Information on EC 3.4.21.69 - Protein C (activated)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.69
-
RECOMMENDED NAME
GeneOntology No.
Protein C (activated)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
degradation of blood coagulation factors Va and VIIIa
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
42617-41-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
German Landrace piglets
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
active factor Va + H2O
inactive factor V + ?
show the reaction diagram
active factor Va + H2O
inactive factor V + domain B
show the reaction diagram
active factor Va + H2O
inactive factor V heavy chain + peptide fragment 307-709
show the reaction diagram
active factor Va mutant R306Q + H2O
?
show the reaction diagram
-
proteolytic inactivation, cleavage at Arg506
-
-
?
active factor Va mutant R306Q + H2O
inactive factor V mutant R306Q + ?
show the reaction diagram
-
proteolytic inactivation, cleavage of the heavy chain at Arg506 and Arg679
-
-
?
active factor Va mutant R306Q/R679Q + H2O
inactive factor V mutant R306Q/R679Q + ?
show the reaction diagram
-
recombinant substrate expressed in COS-1 cells, proteolytic inactivation, cleavage of the heavy chain at Arg506, protected by factor Xa
-
-
?
active factor Va mutant R506Q + H2O
?
show the reaction diagram
-
proteolytic inactivation, cleavage at Arg306
-
-
?
active factor Va mutant R506Q + H2O
inactive factor V mutant R506Q + ?
show the reaction diagram
-
proteolytic inactivation, cleavage of the heavy chain at Arg306 and Arg679
-
-
?
active factor Va mutant R506Q/R679Q + H2O
inactive factor V mutant R506Q/R679Q + ?
show the reaction diagram
-
recombinant substrate expressed in COS-1 cells, proteolytic inactivation, cleavage of the heavy chain at Arg306, stimulated by factor Xa
-
-
?
active factor Va mutant R679Q + H2O
inactive factor V mutant R679Q + ?
show the reaction diagram
-
proteolytic inactivation, cleavage of the heavy chain at Arg306 and Arg506
-
-
?
active factor VIII + H2O
inactive factor VIII + domain B
show the reaction diagram
-
activated protein C and activated factor X play a role in proteolytic inactivation of activated coagulation factor VIII involving the B domain, the inactivated substrate factor VIII is less efficient on blood clotting, overview
-
-
?
active factor VIIIa + H2O
inactive factor VIII + domain B
show the reaction diagram
Benzyloxycarbonyl-Val-Gly-Arg + H2O
?
show the reaction diagram
-
-
-
-
-
Boc-Leu-Ser-Thr-Arg-4-nitroanilide + H2O
Boc-Leu-Ser-Thr-Arg + 4-nitroaniline
show the reaction diagram
Bradykinin + H2O
?
show the reaction diagram
-
proteolytic inactivation
-
-
?
D-Ile-Pro-Arg + H2O
?
show the reaction diagram
-
-
-
-
-
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
show the reaction diagram
-
S-2238
-
-
?
D-Phe-pipecolyl-Arg + H2O
?
show the reaction diagram
-
-
-
-
-
D-Pro-Phe-Arg + H2O
?
show the reaction diagram
-
-
-
-
-
D-Val-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
i.e. S-S2266
-
?
D-Val-cyclohexyl-Ala-Arg + H2O
?
show the reaction diagram
-
-
-
-
-
D-Val-Leu-Arg + H2O
?
show the reaction diagram
-
-
-
-
-
factor V + H2O
?
show the reaction diagram
Factor Va + H2O
?
show the reaction diagram
factor Va Leiden + H2O
?
show the reaction diagram
Factor VaR506Q + H2O
?
show the reaction diagram
-
The substrate is derived from factor Va by replacing Arg506 by Gln. In the presence of phospholipids the substrate is hydrolyzed at Arg306, but in the absence of phospholipids hydrolysis occurs at Arg679, followed by cleavage at Arg306, suggesting that the binding of phospholipids alters the accessibility of Arg679
-
-
-
factor VIII + H2O
?
show the reaction diagram
Factor VIIIa + H2O
?
show the reaction diagram
ghrelin + H2O
?
show the reaction diagram
L-pGln-L-Pro-L-Arg-4-nitroanilide + H2O
L-pGln-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-Arg 4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
show the reaction diagram
-
amidase activity
-
-
-
octanoyl-ghrelin + H2O
?
show the reaction diagram
octanoyl-ghrelin + H2O
octanoyl ghrelin(1-15) + ?
show the reaction diagram
octanoyl-truncated ghrelin + H2O
?
show the reaction diagram
octanoyl-truncated ghrelin + H2O
ghrelin(1-15) + ?
show the reaction diagram
protease activated receptor 1 + H2O
?
show the reaction diagram
protease activated receptor 3 N-terminal peptide + H2O
?
show the reaction diagram
-
the enzyme cleaves a synthetic PAR3 N-terminal peptide at Arg41
-
-
?
protease activated receptor 3 zymogen H2O
active protease activated receptor 3 + ?
show the reaction diagram
protease-activated receptor-1 + H2O
?
show the reaction diagram
-
-
-
-
?
pyroGlu-Pro-Arg-4-nitroanilide + H2O
pyroGlu-Pro-Arg + 4-nitroaniline
show the reaction diagram
S-2238 + H2O
?
show the reaction diagram
-
a chromogenic substrate
-
-
?
