Any feedback?
Information on EC 3.4.21.27 - coagulation factor XIa
for references in articles please use BRENDA:EC3.4.21.27Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.27 coagulation factor XIaSpecify your search results
Word Map
- 3.4.21.27
- bleeding
- thrombin
- clot
- platelet
- thrombosis
-
anticoagulant
- prothrombin
- kallikrein
- kininogen
- prekallikrein
- viii
-
hemostasis
- venous
- fibrinogen
- antithrombin
- zymogen
-
fibrinolysis
-
procoagulant
- fibrin
- willebrand
-
antithrombotic
- hemophilia
- thromboembolism
- plasmin
-
ashkenazi
- fxiia
-
hageman
- coagulopathy
-
amidolytic
- diathesis
-
haemostat
- thrombophilias
- leiden
-
jewish
-
antifibrinolytic
- kaolin
-
proline-specific
-
thrombin-activatable
- meningosepticum
-
fletcher
- c1-inhibitor
-
thromboelastometry
- drug development
-
tenase
- medicine
-
basque
- menorrhagia
- desmopressin
-
tranexamic
-
proline-containing
- tafi
-
recalcified
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Selective cleavage of Arg-/-Ala and Arg-/-Val bonds in factor IX to form factor IXa
Synonyms
factor xi, fxia, factor xia, prolyl endopeptidase, coagulation factor xi, activated factor xi, coagulation factor xia, activated fxi, plasma thromboplastin antecedent, blood coagulation factor xia, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
activated blood-coagulation factor XI
-
-
-
-
activated plasma thromboplastin antecedent
-
-
-
-
blood coagulation factor XIa
blood-coagulation factor XI, activated
-
-
-
-
blood-coagulation factor XIa
-
-
-
-
coagulation factor XI
coagulation factor XIa
factor XI
factor XIa
FXI
FXIa
plasma thromboplastin antecedent
-
-
-
-
prolyl endopeptidase
-
-
-
-
PTA
-
-
-
-
blood coagulation factor XIa
-
-
-
-
factor XI
-
factor XIa
-
-
FXI
-
-
-
-
FXI
-
FXIa
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Selective cleavage of Arg-/-Ala and Arg-/-Val bonds in factor IX to form factor IXa
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37203-61-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
-
-
-
-
?
beta-2-glycoprotein I + H2O
clipped beta-2-glycoprotein I
-
cleavage at Lys317-Thr318
-
-
?
Boc-Glu(OBzl)-Ala-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Glu(OBzl)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
substrate S-2288
-
-
?
factor V + H2O
activated factor V + ?
-
fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
-
-
?
factor VIII + H2O
activated factor VIII + ?
-
fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
-
-
?
Fibrinogen + H2O
?
-
Aalpha-chain and Bbeta-chain, gamma-chain after prolonged incubation
-
-
?
Gly-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Glu-L-Glu-L-Pro-L-Arg-4-nitroanilide + H2O
L-Glu-L-Glu-L-Pro-L-Arg + 4-nitroaniline
-
S-2366
-
-
?
L-pyro-Glu-Pro-Arg-4-nitroanilide + H2O
L-pyro-Glu-Pro-Arg + 4-nitroaniline
i.e. S-2366
-
-
?
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroGlu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroglutamyl-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-7-amido-4-methylcoumarin + H2O
L-pyroglutamyl-L-prolyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
?
-
substrate S-299
-
-
?
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-arginine-p-nitroanilide + H2O
N-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-Cbz-D-arginylglycyl-L-arginyl-4-nitroanilide + H2O
N-Cbz-D-arginylglycyl-L-arginine + 4-nitroaniline
-
-
-
-
?
platelet glycoprotein 1balpha + H2O
?
binding to the A3 domain of FXI
-
-
?
prochemerin chem163S + H2O
chemerin chem162R + chermerin chem158K
-
prochemerin is activated by a series of C-terminal proteolytic cleavages resulting in diverse chemerin forms with different levels of activity
-
-
?
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tissue factor pathway inhibitor + H2O
?
-
the cleavage of the protein occurs between the Kunitz (K)1 and K2 domains (Lys86/Thr87) and at the active sites of the K2 (Arg107/Gly108) and K3 (Arg199/Ala200) domains
-
-
?
Z-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
factor IX + H2O
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
?
factor IX + H2O
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
?
factor IX + H2O
activated factor IX + ?
-
-
683239, 684078, 717416, 717844, 718042, 718045, 752615, 752757, 752995, 753069, 754510, 754516, 755585
-
-
?
factor IX + H2O
activated factor IX + ?
-
model for factor IX activation in which FXIa binds to activated platelets by one chain of the dimer, while binding to factor IX through the other
-
?
factor IX + H2O
activated factor IX + ?
factor XIa has a role in the intrinsic pathway of coagulation, and plays a significant role in venous thrombosis
-
-
?
factor IX + H2O
activated factor IX + ?
-
factor XIa is essential for the optimal activation of FIX
-
-
?
factor IX + H2O
activated factor IX + ?
-
two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX
-
-
?
factor IX + H2O
activated factor IX + ?
cleavage at Ala145 and Ala180
-
-
?
factor IX + H2O
activated factor IX + ?
-
cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type and mutant substrate, overview
-
-
?
factor IX + H2O
activated factor IX + ?
-
cleavage of Arg145-Ala146, and Arg180-Val181, macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX-activation, mechanisms of activation, overview
-
-
?
factor IX + H2O
activated factor IX + ?
natural cleavage sites on FIX performed by FXIa, overview
-
-
?
factor IX + H2O
activated factor IX + ?
FXI is converted to the active protease by cleavage of the Arg369-Ile370 bond on each subunit. This converts the catalytic domains to the active forms, and unmasks exosites on the apple domains required for FIX binding
-
-
?
factor IX + H2O
factor IXa + ?
-
-
-
-
?
factor IX + H2O
factor IXa + ?
-
after binding to factor XIa, factor IX undergoes a single cleavage to form the intermediate factor IXalpha. FIXalpha then rebinds to the A3 domain to undergo a second cleavage, generating factor IXalphabeta
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
?
pro-HGF + H2O
?
-
HGF i. e. hepatocyte growth factor, pro-HGF is processed by cleavage at two sites: Arg494-Val 495 and Arg424-His425. Cleavage at Arg424-His425 is independent of a prior cleavage at the primary kinetically preferred Arg 494-Val495 site. The mutant substrate pro-HGF(R424A/R494E) is completely resistant to cleavage
-
?
pro-HGF + H2O
?
-
the enzyme may regulate processes that involve the HGF/c-Met pathway, such as tissue repair and angiogenesis
-
?
additional information
?
-
-
specific and saturable zinc-dependent FXIa binding is demonstrated to 250 sites per activated platelet and 6.5 sites per umbilical vein endothelial cell. No binding to HEK293 cells is detected
-
?
additional information
?
-
a conformational transition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain zymogen factor XI platelet binding site and exposes the factor XIa platelet binding site within the catalytic domain possibly comprising residues Cys527-Cys542
-
-
?
additional information
?
-
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, overview
-
-
?
additional information
?
-
FXI contains 4 apple domains that form a disk structure with extensive interfaces at the base of the catalytic domain. Binding of FXI to platelets requires residues in the FXI A3 domain. Platelets bind and spread on glass coated with FXI
-
-
?
additional information
?
-
FXI is a homodimer, with each subunit containing four apple domains and a protease domain: the apple domains form a disk structure with binding sites for platelets
-
-
?
additional information
?
-
-
platelets bind and spread on glass coated with FXI. Platelets from ApoER2-deficient mice do not bind FXI
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
factor V + H2O
activated factor V + ?
