
-
-
-
?
N2-acetyl-L-Lys-N6-benzyloxycarbonyl-Gly-L-Arg 4-nitroanilide + H2O
N2-acetyl-L-Lys-N6-benzyloxycarbonyl-Gly-L-Arg + 4-nitroaniline
best substrate
-
-
?
N2-acetyl-N6-benzyloxycarbonyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
N2-acetyl-N6-benzyloxycarbonyl-L-Lys-Gly-L-Arg + 4-nitroaniline
-
-
-
?
N2-acetyl-N6-benzyloxycarbonyl-Lys-Gly-Arg 4-nitroanilide + H2O
N2-acetyl-N6-benzyloxycarbonyl-Lys-Gly-Arg + 4-nitroaniline
-
-
-
-
?
N6-benzyloxycarbonyl-D-Lys-L-Pro-L-Arg 4-nitroanilide + H2O
N6-benzyloxycarbonyl-D-Lys-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
Sar-L-Pro-L-Arg 4-nitroanilide + H2O
Sar-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
tosyl-Gly-L-Pro-L-Arg 4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
tosyl-Gly-L-Pro-L-Lys 4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Lys + 4-nitroaniline
-
-
-
?
Z-AGLQR-7-amido-4-methylcoumarin + H2O
Z-AGLQR + 7-amino-4-methylcoumarin
-
-
-
?
Z-LGR-7-amido-4-methylcoumarin + H2O
Z-LGR + 7-amino-4-methylcoumarin
-
-
-
?
2-aminobenzoyl-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Gly-Leu-Gln-Arg + Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2
-
-
-
?
2-aminobenzoyl-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Gly-Leu-Gln-Arg + Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2
-
-
-
-
?
2-aminobenzoyl-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Leu-Gly-Arg + Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2
-
-
-
?
2-aminobenzoyl-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Leu-Gly-Arg + Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2
-
-
-
-
?
complement C1q zymogen + H2O
active complement C1q + ?
no or reduced activity with substrate mutants K59A, K61A, K58A, and K58A/K59A/K61A
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
-
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
cleavage of a single bond, likely to be Lys-Lys or Arg-Lys
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
the P1'-P4' substrate residues of C2 confer greater affinity of substrate for enzyme and also induce a sigmoidal dependence of enzyme velocity on substrate concentration. The substrate gives rise to homotropic positive cooperative behavior in the enzyme
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
-
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
-
-
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
cleavage of a single Arg-Ala bond in the sequence Leu-Gln-Arg-Ala-Leu-Glu
-
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
the P1'-P4' substrate residues of C4 confer greater affinity of substrate for enzyme and also induce a sigmoidal dependence of enzyme velocity on substrate concentration. The substrate gives rise to homotropic positive cooperative behavior in the enzyme
-
?
insulin-like growth factor-binding protein-5 + H2O
?
-
no activity with insulin-like growth factor-binding protein-1 through -4
-
?
insulin-like growth factor-binding protein-5 + H2O
?
-
the enzyme accounts for cleavage of insulin-like growth factor-binding protein-5 in fibroblast medium
-
?
N-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
?
-
N-alpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester
-
-
?
additional information
?
-
-
the enzyme prefers Arg at P1 3fold over Lys, does not accept citrulline
-
-
?
additional information
?
-
-
importance of the prime subsites of the C1s protease for recognition of substrates no cleavage of GLQRPLEI and GLQRAKEI
-
?
additional information
?
-
-
regulation of the synthesis of the complement enzymes. IFN-gamma increases the synthesis
-
-
?
additional information
?
-
-
binding of C1 to certain viral activators occurs through both C1s and C1q
-
-
?
additional information
?
-
-
the enzyme represents a pivotal upstream point of control in the classical pathway of complement activation
-
?
additional information
?
-
-
C1s is the executioner protease component of the C1 complex in the classical complement pathway cleaving C2 and C4 components of the system, overview
-
-
?
additional information
?
-
-
substrate and active site specificity of C1s in comparison to its equivalent MASP-2 of the lectin complement pathway, overview
-
-
?
additional information
?
-
substrate specificity, library screening, overview. The Lys residue found at the P1' position in C2 and the Gln residue found at the P2 position of C4 are likely to be prohibitive for cleavage of substrates by the C1s protease. The K628Q and K628A mutants of C1s also do not cleave these substrate pools, indicating that K628 does not play a crucial role in preventing interaction with such substrates
-
-
?
additional information
?
-
the enzyme recognizes the a short collagen-like peptide containing the sequence Hyp-Gly-Lys-Leu-Gly-Pro
-
-
?
additional information
?
-
the enzyme cleaves after Arg-/- or Lys-/- and prefers arginine at over 3fold over lysine, the enzyme does not accept citrulline. Occupancy of site S3 may yield an increase in Vmax/Km of over 10fold with the enzyme, but many residues are accepted at positions S2, S3 and S4. No activity with benzyloxycarbonyl-Gly-L-Pro-citrulline 4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme cleaves after Arg-/- or Lys-/- and prefers arginine at over 3fold over lysine, the enzyme does not accept citrulline. Occupancy of site S3 may yield an increase in Vmax/Km of over 10fold with the enzyme, but many residues are accepted at positions S2, S3 and S4. No activity with benzyloxycarbonyl-Gly-L-Pro-citrulline 4-nitroanilide
-
-
?