S-2288 + H2O
?
show the reaction diagram
-
i.e. D-Ile-L-Pro-L-Arg-p-nitroanilide
-
?
S-2366 + H2O
?
show the reaction diagram
S2238 + H2O
?
show the reaction diagram
-
a commercial chromogenic substrate
-
-
?
S2366 + H2O
?
show the reaction diagram
spectrozyme PCa + H2O
?
show the reaction diagram
-
-
?
SpPCa + H2O
?
show the reaction diagram
-
a commercial tripeptidyl chromogenic substrate
-
-
?
Toluene-p-sulfonyl-Gly-Pro-Arg + H2O
?
show the reaction diagram
-
-
-
-
-
Toluene-p-sulfonyl-Gly-Pro-Lys + H2O
?
show the reaction diagram
-
-
-
-
-
Z-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Z-Gly-Gly-Arg-aminomethylcoumarin + H2O
?
show the reaction diagram
-
a fluorogenic substrate, S-2366
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
active factor Va + H2O
inactive factor V + ?
show the reaction diagram
active factor Va + H2O
inactive factor V + domain B
show the reaction diagram
active factor Va + H2O
inactive factor V heavy chain + peptide fragment 307-709
show the reaction diagram
-
proteolytic inactivation
-
-
?
active factor VIII + H2O
inactive factor VIII + domain B
show the reaction diagram
-
activated protein C and activated factor X play a role in proteolytic inactivation of activated coagulation factor VIII involving the B domain, the inactivated substrate factor VIII is less efficient on blood clotting, overview
-
-
?
active factor VIIIa + H2O
inactive factor VIII + domain B
show the reaction diagram
factor V + H2O
?
show the reaction diagram
-
proteolytic inactivation
-
?
Factor Va + H2O
?
show the reaction diagram
factor VIII + H2O
?
show the reaction diagram
Factor VIIIa + H2O
?
show the reaction diagram
ghrelin + H2O
?
show the reaction diagram
protease activated receptor 1 + H2O
?
show the reaction diagram
protease activated receptor 3 zymogen H2O
active protease activated receptor 3 + ?
show the reaction diagram
-
the enzyme cleaves the substrate PAR3 in transfected and endothelial cells in the presence of endothelial protein C receptor, as well as substrate mutant K38Q-PAR3, but fails to cleave the substrate mutant R41Q-PAR3
-
-
?
protease-activated receptor-1 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chondroitin sulfate
-
anticoagulant cofactor for APC
dermatan sulfate
-
anticoagulant cofactor for APC, important physiological cofactor
heparan sulfate
-
anticoagulant cofactor for APC
protein S
-
vitamin K
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cs+
-
activates, Km: 11 mM
Mg2+
-
significantly increases recombinant activated protein C binding to the neutrophil surface
Zn2+
-
Zn2+ enhances the binding of protein C/activated protein C to endothelial cell protein C receptor on endothelial cells by increasing the binding affinities. Zn2+ binding induces conformational changes in protein C/APC. Zn2+ binding to APC inhibits the amidolytic activity of APC, but the inhibition is reversed by Ca2+. Zn2+ increases the rate of APC generation on endothelial cells in the presence of physiological concentrations of Ca2+, but does not further enhance increased APC generation obtained in the presence of physiological concentrations of Mg2+ with Ca2+. Zn2+ has no effect on the anticoagulant activity of APC. Zn2+ enhances APC-mediated activation of protease activated receptor 1 and p44/42 MAPK
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Amino-D-Phe-Pro-Arg-CH2Cl
-
-
Ala-Phe-Arg-CH2Cl
-
-
alpha-2-Macroglobulin
-
-
-
Alpha1-antitrypsin
-
antithrombin III
-
-
-
Aprotinin
-
-
Benzamidine hydrochloride
D-Phe-Pro-Arg-CH2Cl
-
-
D-Tyr-Pro-Arg-CH2Cl
-
-
DAN-Glu-Gly-Arg-CMK
-
dansyl-glutamyl-glycyl-arginyl-chloromethylketone, blocks the enzyme
diisopropyl fluorophosphate
factor Xa
-
stimulates factor Va cleavage at Arg306, but inhibits the cleavage at Arg506 20fold, which is counteracted by protein S, overview, factor Xa and protein S interact with distinct sites on factor Va
-
heparin
-
heparin forms a complex with enzyme and inhibits optimal docking at Arg506 of substrate factor Va, instead promoting association between factor Va and enzyme at position Arg306
I2-D-Phe-Pro-Arg-CH2Cl
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-
Ile-Leu-Arg-CH2Cl
-
-
Ile-Pro-Arg-CH2Cl
-
-
Leupeptin-like inhibitor
-
-
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Macromolecular inhibitor
-
conversion of glutamic acid 192 to glutamine in activated protein C increases the reactivity towards macromolecular inhibitors
-
Monoclonal antibodies to human protein C
-