-
fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
-
-
?
factor VIII + H2O
activated factor VIII + ?
-
fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
-
-
?
pro-HGF + H2O
?
-
the enzyme may regulate processes that involve the HGF/c-Met pathway, such as tissue repair and angiogenesis
-
?
prochemerin chem163S + H2O
chemerin chem162R + chermerin chem158K
-
prochemerin is activated by a series of C-terminal proteolytic cleavages resulting in diverse chemerin forms with different levels of activity
-
-
?
tissue factor pathway inhibitor + H2O
?
-
the cleavage of the protein occurs between the Kunitz (K)1 and K2 domains (Lys86/Thr87) and at the active sites of the K2 (Arg107/Gly108) and K3 (Arg199/Ala200) domains
-
-
?
factor IX + H2O
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
?
factor IX + H2O
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
?
factor IX + H2O
activated factor IX + ?
-
-
-
-
?
factor IX + H2O
activated factor IX + ?
factor XIa has a role in the intrinsic pathway of coagulation, and plays a significant role in venous thrombosis
-
-
?
factor IX + H2O
activated factor IX + ?
-
factor XIa is essential for the optimal activation of FIX
-
-
?
factor IX + H2O
activated factor IX + ?
-
two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX
-
-
?
factor IX + H2O
factor IXa + ?
-
-
-
-
?
factor IX + H2O
factor IXa + ?
-
after binding to factor XIa, factor IX undergoes a single cleavage to form the intermediate factor IXalpha. FIXalpha then rebinds to the A3 domain to undergo a second cleavage, generating factor IXalphabeta
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
fondaparinux pentasaccharide, all catalytic domains exhibit similar inhibition to catalytic domain-wild-type by antithrombin in the absence and presence of fondaparinux
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Zn2+
in the presence of zinc ions, kininogen is required for optimal FXI binding to GP1b on activated platelets in suspension, enhancing the binding stoichiometry by approximately 2fold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2,4-dibromo-3-[[(4-carbamimidamidobutyl)carbamoyl]oxy]-6-hydroxyphenyl)acetic acid
-
(2,4-dibromo-6-[[(4-carbamimidamidobutyl)carbamoyl]oxy]-3-hydroxyphenyl)acetic acid
-
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
-
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
-
(2S)-2-([[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]amino)-N-[(2S)-1-[[(2S)-5-carbamimidamido-1-oxo-1-(1,3-thiazol-2-yl)pentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]-2-(4-hydroxyphenyl)ethanamide
-
(2S)-2-([[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]amino)-N-[(2S)-1-[[(2S)-5-carbamimidamido-1-oxo-1-(1,3-thiazol-2-yl)pentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]-2-(pyridin-3-yl)ethanamide
-
(3R)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
-
(3R)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
-
(3S)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
-
(3S)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
-
(4S,7S)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,12,13,14,15-dodecahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
-
-
(4S,7S,10S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-10-phenyl-4,5,7,8,10,11,14,15-octahydro-1H-[1,4,7]triazacyclohexadecino[10,9-b]indole-3,6,9(2H)-trione
-
-
(4S,7S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,14,15-decahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
-
-
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
-
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5,6,7,8-tetrahydroisoquinoline-6-carboxamide
-
-
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]isoquinoline-6-carboxamide
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2,6-difluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2-fluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chlorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-fluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methoxybenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methylbenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[2-(aminomethyl)-5-chlorobenzyl]urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(trifluoromethyl)benzyl]urea
-
-
2'-[(6-carbamimidoyl-1-ethyl-1H-indol-3-yl)methyl]-4-methyl-5'-[[(5-methylpyrazin-2-yl)methyl]carbamoyl]biphenyl-2-carboxylic acid
-
2,4-dibromo-3-([(4-carbamimidamidobutyl) carbamoyl]oxy)-6-hydroxyphenyl acetic acid
clavatadine A
2-(2-amino-2-oxoethyl)-3,5-dibromo-4-hydroxyphenyl (4-carbamimidamidobutyl)carbamate
clavatadine B
2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-L-arginyl-L-valyl-L-arginyl)-1,3-thiazole
-
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N5-carbamoyl-L-ornithyl-L-valyl-L-arginyl)-1,3-thiazole
-
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
3'-[(2S,4R)-6-carbamimidoyl-4-methyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]-4-carbamoyl-5'-[(3-methylbutanoyl)amino]biphenyl-2-carboxylic acid
-
3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1,2-benzoxazole-6-carboxamide
-
-
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1H-indazole-6-carboxamide
-
-
3-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
3-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(pyridin-3-yl)-L-alanyl]amino]benzoic acid
-
-
3-[[N2-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(pyrazin-2-ylmethyl)-L-asparaginyl]amino]benzoic acid
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N,N-dimethylbenzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N-methylbenzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-bromo-1H-imidazol-4-yl)-benzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-chloro-1H-imidazol-4-yl)-benzamide
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-fluoro-1H-imidazol-4-yl)-benzamide
-
4-(2-(S-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzoic acid
-
4-[(N-[(2E)-3-[2-(aminomethyl)-5-chlorophenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
4-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
4-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-tryptophyl)amino]benzoic acid
-
-
4-[(N2-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[2-(morpholin-4-yl)ethyl]-L-asparaginyl)amino]benzoic acid
-
-
4-[[(2S)-2-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-4-(methylsulfonyl)butanoyl]amino]benzoic acid
-
-
4-[[N-[(2E)-3-[3-chloro-2-fluoro-6-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(1-ethyl-5-methyl-1H-pyrazol-3-yl)-L-alanyl]amino]benzoic acid
-
-
4-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(thiophen-2-yl)-L-alanyl]amino]benzoic acid
-
-
5-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]thiophene-2-carboxylic acid
-
-
5-[[3-(ethoxycarbonyl)-5-hydroxy-6-methoxy-1-benzofuran-2-yl]methoxy]-6-methoxy-2-methyl-1-benzofuran-3-carboxylic acid
-
-
amyloid beta-precursor protein Kunitz domain
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
-
decasodium 1,2,3,4,6-pentakis-O-[3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
-
complete inhibition at 1 mg/ml
decasodium 1,2,3,4,6-pentakis-O-[4-hydroxy-3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
-
complete inhibition at 0.2 mg/ml
diisopropylfluorphosphate
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
disodium 3-([[3,5-dicyano-6-nitro-4-(4-phenoxyphenyl)pyridin-2-yl]sulfanyl]acetyl)benzene-1,2-diyl disulfate
-
-
disodium 4-[[3-(1,3-dioxo-5-[[4-(sulfonatooxy)phenyl]carbamoyl]-1,3-dihydro-2H-isoindol-2-yl)benzoyl]amino]phenyl sulfate
-
-
ethyl 2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
ethyl 2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
ethyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-10-methyl-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecine-2-carboxylate
-
-
ethyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-15-[(methoxycarbonyl)amino]-2,3,4,5,6,7-hexahydro-1H-8,12-(metheno)-1,9-benzodiazacyclotetradecine-2-carboxylate
-
-
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]leucinate
-
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]phenylalaninate
-
ethyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-1,6,7,9-tetrahydro-11,8-(azeno)-2,9-benzodiazacyclotridecin-2(3H)-yl]acetate
-
-
fractionated heparin of 64 disaccharide units
-
70-80% saturable maximal inhibition at 37°C
-
methyl (4-[2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[2-[(benzyl[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)methyl]-5-chloro-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([N-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(1-methyl-1H-pyrazol-3-yl)-L-alanyl]amino]phenyl)carbamate
-
-
methyl 2-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino][1,2,4]triazolo[1,5-a]pyridine-6-carboxylate
-
-
methyl 4-(2-((S)-1-(trans-4-(aminomethyl)-cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-benzoate
-
methyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecine-2-carboxylate
-
-
methyl [(10S)-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
-
methyl [(10S)-13-chloro-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
-
methyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-10-methyl-2,3,6,7-tetrahydro-9H-11,8-(azeno)-1,9-benzoxazacyclotridecin-14-yl]carbamate
-
-
methyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-10-methyl-2-oxo-2,3,6,7-tetrahydro-1H-8,12-(metheno)-1,9,11-benzotriazacyclotetradecin-15-yl]carbamate
-
-
methyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2,2-dioxido-1,6,7,9-tetrahydro-3H-11,8-(azeno)-2,1,9-benzothiadiazacyclotridecin-14-yl]carbamate
-
-
methyl [(5S)-2-chloro-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,12,13,14,15-hexahydro-3H-1,4-(azeno)-7,11-(metheno)-3-benzazacycloheptadecin-17-yl]carbamate
-
-
methyl [(5S)-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,11,12,13,14-hexahydro-3H-1,4-(azeno)-7,10-etheno-3-benzazacyclohexadecin-16-yl]carbamate
-
-