positions of some monoclonal antibody-binding sites in the protein C molecule
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Mutants of alpha1-antichymotrypsin with P1 arginine residue
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-
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N-(2-carboxyethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)argininamide
-
-
N-(4-carbamimidoylbenzyl)-2-[(3-cyclohexyl-L-alanyl)amino]-4-(piperidin-4-yl)butanamide
-
-
N-(4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2,2-dimethyl-4-oxobutyl)glycine
-
-
N-(4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-cyclohexyl-4-oxobutyl)glycine
-
-
N-(4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-4-oxobutyl)glycine
-
-
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-4-(aminomethyl)-N-(4-carbamimidoylbenzyl)phenylalaninamide
-
-
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-4-amino-N-(4-carbamimidoylbenzyl)-D-phenylalaninamide
-
-
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-N-(4-carbamimidoylbenzyl)-4-cyanophenylalaninamide
-
-
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-N-(4-carbamimidoylbenzyl)-D-phenylalaninamide
-
-
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-N-(4-carbamimidoylbenzyl)-D-tyrosinamide
-
-
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)-3-piperidin-4-ylalaninamide
-
-
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)-3-pyrrolidin-2-yl-D-alaninamide
-
-
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)-3-pyrrolidin-2-yl-L-alaninamide
-
-
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)argininamide
-
-
N-[(1S)-2-([1-[(4-carbamimidoylbenzyl)amino]-1-oxo-4-(piperidin-4-yl)butan-2-yl]amino)-1-cyclohexyl-2-oxoethyl]glycine
-
-
N-[(1S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]amino)-1-cyclohexyl-2-oxoethyl]glycine
-
the compound shows a 21fold selectivity for activated protein C over thrombin
N-[(2R)-2-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)-3-methylpentyl]glycine
-
-
N-[(2R)-2-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)-4-methylpentyl]glycine
-
-
N-[(2R)-2-benzyl-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-4-oxobutyl]glycine
-
-
N-[(2R)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-(cyclohexylmethyl)-4-oxobutyl]glycine
-
-
N-[(2R)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-ethyl-4-oxobutyl]glycine
-
-
N-[(2R)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-methyl-4-oxobutyl]glycine
-
-
N-[(2S)-1-([1-[(4-carbamimidoylbenzyl)amino]-1-oxo-4-(piperidin-4-yl)butan-2-yl]amino)-3-cyclohexyl-1-oxopropan-2-yl]glycine
-
the compound shows a 23fold selectivity for activated protein C over thrombin
N-[(2S)-1-[[(1S)-2-[(4-carbamimidoylbenzyl)amino]-2-oxo-1-(piperidin-4-yl)ethyl]amino]-3-cyclohexyl-1-oxopropan-2-yl]glycine
-
-
N-[(2S)-2-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)-3,3-dimethylbutyl]glycine
-
-
N-[(2S)-2-([1-benzyl-2-[(4-carbamimidoylbenzyl)amino]-2-oxoethyl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)amino]-1-(2,3-dihydro-1H-inden-2-yl)-2-oxoethyl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)amino]-1-(diphenylmethyl)-2-oxoethyl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-cyclopenta[a]naphthalen-2-yl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-cyclopenta[b]naphthalen-2-yl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-phenalen-2-yl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([6-[(4-carbamimidoylbenzyl)carbamoyl]-6,7-dihydro-5H-cyclopenta[b]pyridin-6-yl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([6-[(4-carbamimidoylbenzyl)carbamoyl]-6,7-dihydro-5H-cyclopenta[c]pyridin-6-yl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-2-([6-[(4-carbamimidoylbenzyl)carbamoyl]-6,7-dihydro-5H-dibenzo[a,c][7]annulen-6-yl]carbamoyl)-3-methylbutyl]glycine
-
-
N-[(2S)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-(1-methylethyl)-4-oxobutyl]glycine
-
-
N-[(2S)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-cyclohexyl-4-oxobutyl]glycine
-
-
N-[[1-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)cyclopentyl]methyl]glycine
-
-
N2-[(2S)-2-amino-2-cyclohexylacetyl]-N-(4-carbamimidoylbenzyl)argininamide
-
-
peptide VP311-325
-
a peptide comprising residues 311-325 in factor Va, potent inhibition of factor Va-dependent prothrombin activation by factor Xa in the absence of APC, the peptide also inhibits the inactivation of factor Va by APC by APC-dependent cleavage of both Arg506 and Arg306, thus inhbits cleavage of wild-type factor Va and of the mutant R306Q and R506Q, overview
-
Phe-Ala-Arg-CH2Cl
-
-
Phe-Phe-Arg-CH2Cl
-
-
Phe-Pro-Arg-chloromethylketone
phenylmethylsulfonyl fluoride
Platelet plasminogen activator inhibitor
-
reacts with the enzyme to yield both, an SDS-stable complex and a modified inhibitor
-
ProTac
-
a protein C activator isolated from snake venom
-
Protease nexin I
-
-
-
Protein C inhibitor
-
protein C inhibitor PCI
-
inhibition stimulated by heparin
-
protein S
-
the cofactor is active as free protein and in complex with C4b binding protein, the latter shows a less potent effect, activation up to 10fold, but the complex inhibits proteolysis at Arg506 by 3-4fold, overview
-
prothrombin
-
Tyr-Phe-Arg-CH2Cl
-
-
Val-Val-Arg-CH2Cl
-
-
Zn2+
-
Zn2+ enhances the binding of protein C/activated protein C to endothelial cell protein C receptor on endothelial cells by increasing the binding affinities. Zn2+ binding induces conformational changes in protein C/APC. Zn2+ binding to APC inhibits the amidolytic activity of APC, but the inhibition is reversed by Ca2+. Zn2+ increases the rate of APC generation on endothelial cells in the presence of physiological concentrations of Ca2+, but does not further enhance increased APC generation obtained in the presence of physiological concentrations of Mg2+ with Ca2+. Zn2+ has no effect on the anticoagulant activity of APC. Zn2+-mediated inhibition of APC amidolytic activity rather than the direct inhibition of protein C activation
[[(2R)-1-[[(2R)-1-[(4-carbamimidoylbenzyl)amino]-3-(naphthalen-1-yl)-1-oxopropan-2-yl]amino]-3-cyclohexyl-1-oxopropan-2-yl]amino]acetic acid
-
non-preferred name
[[(2R)-1-[[(2R)-1-[(4-carbamimidoylbenzyl)amino]-3-(naphthalen-2-yl)-1-oxopropan-2-yl]amino]-3-cyclohexyl-1-oxopropan-2-yl]amino]acetic acid
-
non-preferred name
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
certoparin
-
clinical LMWH enhances activity
-
cholesterol
-
in phosphatidylcholine/phosphatidylserine vesicles, cholesterol enhances Factor Va inactivation and the rate of cleavage by enzyme both at R506 and R306
dalteparin
-
clinical LMWH enhances activity
-
dermatan sulfate
enoxaparin
-
clinical LMWH enhances activity
factor Xa
-
stimulates factor Va cleavage at Arg306, but inhibits the cleavage at Arg506 20fold, overview, factor Xa and protein S interact with distinct sites on factor Va
-
glycosaminoglycan
-
enhances activity with factor V but not with factor Va as substrate
LMW heparin
-
enhances the anticoagulant action of activated protein C
-
nadroparin
-
clinical LMWH enhances activity
-
phosphatidylcholine
-
as phospholipid vesicles with 80% phosphatidylcholine and 20% phosphatidylserine, specific binding to the enzyme of anionic phospholipid vesicles passed over the protein C surface, defective phospholipid binding of mutant variants also resulted in severely impaired anticoagulant activity in protein C-deficient plasma
phosphatidylserine
-
as phospholipid vesicles with 80% phosphatidylcholine and 20% phosphatidylserine, specific binding to the enzyme of anionic phospholipid vesicles passed over the protein C surface, defective phospholipid binding of mutant variants also resulted in severely impaired anticoagulant activity in protein C-deficient plasma
Phospholipid
Phospholipids
-
-
polysulfated dermatan sulfate
-
more active than dermatan sulfate-derived oligosaccharide on basis of comparable molecular weight. Most active polysulfated dermatan sulfate has a molecular weight of 2749 and increases enzyme activty by about 230%
-
ProTac
-
protein S
-
tinzaparin
-
clinical LMWH enhances activity
-
vitamin K
-
dependent on
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.528
Benzyloxycarbonyl-Val-Gly-Arg
-
-
0.000196
cleavage of Arg306 in factor VaR506Q
-
-
-
0.00002
cleavage of Arg506 in membrane-bound factor Va
-
-
-
0.606
D-Ile-Pro-Arg
-
-
0.373
D-Phe-pipecolyl-Arg
-
-
0.505
D-Pro-Phe-Arg
-
-
0.259
D-Val-cyclohexyl-Ala-Arg
-
-
0.345
D-Val-Leu-Arg
-
-
0.0000197
Factor Va
-
pH 7.4, 22C
-
0.0001 - 0.000102
Factor VIIIa
-
0.43 - 0.9
Nalpha-benzoyl-L-arginine 4-nitroanilide
0.39 - 1.723
S-2288
0.0009 - 0.00098
S-2366
0.131 - 0.177
spectrozyme PCa
0.234 - 0.258
SpPCa
-
0.762
Toluene-p-sulfonyl-Gly-Pro-Arg
-
-
0.116
Toluene-p-sulfonyl-Gly-Pro-Lys
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
Benzyloxycarbonyl-Val-Gly-Arg
Homo sapiens
-
-
0.37
cleavage of Arg306 in factor VaR506Q
Homo sapiens
-
-
-
0.96
cleavage of Arg506 in membrane-bound factor Va