methyl [(7E)-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3,5,6,9,10,11-hexahydro-1,4-(azeno)-3-benzazacyclotridecin-13-yl]carbamate
-
-
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
-
methyl [(9S)-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
-
methyl [1-(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)-1,2,3,4-tetrahydroquinolin-6-yl]carbamate
-
-
methyl [10-chloro-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-(trifluoromethyl)-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [2-(4-chloro-1-methyl-1H-pyrazol-3-yl)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-10-methyl-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-(3-methyloxetan-3-yl)-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3,3-difluoro-4-oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,5,9-benzotriazacyclotridecin-14-yl]carbamate
-
-
N-(3-amino-1H-indol-6-yl)-Nalpha-([[5-chloro-2-(1H-tetrazol-1-yl)phenyl]sulfinyl]acetyl)-L-phenylalaninamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1-(3-aminopropyl)cyclohexanecarboxamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2,6-difluoro-4-methoxybenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methoxybenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methylbenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)-2-fluorobenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)benzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylbenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5-chloro-2-fluorobenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-pyrazol-1-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(4H-1,2,4-triazol-4-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]benzene-1,4-dicarboxamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2,2-dimethylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(2,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(4-chlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorophenyl)sulfonyl]amino]methyl)-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(4-fluorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylacetyl)amino]methyl]-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylcarbonyl)amino]methyl]-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(phenylcarbamoyl)amino]methyl]-L-phenylalaninamide
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]propyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(1S)-2-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]amino]-1-cyclohexyl-2-oxoethyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-carboxamide
-
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-3-oxo-3,4-dihydro-2H-1,4-benzothiazine-7-carboxamide
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-4-hydroxy-2-oxo-1,2,3,4-tetrahydroquinoline-6-carboxamide
-
-
N-[(3,4-dichlorobenzyl)carbamoyl]-L-leucyl-N-[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]-L-phenylalaninamide
-
N-[2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]-Na-(imidazo[1,2-a]pyrimidin-2-ylcarbonyl)-L-phenylalaninamide
-
-
N-[2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]-Nalpha-(1H-indazol-3-ylcarbonyl)-L-phenylalaninamide
-
-
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-(pent-4-enoylamino)acetyl]-L-leucinamide
-
-
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-[[(2S)-2-phenylpent-4-enoyl]amino]acetyl]-L-leucinamide
-
-
N2-(benzylcarbamoyl)-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
N2-acetyl-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N1-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-aspartamide
-
N2-[[1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
Na-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-fluoro-N-[4-(1H-tetrazol-5-yl)phenyl]-L-phenylalaninamide
-
-
Na-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[4-(1H-tetrazol-5-yl)phenyl]-L-phenylalaninamide
-
-
Na-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N2-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tyrosinamide
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(1,2,3,4-tetrahydroisoquinolin-6-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(1-oxo-2,3-dihydro-1H-isoindol-5-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(2-oxoazepan-3-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(6-fluoro-1,3-benzothiazol-2-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[4-[(methoxycarbonyl)amino]cyclohexyl]-L-phenylalaninamide
-
-
Nalpha-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tryptophanamide
-
protease nexin-2
highly specific and potent inhibitor of FXIa, is about 775fold more potent than basic pancreatic trypsin inhibitor in FXIa inhibition, provides single-step slow equilibration inhibition
-
sodium 2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-3-(methoxycarbonyl)-1-benzofuran-5-yl sulfate
-
-
sodium 2-[[(3-carboxy-6-methoxy-2-methyl-1-benzofuran-5-yl)oxy]methyl]-3-(ethoxycarbonyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-(propan-2-yloxy)-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-6-methoxy-2-[([6-methoxy-2-methyl-3-[(prop-2-en-1-yloxy)carbonyl]-1-benzofuran-5-yl]oxy)methyl]-1-benzofuran-5-yl sulfate
-
-
sodium 6-ethoxy-3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-1-benzofuran-5-yl sulfate
-
most potent inhibitor
sodium 6-methoxy-3-(methoxycarbonyl)-2-([[6-methoxy-3-(methoxycarbonyl)-2-methyl-1-benzofuran-5-yl]oxy]methyl)-1-benzofuran-5-yl sulfate
-
-
trans-4-(aminomethyl)-N-((S)-1-(4-(3-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-1-(4-(4-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-1-(5-oxo-1-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-2-phenylethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(2-phenyl-1H-imidazol-4-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-1,2,4-triazol-5-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-pyrazol-5-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-(4-sulfamoylphenyl)-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(5-phenyloxazol-2-yl)ethyl)cyclohexanecarboxamide
-
trans-4-(aminomethyl)-N-[1-(1-methyl-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-2-phenylpyridin-4-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-5-phenylpyridin-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(5-chloro-4-phenyl-1H-imidazol-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(5-fluoro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-amino-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-chloro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-hydroxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-methoxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(biphenyl-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-[6-(methylamino)-4-phenylpyridin-2-yl]-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(2-phenylpyridin-4-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyrimidin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(5-phenylpyridin-3-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyrimidin-4-yl)ethyl]cyclohexanecarboxamide
-
-
trans-N-((S)-1-(4-(3-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
reversible enzyme inhibition
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-fluoro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-((S)-1-(4-(4-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylcyclohexanecarboxamide
-
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]cyclohexane-1,4-dicarboxamide
-
-
trans-N-[1-[3-(3-amino-1H-indazol-6-yl)phenyl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)-6-oxo-1,6-dihydropyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)pyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[5-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
-
-
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
-
4-aminobenzamidine
-
a reversible serine protease inhibitor, competitive versus substrate S-2366, noncompetitive versus substrate factor IX, inhibition of wild-type enzyme and recombinant peptide FXI/E361-V607
4-aminobenzamidine
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-3-oxo-3,4-dihydro-2H-1,4-benzothiazine-7-carboxamide
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-3-oxo-3,4-dihydro-2H-1,4-benzothiazine-7-carboxamide
-
-
protease nexin 2
-
the major interactions required for factor XIa inhibition are localized to the catalytic domain of factor XIa and the Kunitz domain of protease nexin II
-
protease nexin 2
-
activated platelet surface has littlke or no direct effect on the rate of factor IX activation by factor Xia and the reaction proceeds at uninhibited rates when protease nexin 2 is present. Factor Xia-catalyzed FIX activation is completely inhibited by protease nexin 2 in solution or in the presence of umbilical vein endothelial cells
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
-
-
additional information
the recombinant catalytic domain Ile370-Val607 of FXIa inhibits the binding of factor XIa to the platelets with a Ki of 3.5 nM, whereas the recombinant factor XI heavy chain does not
-
additional information
inhibitor design and synthesis, overview, inhibitor in vitro anticoagulant activity in human plasma
-
additional information
-
inhibitor design and synthesis, overview, inhibitor in vitro anticoagulant activity in human plasma
-
additional information
heparin accelerates inhibition of factor XIa. Heparin enhances antithrombin inhibition of catalytic domain-wild-type 212fold, but only 37-94fold for catalytic domain mutants
-
additional information
Arg184 may be part of a switch that holds FXI in an inactive conformation in the zymogen
-
additional information
-
not inhibited by unfractionated heparin, enoxaparin, fondaparinux, sucrose octasulfate, chondroitin sulfate A, dermatan sulfate, and chondroitin sulfate C
-
additional information
-