Homo sapiens
-
-
-
200
D-Ile-Pro-Arg
Homo sapiens
-
-
53
D-Phe-pipecolyl-Arg
Homo sapiens
-
-
31
D-Pro-Phe-Arg
Homo sapiens
-
-
1.9
D-Val-cyclohexyl-Ala-Arg
Homo sapiens
-
-
35
D-Val-Leu-Arg
Homo sapiens
-
-
0.395
Factor Va
Homo sapiens
-
pH 7.4, 22C
-
0.32
Nalpha-benzoyl-L-arginine 4-nitroanilide
Bos taurus
-
with Na+ or Cs+ as activating cation
70 - 78
S-2366
44 - 48
spectrozyme PCa
33.1 - 35
SpPCa
-
87
Toluene-p-sulfonyl-Gly-Pro-Arg
Homo sapiens
-
-
0.81
Toluene-p-sulfonyl-Gly-Pro-Lys
Homo sapiens
-
-
additional information
additional information
Homo sapiens
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20000
Factor Va
Homo sapiens
-
pH 7.4, 22C
3692
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028
N-(2-carboxyethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)argininamide
Homo sapiens
-
pH 7.4, 37C
0.0031
N-(4-carbamimidoylbenzyl)-2-[(3-cyclohexyl-L-alanyl)amino]-4-(piperidin-4-yl)butanamide
Homo sapiens
-
pH 7.4, 37C
0.044
N-(4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2,2-dimethyl-4-oxobutyl)glycine
Homo sapiens
-
-
0.033
N-(4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-cyclohexyl-4-oxobutyl)glycine
Homo sapiens
-
above
0.033
N-(4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-4-oxobutyl)glycine
Homo sapiens
-
above
0.0011
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-4-(aminomethyl)-N-(4-carbamimidoylbenzyl)phenylalaninamide
Homo sapiens
-
pH 7.4, 37C
0.00013
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-4-amino-N-(4-carbamimidoylbenzyl)-D-phenylalaninamide
Homo sapiens
-
pH 7.4, 37C
0.0038
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-N-(4-carbamimidoylbenzyl)-4-cyanophenylalaninamide
Homo sapiens
-
pH 7.4, 37C
0.00067
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-N-(4-carbamimidoylbenzyl)-D-phenylalaninamide
Homo sapiens
-
pH 7.4, 37C
0.00026
N-(carboxymethyl)-3-cyclohexyl-D-alanyl-N-(4-carbamimidoylbenzyl)-D-tyrosinamide
Homo sapiens
-
pH 7.4, 37C
0.0013
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)-3-piperidin-4-ylalaninamide
Homo sapiens
-
pH 7.4, 37C
0.044
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)-3-pyrrolidin-2-yl-D-alaninamide
Homo sapiens
-
above, pH 7.4, 37C
0.0056
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)-3-pyrrolidin-2-yl-L-alaninamide
Homo sapiens
-
pH 7.4, 37C
0.00047
N-(carboxymethyl)-3-cyclohexyl-L-alanyl-N-(4-carbamimidoylbenzyl)argininamide
Homo sapiens
-
pH 7.4, 37C
0.044
N-[(1S)-2-([1-[(4-carbamimidoylbenzyl)amino]-1-oxo-4-(piperidin-4-yl)butan-2-yl]amino)-1-cyclohexyl-2-oxoethyl]glycine
Homo sapiens
-
above, pH 7.4, 37C
0.0017
N-[(1S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]amino)-1-cyclohexyl-2-oxoethyl]glycine
Homo sapiens
-
pH 7.4, 37C
0.00112
N-[(2R)-2-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)-3-methylpentyl]glycine
Homo sapiens
-
-
0.00075
N-[(2R)-2-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)-4-methylpentyl]glycine
Homo sapiens
-
-
0.01125
N-[(2R)-2-benzyl-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-4-oxobutyl]glycine
Homo sapiens
-
-
0.0001
N-[(2R)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-(cyclohexylmethyl)-4-oxobutyl]glycine
Homo sapiens
-
-
0.00204
N-[(2R)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-ethyl-4-oxobutyl]glycine
Homo sapiens
-
-
0.00908
N-[(2R)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-methyl-4-oxobutyl]glycine
Homo sapiens
-
-
0.0092
N-[(2S)-1-([1-[(4-carbamimidoylbenzyl)amino]-1-oxo-4-(piperidin-4-yl)butan-2-yl]amino)-3-cyclohexyl-1-oxopropan-2-yl]glycine
Homo sapiens
-
pH 7.4, 37C
0.0031
N-[(2S)-1-[[(1S)-2-[(4-carbamimidoylbenzyl)amino]-2-oxo-1-(piperidin-4-yl)ethyl]amino]-3-cyclohexyl-1-oxopropan-2-yl]glycine
Homo sapiens
-
pH 7.4, 37C
0.00383
N-[(2S)-2-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)-3,3-dimethylbutyl]glycine
Homo sapiens
-
-
0.00071
N-[(2S)-2-([1-benzyl-2-[(4-carbamimidoylbenzyl)amino]-2-oxoethyl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.00035
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)amino]-1-(2,3-dihydro-1H-inden-2-yl)-2-oxoethyl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.033
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)amino]-1-(diphenylmethyl)-2-oxoethyl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
above
0.00025
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-cyclopenta[a]naphthalen-2-yl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.00928