potent activated factor VII inhibition with insect-derived serine protease inhibitor, but this protein is only 10fold selective over activated factor X. Inhibition by FXI neutralizing antibodies, which allow preexisting activated factor XI to remain active
-
additional information
-
a monoclonal antibody against FXI or activated factor XI reduces thrombus formation in balloon-injured iliac arteries
-
additional information
-
ketoarginine-based peptidomimetics are irreversible inhibitors of actived factor XI and form a covalent bond to the catalytic serine of the enzyme. Intravenous infusion is efficacious in a rat model of venous thrombosis. A pyridyl analog in a rat mesenteric bleeding model at a 4fold efficacious dose does not alter bleeding time
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activated factor IX
autoactivation, cleavage of FXI at the Arg369-Ile370 bond. activated factor IX is part of a feedback loop that sustains thrombin generation through FIX activation to consolidate coagulation
-
Protein disulfide isomerase
-
reduction of the enzyme by protein disulfide isomerase enhances its cleavage activity
-
activated factor XII
FXI activation proceeds through an intermediate with only one activated submit
-
activated factor XII
-
activated factor XII-mediated activation of FXI appears to play a central role in formation of pathologic thrombi in murine thrombosis models
-
desmopressin
increase of both FXI activity (up to 31%) and antigen levels 60 min after infusion. Also contradictory results with a lack of rise of FXI levels after infusion
Factor XII
-
FXI is activated by factor XII during ischemia reperfusion injury and within the growing thrombus according to the classical intrinsic pathway cascade
-
thrombin
activated factor V is a cofactor for the activation of factor XI by thrombin. Depletion of factor V, or the addition of activated protein C, decreases the activation of the intrinsic pathway by thrombin in plasma. Factor XI binds to factor V with multiple binding sites. Addition of FVIIIa, kininogen, or protein S does not influence the formation of activated factor XI
-
thrombin
FXI activation proceeds through an intermediate with only one activated submit
-
thrombin
thrombin generated early in coagulation by the tissue factor pathway activates FXI creating a positive feedback loop that sustains coagulation following inactivation of the factor VIIa/tissue factor complex by tissue factor pathway inhibitor
-
thrombin
-
activates FXI. FXI activation by thrombin is enhanced by charged substances, such as dextran sulfate or heparin. Thrombin binds to the A1 domain of FXI, with residues Glu66, Lys83, and Gln84 forming part of the binding site. The dimer is required for optimal FXI activation by thrombin
-
additional information
-
activation of factor XI by thrombin and autoactivation to factor XIa
-
additional information
FXI monomers are activated poorly, dimeric form is needed for activation. As FXI lacks a Gla domain, the dimeric structure may represent an alternative solution to the problem of tethering a prothrombotic molecule to a cellular surface in flowing blood in the vicinity of a wound
-
additional information
platelets may play a role in FXI activation. FXI binding to platelets is not enhanced by kininogen
-
additional information
-
in blood challenged with low concentrations of tissue factor, factor XI can be activated independently of factor XII
-
additional information
-
antibody 14E11 exerts an inhibitory effect on fXI activation, but not fXIa activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
D-Ile-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
0.0003
factor IX
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.205
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.268
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.292
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.315
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.336
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.339
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.383
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.4
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.525
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.538
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.603
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.828
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.852
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.552
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A/R171A/R173A mutant
0.655
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A mutant
0.757
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-wild type
0.764
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K179A mutant
0.81
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R173A mutant
0.812
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R171A mutant
0.829
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K175A mutant
0.993
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-R37Q mutant
0.26
pyroGlu-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of isolated subunits with each one active site, stoichiometry of FIX and FIXalphabeta binding to FXIa, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
110.2
D-Ile-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
0.2
factor IX
-
in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
kcat less than 0.2 s-1, mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.2
factor IX
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.73
factor IX
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
5.8
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
7
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
8
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
14
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
21
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
29
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
30
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
42
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
58
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
86
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
95
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
95
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
201
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
98
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A mutant
115
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K170A/R171A/R173A mutant
115
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R171A mutant
116
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K179A mutant
117
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-K175A mutant
117
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-R173A mutant
119
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
fXIa-catalytic domain-wild type
0.268
pyroGlu-Pro-Arg-4-nitroanilide
-
pH 7.4, 37°C, recombinant wild-type enzyme
145
pyroGlu-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000005
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
at 25°C, pH not specified in the publication
0.0000012
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
at 25°C, pH not specified in the publication
0.00000215
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5,6,7,8-tetrahydroisoquinoline-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000019
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]isoquinoline-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000023
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2,6-difluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000057
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2-fluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000054
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chlorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000031
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-fluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000075
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methoxybenzyl)urea
-
at 25°C, pH not specified in the publication
0.000053
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methylbenzyl)urea
-
at 25°C, pH not specified in the publication
0.0000058
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[2-(aminomethyl)-5-chlorobenzyl]urea
-
at 25°C, pH not specified in the publication
0.00024
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(trifluoromethyl)benzyl]urea
-
at 25°C, pH not specified in the publication
0.000275
2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
at pH 7.4 and 37°C
0.00015
2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
at pH 7.4 and 37°C
0.0000002
3'-[(2S,4R)-6-carbamimidoyl-4-methyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]-4-carbamoyl-5'-[(3-methylbutanoyl)amino]biphenyl-2-carboxylic acid
at pH 7.4 and 37°C
0.0011
3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
at pH 7.4 and 37°C
0.000125
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1,2-benzoxazole-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000058
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1H-indazole-6-carboxamide
-
at 25°C, pH not specified in the publication
0.00286
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N,N-dimethylbenzamide
at pH 7.4 and 37°C
0.00035
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N-methylbenzamide
at pH 7.4 and 37°C
0.00003
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
at pH 7.4 and 37°C
0.000009
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-bromo-1H-imidazol-4-yl)-benzamide
at pH 7.4 and 37°C
0.000004
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-chloro-1H-imidazol-4-yl)-benzamide
at pH 7.4 and 37°C
0.00003
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-fluoro-1H-imidazol-4-yl)-benzamide
at pH 7.4 and 37°C
0.00059
4-(2-(S-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzoic acid
at pH 7.4 and 37°C
0.000627
basic pancreatic trypsin inhibitor
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.0000041