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-cyclopenta[b]naphthalen-2-yl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.00043
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-phenalen-2-yl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.01091
N-[(2S)-2-([2-[(4-carbamimidoylbenzyl)carbamoyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.0011
N-[(2S)-2-([6-[(4-carbamimidoylbenzyl)carbamoyl]-6,7-dihydro-5H-cyclopenta[b]pyridin-6-yl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.0017
N-[(2S)-2-([6-[(4-carbamimidoylbenzyl)carbamoyl]-6,7-dihydro-5H-cyclopenta[c]pyridin-6-yl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.01265
N-[(2S)-2-([6-[(4-carbamimidoylbenzyl)carbamoyl]-6,7-dihydro-5H-dibenzo[a,c][7]annulen-6-yl]carbamoyl)-3-methylbutyl]glycine
Homo sapiens
-
-
0.0008
N-[(2S)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-(1-methylethyl)-4-oxobutyl]glycine
Homo sapiens
-
-
0.00082
N-[(2S)-4-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-cyclohexyl-4-oxobutyl]glycine
Homo sapiens
-
-
0.053
N-[[1-(2-[2-[(4-carbamimidoylbenzyl)carbamoyl]-2,3-dihydro-1H-inden-2-yl]-2-oxoethyl)cyclopentyl]methyl]glycine
Homo sapiens
-
-
0.0016
N2-[(2S)-2-amino-2-cyclohexylacetyl]-N-(4-carbamimidoylbenzyl)argininamide
Homo sapiens
-
pH 7.4, 37C
0.0011
[[(2R)-1-[[(2R)-1-[(4-carbamimidoylbenzyl)amino]-3-(naphthalen-1-yl)-1-oxopropan-2-yl]amino]-3-cyclohexyl-1-oxopropan-2-yl]amino]acetic acid
Homo sapiens
-
pH 7.4, 37C
0.00098
[[(2R)-1-[[(2R)-1-[(4-carbamimidoylbenzyl)amino]-3-(naphthalen-2-yl)-1-oxopropan-2-yl]amino]-3-cyclohexyl-1-oxopropan-2-yl]amino]acetic acid
Homo sapiens
-
pH 7.4, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57.3
-
purified native enzyme, amidolytic activity, pH 8.0, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.5
-
assay at
7.7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
anticoagulation assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
rheumatoid synovial fibroblasts
Manually annotated by BRENDA team
-
enzyme synthesis
Manually annotated by BRENDA team
-
breast cancer cells
Manually annotated by BRENDA team
-
an immortalized human monocytic cell line
Manually annotated by BRENDA team
additional information
-
inactive zymogen protein C is produced by endothelial cells and keratinocytes, secreted and activated on the cell surface by binding to endothelial protein C receptor and cleaved by thrombin bound to thrombomodulin
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
1 * 21000 + 1 * 35000, SDS-PAGE of reduced enzyme
41000
-
1 * 41000 + 1 * 21000, bovine protein C, SDS-PAGE of reduced protein, heavy and light chain are connected by a disulfide bond, cleavage of Arg12-Leu13 in the heavy chain releases a small activation peptide, MW 1400 and protein Ca
54300
-
bovine, protein C, amino acid and carbohydrate composition data, conversion to protein Ca by hydrolysis of a specific peptide bond in the amino-terminal region of the heavy chain between Arg14 and Ile15, giving rise to protein Ca, MW 52650 and an activation peptide, MW 1650
56000
-
x * 56000, SDS-PAGE
62000
-
x * 62000
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
side-chain modification
-
beta-hydroxylation of Asp71, and carboxylation of nine glutamic acid residues in the N-terminus
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant
-
native enzyme from bovine plasma by gel filtration, mannose affinity and Blue Sepharose chromatography
-
recombinant enzyme
-
recombinant wild-type and mutant enzymes from HEK-293 cell culture medium by anion exchange chromatography
-
use of the insolubilized inhibitor aprotinin for purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APCTPTGla chimera, much more potent anticoagulant than wild-type APC in plasma
-
expression in AV12-664 cells, activation with rat thrombomodulin/bovine thrombin complex
-
expression of Gla domainless Protein C GDPC andGDPC E80K by the RSV-PL4 expression/purification vector system in human 293 cells
-
expression of the mutant zymogen protein C(S360A) in HEK-293 cells
-
expression of wild-type an dmutant enzymes in HEK-293 cells
-
expression of wild-type and mutant enzymes in HEK-293 cells
-
expression of wild-type and mutant enzymes in HEK-293 cells, secretion to the medium
-
gene PROC, location on chromosome 1p13-14
-
gene PROC, location on on chromosome 2 (2q13q14)
-
mutant cloned into pcDNA 3.1(+)/Hygro vector and expressed in HEK-293 cells
-
protein C mutants prepared by PCR methods expressed in HEK293 cells
recombinant expression of the enzyme, co-expression with SEAP from a SEAP-protease activated receptor 3 fusion protein in HEK-293 cells with or without stable endothelial protein C receptor coexpression
-
stable, functional expression of wild-type and mutant enzymes in HEK-293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence of the APC cofactor, protein S, thrombomodulin, endothelial protein C receptor and a phospholipid surface are important for the expression of anticoagulant APC activity
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D167F/D172G
-
at saturating Ca2+ concentrations, the activation rates of the mutant and wild-type protein C by the thrombin-TM complex are comparable, but the mutant requires four-fold higher Ca2+ concentrations than wild-type APC to achieve half-maximal activation rates. When only thrombin is present, Ca2+ is not able to influence the activation of the D167F/D172G mutant, though Ca2+ effectively inhibits activation of wild-type protein C by thrombin
D222E
-
mutation of the Arg-Gly-Asp sequence abolishes both integrin binding and inhibition of neutrophil migration
D35T/D36A
-
site-directed mutagenesis, the mutant shows slightly increased factor Va proteolysis compared to the wild-type enzyme, the activation by protein S is reduced
D36A/L38D/A39V
-
site-directed mutagenesis, the mutant shows no activation by protein S
E149A
-
the cytoprotective effects of the APC mutant are severely diminished, despite a normal cleavage of PAR-1 and normal binding to EPCR. E149A-APC expresses only 6% of the anti-apoptotic activity of wild-type APC in a staurosporine-induced apoptosis model in endothelial cells and was unable to down-regulate IL-6 release in lipopolysaccharide treated U937 monocytes
E167A
-
site-directed mutagenesis, the surface loop residue mutation eliminates the cytoprotective signaling properties of APC without affecting its anticoagulant activity, inability of E167A to exhibit significant protective activity in response to TNF-alpha-induced inflammatory events in endothelial cells
E16D
-
site-directed mutagenesis, the mutation causes aberrant Ca2+ binding and Gla domain misfolding
E170A
-
site-directed mutagenesis, the surface loop residue mutation eliminates the cytoprotective signaling properties of APC without affecting its anticoagulant activity, inability of E170A to exhibit significant protective activity in response to TNF-alpha-induced inflammatory events in endothelial cells
E20A/V34M
-
the mutation is associated with thrombotic complications, despite the fact that carriers of these mutations have normal protein C antigen levels and APC amidolytic activity
E357Q
-
E357 is involved in binding of macromolecular substrates. Engineered E357Q-APC shows two to threefold improved FVa inactivation, but slightly reduced anticoagulant activity in plasma compared to wild-type APC
E7D
-
the mutation is associated with thrombotic complications, despite the fact that carriers of these mutations have normal protein C antigen levels and APC amidolytic activity
E80K
-
GDPC derivative
G216D
-
a naturally occuring mutation, the mutant shows impaired protease activity, while preserving the overall protein fold. Superposition of the integrin binding motifs in wild-type and mutant forms suggests that the interaction with integrin can still occur and thus the mutant is likely to retain its antiseptic function related to the neutrophyl integrin binding
H10Q/S11G/S12N/D23S/Q32E/N33D/H44Y
-
naturally occuring Gla-domain mutant, the mutant enzyme shows a higher anticoagulant effect compared to the wild-type enzyme, the combination with the B148 mutation in the serine protease domain even enhances the effect, overview
K174E
-
site-directed mutagenesis, the activation rate of the mutant by thrombin is 12fold faster than that observed for wild-type protein C in the presence of Ca2+, and unchanged in the absence of Ca2+. Thrombin does not stimulate activation of the protein C variant
K191A
-
Km- and kcat-value similar to wild-type, minor contribution to interaction with thrombin-thrombomodulin
K192A
-
Km- and kcat-value similar to wild-type, major contribution to interaction with thrombin-thrombomodulin
K217A
-
Km- and kcat-value similar to wild-type, minor contribution to interaction with thrombin-thrombomodulin
K218A
-
Km- and kcat-value similar to wild-type, minor contribution to interaction with thrombin-thrombomodulin
K37S/K38Q/K39Q
-
created by site-directed in vitro mutagenesis