basic pancreatic trypsin inhibitor mutant K15R
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00063
ethyl 2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
at pH 7.4 and 37°C
0.000495
ethyl 2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
at pH 7.4 and 37°C
0.0000067
methyl (4-[2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000027 - 0.0000058
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
0.0000019
methyl (4-[5-chloro-2-[(1S)-1-([3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000034
methyl (4-[5-chloro-2-[(1S)-1-([N-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0008
methyl 4-(2-((S)-1-(trans-4-(aminomethyl)-cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-benzoate
at pH 7.4 and 37°C
0.0005
methyl [(10S)-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000092
methyl [(10S)-13-chloro-10-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,9,10,12-hexahydro-14,11-(azeno)-8,4-(metheno)-2,12-benzodiazacyclohexadecin-17-yl]carbamate
-
at 25°C, pH not specified in the publication
0.0000015
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.00000032
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.00000053
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-15,12-(azeno)-5,9-(metheno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.00000002
methyl [(11S)-11-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2H-5,9:15,12-di(azeno)-1,13-benzodiazacycloheptadecin-18-yl]carbamate
-
at 37°C, pH not specified in the publication
0.0000082
methyl [(5S)-2-chloro-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,12,13,14,15-hexahydro-3H-1,4-(azeno)-7,11-(metheno)-3-benzazacycloheptadecin-17-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000071
methyl [(5S)-5-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-5,6,11,12,13,14-hexahydro-3H-1,4-(azeno)-7,10-etheno-3-benzazacyclohexadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000017 - 0.0081
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
0.0064
methyl [(9S)-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.00000149
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1-(3-aminopropyl)cyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
0.000065
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2,6-difluoro-4-methoxybenzamide
-
at 25°C, pH not specified in the publication
0.00028
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methoxybenzamide
-
at 25°C, pH not specified in the publication
0.0002
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methylbenzamide
-
at 25°C, pH not specified in the publication
0.00000103
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)-2-fluorobenzamide
-
at 25°C, pH not specified in the publication
0.00000116
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)benzamide
-
at 25°C, pH not specified in the publication
0.00039
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylbenzamide
-
at 25°C, pH not specified in the publication
0.00053
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5-chloro-2-fluorobenzamide
-
at 25°C, pH not specified in the publication
0.00045
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-pyrazol-1-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.0000015
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.000046
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(4H-1,2,4-triazol-4-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.00031
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]benzene-1,4-dicarboxamide
-
at 25°C, pH not specified in the publication
0.00000081
protease nexin-2
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000492
protease nexin-2 mutant F34A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000081
protease nexin-2 mutant M17A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000296
protease nexin-2 mutant P13A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.0000113
protease nexin-2 mutant R15K
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000283
protease nexin-2 mutant R20A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000093
protease nexin-2 mutant S19A
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00112
trans-4-(aminomethyl)-N-((S)-1-(4-(3-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00023
trans-4-(aminomethyl)-N-((S)-1-(4-(4-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.003074
trans-4-(aminomethyl)-N-((S)-1-(5-oxo-1-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-2-phenylethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00164
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(2-phenyl-1H-imidazol-4-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00098
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-1,2,4-triazol-5-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00694
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-pyrazol-5-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00134
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-(4-sulfamoylphenyl)-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00012
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00144
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(5-phenyloxazol-2-yl)ethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.000479
trans-4-(aminomethyl)-N-[1-(1-methyl-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00253
trans-4-(aminomethyl)-N-[1-(1-oxido-2-phenylpyridin-4-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00169
trans-4-(aminomethyl)-N-[1-(1-oxido-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.001063
trans-4-(aminomethyl)-N-[1-(1-oxido-5-phenylpyridin-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000012
trans-4-(aminomethyl)-N-[1-(5-chloro-4-phenyl-1H-imidazol-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00032
trans-4-(aminomethyl)-N-[1-(5-fluoro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000227
trans-4-(aminomethyl)-N-[1-(6-amino-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000206
trans-4-(aminomethyl)-N-[1-(6-chloro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000113
trans-4-(aminomethyl)-N-[1-(6-hydroxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000949
trans-4-(aminomethyl)-N-[1-(6-methoxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000936
trans-4-(aminomethyl)-N-[1-(biphenyl-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00086
trans-4-(aminomethyl)-N-[1-[6-(methylamino)-4-phenylpyridin-2-yl]-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000433
trans-4-(aminomethyl)-N-[2-phenyl-1-(2-phenylpyridin-4-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00012
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000377
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.01142
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyrimidin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00033
trans-4-(aminomethyl)-N-[2-phenyl-1-(5-phenylpyridin-3-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.03021
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000331
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyrimidin-4-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000545
trans-N-((S)-1-(4-(3-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.0000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-fluoro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.0004
trans-N-((S)-1-(4-(4-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
at pH 7.4 and 37°C
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
0.000068
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylcyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
0.0029
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]cyclohexane-1,4-dicarboxamide
-
at 25°C, pH not specified in the publication
0.000021
trans-N-[1-[3-(3-amino-1H-indazol-6-yl)phenyl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000037
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)-6-oxo-1,6-dihydropyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000013
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)pyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000032
trans-N-[1-[5-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000211
4-aminobenzamidine
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000245
4-aminobenzamidine
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000362
4-aminobenzamidine
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000396
4-aminobenzamidine
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000416
4-aminobenzamidine
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000419
4-aminobenzamidine
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000497
4-aminobenzamidine
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000513
4-aminobenzamidine
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000714
4-aminobenzamidine
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000739
4-aminobenzamidine
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.000079
4-aminobenzamidine
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0001529
4-aminobenzamidine
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.06
4-aminobenzamidine
-
37°C, recombinant wild-type enzyme, versus substrate S-2366
0.085
4-aminobenzamidine
-
37°C, recombinant peptide FXI/E361-V607, versus substrate S-2366
0.086
4-aminobenzamidine
-
37°C, recombinant peptide FXI/E361-V607, versus substrate factor IX
0.095
4-aminobenzamidine
-
37°C, recombinant wild-type enzyme, versus substrate factor IX
0.52
Aprotinin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, free FXIa
1.43
leupeptin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, free FXIa
209
leupeptin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, FXIa-FIX complex
0.0000027
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000058
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 37°C, pH not specified in the publication
0.000017
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.0081
methyl [(9S)-12-chloro-9-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3-oxo-1,2,3,8,9,11-hexahydro-13,10-(azeno)-4,7-etheno-2,11-benzodiazacyclopentadecin-16-yl]carbamate
-
at 25°C, pH not specified in the publication
0.000001
protease nexin 2
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000011
protease nexin 2
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000013
protease nexin 2
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000013
protease nexin 2
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000014
protease nexin 2
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000015
protease nexin 2
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000015
protease nexin 2
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000047
protease nexin 2
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.42
S-2366
-
37°C, recombinant peptide FXI/E361-V607, versus substrate factor IX
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
additional information
additional information
competition for platelet binding by the wild-type enzyme and mutants, overview
-
additional information
additional information
second-order inhibition rate constants, wild-type and mutant enzymes with different inhibitors, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000132
(3R)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
Homo sapiens
pH 7.4, 37°C
0.000533
(3R)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
Homo sapiens
pH 7.4, 37°C
0.00001
(3S)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
Homo sapiens
pH 7.4, 37°C
0.000028
(3S)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
Homo sapiens
pH 7.4, 37°C
0.1759
(4S,7S)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,12,13,14,15-dodecahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.1358
(4S,7S,10S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-10-phenyl-4,5,7,8,10,11,14,15-octahydro-1H-[1,4,7]triazacyclohexadecino[10,9-b]indole-3,6,9(2H)-trione
Homo sapiens
-
pH and temperature not specified in the publication
0.7678
(4S,7S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,14,15-decahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000076 - 0.0002
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
0.0073
1-[2-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl]guanidine
Homo sapiens
-
-
0.000007
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-L-arginyl-L-valyl-L-arginyl)-1,3-thiazole
Homo sapiens
pH 7.4, 37°C
0.00003
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N5-carbamoyl-L-ornithyl-L-valyl-L-arginyl)-1,3-thiazole
Homo sapiens
pH 7.4, 37°C
0.0014
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
Homo sapiens
-
-
0.0014
decasodium 1,2,3,4,6-pentakis-O-[3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
Homo sapiens
-
at pH 7.4 and 37°C
0.0005
decasodium 1,2,3,4,6-pentakis-O-[4-hydroxy-3,5-bis(sulfonatooxy)benzoyl]-beta-D-threo-hexopyranose
Homo sapiens
-
at pH 7.4 and 37°C
0.000403
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]leucinate
Homo sapiens
pH 7.4, 37°C
0.000258
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]phenylalaninate
Homo sapiens
pH 7.4, 37°C
0.0092
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2,2-dimethylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000045
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(2,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000063
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000114
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(4-chlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000093
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.0026
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorophenyl)sulfonyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.00016
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(4-fluorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.0023
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylacetyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.0022
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylcarbonyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.00192
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(phenylcarbamoyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.00092
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]propyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.00034
N-[(1S)-2-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]amino]-1-cyclohexyl-2-oxoethyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.00071
N-[(3,4-dichlorobenzyl)carbamoyl]-L-leucyl-N-[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]-L-phenylalaninamide
Homo sapiens
pH 7.4, 37°C
0.1031
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-(pent-4-enoylamino)acetyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1459
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-[[(2S)-2-phenylpent-4-enoyl]amino]acetyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
N2-(benzylcarbamoyl)-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.027
N2-acetyl-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000356
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000008
N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N1-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-aspartamide
Homo sapiens
pH 7.4, 37°C
0.00001
N2-[[1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
pH 7.4, 37°C
0.000006
Na-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N2-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tyrosinamide
Homo sapiens
pH 7.4, 37°C
0.000029
Nalpha-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tryptophanamide
Homo sapiens
pH 7.4, 37°C
0.000076
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
Homo sapiens
pH 7.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type andmutant substrate, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
36529, 36530, 36531, 36532, 36536, 36537, 36538, 36539, 36540, 36541, 649981, 650724, 652013, 652309, 652338, 667059, 667583, 667611, 667620, 669347
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the enzyme binds to platelets, a conformational transition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain zymogen factor XI platelet binding site and exposes the factor XIa platelet binding site within the catalytic domain possibly comprising residues Cys527-Cys542, overview
brenda
additional information
hemophilia C (deficiency in FXI) is present in both sexes
brenda
additional information
-
hemophilia C (deficiency in FXI) is present in both sexes
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
a deficiency in FXI (hemophilia C) results in a more benign bleeding phenotype compared with a deficiency in either FVIII (hemophilia A) or FIX (hemophilia B). Most hemophilia C cases involve Ashkenazi Jews and result from either of 2 mutations in the FXI gene (E117X and F283L). Greater than 180 mutations are present but in lesser frequency. FXI deficiency also arises from acquired inhibitors that neutralize its activity, these patients may not respond well to FXI replacement therapy. Bleeding in those with hemophilia C is rarely spontaneous, it tends to occur in response to surgery or trauma, and especially in tissue prone to fibrinolysis (the urinary track or oral cavity). Prolonged activated partial thromboplastin time due to FXI deficiency
malfunction
activated partial thromboplastin time is abnormal in all cases with severe or moderate FXI deficiency. FXI deficiency is not an absolute contraindication to neuraxial anesthesia
malfunction
-
addition of murine FXI to human FXI deficient plasma rescues the prolonged activated partial thromboplastin time, but with a slightly reduced activity compared with the human protein. FXI-/- mice are healthy, fertile, and phenotypically indistinguishable from wild-type animals. Mating between heterozygous FXI+/- mice follows the expected Mendelian ratio arguing against an association of FXI deficiency and increased risk of abortion. Plasma from FXI null mice show a severely prolonged activated partial thromboplastin time compared with wild-type animals. Bleeding times in adult FXI-/- mice are indistinguishable from wild-type animals, suggesting that FXI does not significantly contribute to fibrin formation. Formation of thrombi is severely defective in FXI-/- mice. Both fibrin deposition and platelet accumulation are reduced in FXI null mice compared with wild-type. FXI deficiency increases survival and reduces leukocyte infiltration and coagulopathy
malfunction
congenital FXI deficiency is associated with a variable, mild to moderate bleeding disorder. Severe deficiency is prevalent in people of Jewish ancestry. The severe mutation Glu117Stop encodes a truncated protein, and homozygotes lack plasma FXI antigen. The more subtle missense mutation Phe283Leu causes a defect in FXI dimer formation. Most cases of FXI deficiency are associated with low plasma levels of FXI protein. Deficiency or inhibition of FXI interferes with platelet accumulation in growing thrombi. A4 domain mutations associated with FXI deficiency interfere with dimerization. FXI-deficient plasma exhibits a prolonged activated partial thromboplastin clotting time
malfunction
FXI deficiency is a rare inherited coagulation disorder characterized by infrequent spontaneous bleeding, but increased risk of hemorrhagic complications especially after trauma or surgery
malfunction
FXI deficient humans suffer from mild hemorrhage (hemophilia C), which is characterized by trauma or soft tissue-related hemorrhage, primarily involving tissues with high fibrinolytic activity. Bleeding severity in FXI deficiency is not associated with FXI plasma levels. Addition of murine FXI to human FXI deficient plasma rescues the prolonged activated partial thromboplastin time, but with a slightly reduced activity compared with the human protein
malfunction
-