K37S/K38Q/K39Q/K62N/K63D
-
created by site-directed in vitro mutagenesis
K78A
prepared by PCR methods
L8Q
-
mutant variants L8Q and R9H show reduced affinity for EPCR and can contribute to the reduced anticoagulant activity
N33S/V34S/D35T/D36A/L38D/A39V
-
site-directed mutagenesis, the mutant shows slightly increased factor Va proteolysis compared to the wild-type enzyme, no activation by protein S
P168V
-
at saturating Ca2+ concentrations, the activation rates of the mutant and wild-type protein C by the thrombin-TM complex are comparable, but the mutant requires four-fold higher Ca2+ concentrations than wild-type APC to achieve half-maximal activation rates. When only thrombin is present, Ca2+ is not able to influence the activation of the P168V mutant, though Ca2+ effectively inhibits activation of wild-type protein C by thrombin
R15G
-
the mutation leads to increased thrombotic tendency
R15W
-
the mutation leads to increased thrombotic tendency
R177E
-
site-directed mutagenesis, the activation rate of the mutant by thrombin is 12fold faster than that observed for wild-type protein C in the presence of Ca2+, and unchanged in the absence of Ca2+. Thrombin does not stimulate activation of the protein C variant
R178E
-
site-directed mutagenesis, the activation rate of the mutant by thrombin is 12fold faster than that observed for wild-type protein C in the presence of Ca2+, and unchanged in the absence of Ca2+. Thrombin does not stimulate activation of the protein C variant
R229A
-
Km- and kcat-value similar to wild-type, major contribution to interaction with thrombin-thrombomodulin
R229A/R230A/K191A/K192A/K193A
-
site-directed mutagenesis, construction of an APC protease domain mutant, 5A-APC, the mutant has minimal anticoagulant activity but normal cytoprotective activities that are dependent on endothelial protein C receptor and protease-activated receptor-1 as compared to the wild-tpe enzyme, activation of thrombin activable fibrinolysis inhibitor is essentially unaffected by 5A-APC due to its low anticoagulant activity, a 1000fold higher concentration of 5A-APC is required to give a factor Va inactivation pattern similar to that of recombinant wild-type APC
R230A
-
Km- and kcat-value similar to wild-type, major contribution to interaction with thrombin-thrombomodulin
R312A
-
Km- and kcat-value similar to wild-type, minor contribution to interaction with thrombin-thrombomodulin
R67C/R82C
-
site-directed mutagenesis, construction of a protein C variant in which an engineered disulfide bond between two beta-sheets stabilizes the functionally critical Ca2+-binding 70-80 loop of the molecule. The 70-80 loop of this mutant no longer binds Ca2+, and the activation of the mutant by thrombin is enhanced 60-80fold independently of thrombomodulin, the anticoagulant activity of the activated protein C mutant is nearly eliminated. The endothelial protein C receptor- and protease activated receptor-1-dependent protective signaling properties of the mutant are minimally altered compared to the wild-type enzyme. The mutant loses its ability to interact with the procoagulant cofactors but not with the protective signaling molecules. The binding of EPCR is 2fold reduced compared to the wild-type enzyme
R74A
prepared by PCR methods
R74E/R75E/K78E
triple mutant, Gla-domainless form of APC
R74Q
-
created by site-directed in vitro mutagenesis
R75A
prepared by PCR methods
R9H
-
mutant variants L8Q and R9H show reduced affinity for EPCR and can contribute to the reduced anticoagulant activity
S11G/S12N
-
site-directed mutagenesis, the mutant shows slightly increased factor Va proteolysis compared to the wild-type enzyme
S190A
-
Km- and kcat-value similar to wild-type, minor contribution to interaction with thrombin-thrombomodulin
S195A
-
site-directed mutagenesis, inactive mutant
S360C
-
site-directed mutagenesis, the active site residue mutant shows no amidolytic activity
W231A
-
Km- and kcat-value similar to wild-type, minor contribution to interaction with thrombin-thrombomodulin
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
at therapeutically relevant concentrations, activated protein C suppresses the release of interleukin-6 from stimulated human neutrophils and inhibited chemotaxis, without affecting the respiratory burst, apoptosis, and expression of other key cytokines. These effects are likely to be cell-type specific but may have implications for treatment of patients with activated protein C
medicine
pharmacology