FXI-null mice are healthy, and their reproduction follows the expected mendelian ratios without impaired fecundity. FXI-null mice are protected against oxidative iron chloride-induced carotid artery thrombosis and infusion of human FXI reverses this protection. Thrombus formation in FXI-null mice is also reduced in response to laser injury of arterioles in the cremaster muscle. FXI deletion is also effective in preserving carotid artery blood flow in response to compression injury
malfunction
-
mice lacking FIX, FXI, or FXII on a background of low tissue factor expression have a severe bleeding disorder but are viable. Superimposing FIX or FXI deficiency on the low tissue factor background results in death in utero from bleeding
malfunction
-
patients who have a very severe FXI deficiency are prone to development of inhibitor antibodies. During major surgeries, a single low dose of recombinant activated factor VII and tranexamic acid secure normal haemostasis in patients with severe FXI deficiency who can not receive blood products
malfunction
-
enzyme deficiency results in bleeding diathesis referred to as hemophilia C
malfunction
-
factor XI deficiency can lead to delayed clot formation and decreased thrombin generation
physiological function
-
78% homology to human FXI at the protein level. FXI is critical for fibrin formation in vivo. FXI may have additional functions in regulation of inflammation or tissue repair distinct from its role in coagulation
physiological function
FXI is a biomarker with increased levels reported as a risk factor for venous thromboembolism and myocardial ischemia or stroke
physiological function
FXI is the zymogen of a blood coagulation protease, factor XIa (activated factor IX), that contributes to hemostasis through activation of factor IX. Almost all FXI circulate in a complex with kininogen
physiological function
FXI is the zymogen of a plasma protease that contributes to fibrin formation and stability by activating factor IX. Circulates in plasma in complex with high molecular weight kininogen
physiological function
-
involvment of FXI in thrombosis, role for activated factor FXI in tissue infammation
physiological function
-
presence of a single precursor of FXI and plasma kallikrein, appearance of FXI among early tetrapods
physiological function
-
the opossum genome has two distinct genes for both FXI and plasma kallikrein, indicating that the gene duplication event leading to separate factors occurred early in mammalian evolution
physiological function
-
activated factor XI inhibits chemotaxis of polymorphonuclear leukocytes. Coagulation factor XI participates in the intrinsic coagulation pathway upon its activation, contributing to hemostasis and thrombosis. Factor XIa attenuates N-formylmethionyl-leucyl-phenylalanine-induced Ca2+mobilization
physiological function
-
factor XIa plays its major role in promoting late thrombin formation (i.e. the thrombin required for thrombin activatable fibrinolysis inhibitor-mediated inhibition of fibrinolysis)
physiological function
-
activated factor XI increases the procoagulant activity of the extrinsic pathway by inactivating tissue factor pathway inhibitor
physiological function
-
factor XI is important in the tissue factor-independent propagation phase of clot formation, not in the initiation process
physiological function
-
coagulation factor XI induces Ca2+ response and accelerates cell migration in vascular smooth muscle cells via proteinase-activated receptor 1
physiological function
-
low concentrations of tissue factor and exogenous factor XIa, each too low to elicit a burst in thrombin production alone, act synergistically when in combination to cause substantial thrombin production
physiological function
-
the enzyme plays a pivotal role in regulation of chemerin bioactivity in plasma
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FA11_BOVIN
625
0
69872
Swiss-Prot
Secretory Pathway (Reliability: 2)
FA11_HUMAN
625
0
70109
Swiss-Prot
Secretory Pathway (Reliability: 2)
FA11_MOUSE
624
0
69789
Swiss-Prot
Secretory Pathway (Reliability: 2)
A0A425HRD9_TOXGO
654
0
71093
TrEMBL
Secretory Pathway (Reliability: 3)
A0A086Q258_TOXGO
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
S8EZX1_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
2328
0
253640
TrEMBL
Mitochondrion (Reliability: 2)
S7UMV2_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
F0JAV0_NEOCL
Neospora caninum (strain Liverpool)
350
0
37855
TrEMBL
Secretory Pathway (Reliability: 3)
S7UVR9_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
126
0
13457
TrEMBL
other Location (Reliability: 3)
A0A2T6II49_TOXGO
1320
0
145538
TrEMBL
Mitochondrion (Reliability: 4)
A0A086JAS2_TOXGO
1860
0
202886
TrEMBL
other Location (Reliability: 1)
A0A086JYX0_TOXGO
70
0
7576
TrEMBL
other Location (Reliability: 1)
V4ZEU8_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
1860
0
202915
TrEMBL
other Location (Reliability: 1)
A0A3R7YPK8_TOXGO
1320
0
145538
TrEMBL
Mitochondrion (Reliability: 4)
A0A2T6II52_TOXGO
1664
0
181619
TrEMBL
other Location (Reliability: 2)
A0A086JH56_TOXGO
1320
0
145552
TrEMBL
Mitochondrion (Reliability: 4)
A0A086JH62_TOXGO
62
0
6550
TrEMBL
other Location (Reliability: 1)
A0A086PG37_TOXGO
1856
0
202508
TrEMBL
other Location (Reliability: 2)
A0A086JTG7_TOXGO
654
0
71119
TrEMBL
Secretory Pathway (Reliability: 3)
A0A086KQT7_TOXGO
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
A0A086PIW8_TOXGO
1320
0
145522
TrEMBL
Mitochondrion (Reliability: 4)
A0A2G8XM15_TOXGO
1860
0
202871
TrEMBL
other Location (Reliability: 1)
A0A086LTJ4_TOXGO
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
A0A086JSN5_TOXGO
1320
0
145538
TrEMBL
Mitochondrion (Reliability: 4)
A0A086JYV7_TOXGO
1860
0
202899
TrEMBL
other Location (Reliability: 1)
A0A2G8XWV4_TOXGO
70
0
7499
TrEMBL
other Location (Reliability: 1)
S7VNS6_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
1559
0
170517
TrEMBL
other Location (Reliability: 1)
A0A086JHJ8_TOXGO
1860
0
202938
TrEMBL
other Location (Reliability: 1)
S8GE96_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
1931
0
210582
TrEMBL
other Location (Reliability: 1)
A0A086JYT0_TOXGO
1320
0
145538
TrEMBL
Mitochondrion (Reliability: 4)
A0A139XT94_TOXGO
654
0
71096
TrEMBL
Secretory Pathway (Reliability: 3)
A0A086M0U2_TOXGO
1320
0
145508
TrEMBL
Mitochondrion (Reliability: 4)
A0A086PJV3_TOXGO
525
0
56553
TrEMBL
other Location (Reliability: 2)
A0A2G8XWV2_TOXGO
1320
0
145500
TrEMBL
Mitochondrion (Reliability: 4)
A0A3R8AFY2_TOXGO
1731
0
189233
TrEMBL
other Location (Reliability: 1)
A0A086PP13_TOXGO
1320
0
145522
TrEMBL
Mitochondrion (Reliability: 4)
A0A2T6II66_TOXGO
62
0
6550
TrEMBL
other Location (Reliability: 1)
A0A2G8XSQ7_TOXGO
654
0
71109
TrEMBL
Secretory Pathway (Reliability: 3)
A0A125YNB1_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
A0A139XIW7_TOXGO
1320
0
145552
TrEMBL
Mitochondrion (Reliability: 4)
S7URJ3_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
1320
0
145512
TrEMBL
Mitochondrion (Reliability: 4)
A0A086QR16_TOXGO
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
V4YRM6_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
1320
0
145538
TrEMBL
Mitochondrion (Reliability: 4)
A0A086L8S1_TOXGO
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2T6IUI9_TOXGO
654
0
71123
TrEMBL
Secretory Pathway (Reliability: 3)
S8EWI3_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
1320
0
145552
TrEMBL
Mitochondrion (Reliability: 4)
B9QJ65_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
654
0
71119
TrEMBL
Secretory Pathway (Reliability: 3)
V5B5B1_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
126
0
13381
TrEMBL
other Location (Reliability: 3)
A0A139XIH6_TOXGO
1414
0
155325
TrEMBL
other Location (Reliability: 1)
A0A139XIY4_TOXGO
70
0
7499
TrEMBL
other Location (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
80000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
-
macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa are required for mediation of formation of the Michaelis complex required for factor IX-activation, overview
dimer
-
two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the enzyme bears five N-glycosylation consensus sites per monomer
proteolytic modification
proteolytic modification
factor XI is activated to factor XIa by site-specific cleavage of zymogen factor XI by thrombin, factor XIIa, or autoactivation
proteolytic modification
factor XI is activated to factor XIIa at 37°C, a conformational transition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain zymogen factor XI platelet binding site and exposes the factor XIa platelet binding site within the catalytic domain possibly comprising residues Cys527-Cys542
proteolytic modification
-
FXI activation proceeds through an intermediate with one activated subunit, limited digestion by incubating with FXIIa or thrombin
proteolytic modification
the enzyme shows activation by autolysis involving residues of the autolysis loops, overview
proteolytic modification
-
the zymogen FXI is activated by proteolytic cleavage to FXIa
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length zymogen FXI, and the isolated active protease domain of activated factor IX in complex with natural and synthetic inhibitors. Intimate linkage of the apple domains into a disk-like platform around the base of the catalytic domain
hanging drop vapor diffusion
in complaex with inhibitors, hanging drop vapor diffusion method, using 0.2 M (NH4)2SO4, 25% (w/v) polyethylene glycol methyl ether 2000, and 100 mM NaOAc, pH 4.6
in complex with inhibitors, hanging drop vapor diffusion method, using 0.1 M citrate pH 4.7-5.2, 20-26% (w/v) PEG 4K
purified recombinant catalytic domain of mutant S434A/T475A/C482S/K437A complexed with benzylamidine, crystallization solution is 2.0 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.5, overnight at 10 °C, cryoprotection by 20% v/v glycerol, X-ray diffraction structure determination and anaylsis at 2.25 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C362S/C482S
C398Y
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
C482S
-
the mutant shows 1.45fold enhanced activity as compared with the wild type enzyme
E98A
-
the mutant has normal Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
E98D
-
the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
E98V
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
G104R
this mutation in the PK A2 domain associated with CRM+ PK deficiency causes decreased kininogen binding
G193A
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193D
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 1.6-36fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193E
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193K
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 35-478fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193R
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193V
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G400V
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
I151A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
K145A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K148A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K149A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K170A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K170A/R171A/R173A
catalytic domain with residues 170, 171, and 173 changed to alanine is designated CD-KRR/A
K175A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K179A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K192A
-
the mutant has normal Km value for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
K192E
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
K192Q
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
K192R
-
the mutant has decreased Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
M102T
-
site-directed mutagenesis,missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
M18I
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
R144A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R144A/K145A/R147A/K148A/K149A
site-directed mutagenesis of an autolysis loop residues, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R144A/K145A/R147A/R149A
contains Ala substitutions for Arg-144, Lys-145, Arg-147, and Arg-149 (residues 504, 505, 507, and 509, respectively, in fXI numbering)
R147A
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R171A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
R173A
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
R3704A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
R378C
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
S225F
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
S248N
binds platelets with 5fold reduced affinity compared with wild-type, the A3 domain is probably not affected significantly, as FXI-Asn248 is secreted, activated by activated factor XII, and activates FIX similar to wild-type activated factor IX. Is associated with bleeding and defective FXI binding to platelets but does not affect the activated partial thromboplastin time assay, which does not contain platelets
S434A/K437A/T475A/C482S
to improve crystallizability a quadrupole mutant is generated
S434A/T475A/C482S/K437A
site-directed mutagenesis, crystal structure determination with bound benzylamidine
T575M
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
W569S
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
Y133S
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
Y143A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
Y5901A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
Y5901V
-
the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
additional information
C362S/C482S
site-directed mutagenesis, the mutant shows increased platelet binding compared to the wild-type enzyme
additional information
-
FXIa/PKA4 is made by replacing the FXI A4 domain with the A4 domain from prekallikrein. A dimeric version of FXI/PKA4 (FXI/PKA4-Gly326) is prepared as a control. Activated FXIa/PKA4 and FXIa/PKA4-Gly326 activate factor IX with kinetic parameters similar to that of FXIa. FXI/PKA4 and FXIa/PKA4-Gly326 have coagulant activity similar to FXI. FXIa/PKA4, FXIa/PKA4-Gly326 and FXIa have similar affinities for activated platelets. The dimeric proteins FXI and FXI/PKA4-Gly326 promote coagulation similarly, however, monomeric FXIa/PKA4 has greatly reduced activity. The activated monomeric FXIa/PKA4 activates factor IX poorly in the presence of activated platelets
additional information
chimeric recombinant enzyme mutants rFXI-PKA3 and rFXIa-PKA3, with fusion of FXI to the Apple 3 domain of prekallikrein, show unaffected platelet binding compared to the wild-type enzyme, overview
additional information
-
construction of FXI with a single catalytic active site, construction of recombinant FXI with the A4 domain replaced by the A4 domain from plasma prekallikrein, i.e. FXI/PKA4, overview
additional information
factor XI deficiency caused by compound heterozygous F11 gene mutation
additional information
mutations in the fXIa 170 helix are introduced into a modified human fXI cDNA (fXI-Ser-362,482), which contains serine substitutions for Cys-362 and Cys-482
additional information
two different mutations, c.1546 G>A (Val498Met) and c.1560dupG (Tyr503ValfsX32) in the F11 gene
additional information
-
two different mutations, c.1546 G>A (Val498Met) and c.1560dupG (Tyr503ValfsX32) in the F11 gene
additional information
FXI with substitutions for Cys321 still form stable dimers. The Cys321-Cys321 interchain bond forms poorly in FXI with a single alanine substitution of Leu284, Ile290, or Tyr329
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
factor XIa-triggered thrombin generation assays are not affected by glycoPEGylation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
antibody-affinity chromatography by using the calcium-dependent anti-human fIX monoclonal IgG SB 249417
-
native enzyme from plasma and recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity chromatography with elution by benzamidine
-
recombinant mutant enzyme C362S/C482S from HEK-293 cells by immunoaffinity chromatography
recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity chromatography
recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity, cation exchange, and heparin affinity chromatography
SP-Sepharose column chromatography, Heparin HiTrap column chromatography and Superdex 75 column chromatography
-
Zn2+-chelating Sepharose column chromatography and SP Sepharose column chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expression of mutant enzyme C362S/C482S in HEK-293 cells and secretion of recombinant protein to the medium
expression of the catalytic domain rhFXI370-60 of mutant S434A/T475A/C482S/K437A
expression of the peptide comprising 237 amino acids at the C-terminal end of FXI, peptide FXI/E361-V607, in Pichia pastoris strain X33
-
expression of wild-type and mutant enzymes in HEK-293 cells and secretion of recombinant protein to the medium
genetic location on chromosome 4q35, stable expression of wild-type and mutant enzymes in BHK-570 cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
antisense oligonucleotide produces near-complete inhibition of hepatic FXI mRNA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
-
activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
drug development
-
activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
drug development
-
activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
drug development
activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
medicine
the enzyme may be a suitable target for the development of an antithrombotic therapy
medicine
diagnosis of FXI deficiency may be considered in patients with delayed postoperative bleeding and prolonged activated partial thromboplastin time, especially in a demographically high-risk population, such as Ashkenazi Jews. Women with severe FXI deficiency and prolonged activated partial thromboplastin time can be managed with fresh frozen plasma transfusion before neuraxial anesthesia
medicine
-
therapeutically targeting FXI may offer a strategy for preventing or treating arterial thrombosis that is not associated with the high rate of hemorrhage that accompanies many currently used anticoagulants. Pharmacological FXI inhibitors may be beneficial in septic disease
medicine
treatment options for FXI-deficient patients include virus-inactivated fresh frozen plasma, plasma-derived FXI concentrates, and activated recombinant FVII. Potential role of desmopressin for either treatment of bleeding episodes or the prevention of postoperative bleeding in patients with milder FXI defects. A single desmopressin infusion is sufficient to provide an efficient perioperative hemostasis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lindquist, P.A.; Fujikawa, K.; Davie, E.W.
Activation of bovine factor IX (Christmas factor) by factor XIa (activated plasma thromboplastin antecedent) and a protease from Russells viper venom
J. Biol. Chem.
253
1902-1909
1978
Bos taurus
brenda
Scott, C.F.; Mentzer, R.L.; Budzynski, A.Z.; Colman, R.W.
Human factor XIa cleaves fibrinogen: effects on structure and function
Arch. Biochem. Biophys.
249
480-488
1986
Homo sapiens
brenda
Sinha, D.; Koshy, A.; Seaman, F.S.; Walsh, P.N.
Functional characterization of human blood coagulation factor XIa using hybridoma antibodies
J. Biol. Chem.
260
10714-10719
1985
Homo sapiens
brenda
Meijers, J.C.M.; Vlooswijk, R.A.A.; Bouma, B.N.
Inhibition of human blood coagulation factor XIa by C-1 inhibitor
Biochemistry
27
959-963
1988
Homo sapiens
brenda
Van der Graaf, F.; Greengard, J.S.; Bouma, B.N.; Kerbiriou, D.M.; Griffin, J.H.
Isolation and functional characterization of the active light chain of activated human blood coagulation factor XI
J. Biol. Chem.
258
9669-9675
1983
Homo sapiens
brenda
Koide, T.; Kato, H.; Davie, E.W.
Bovine factor XI (plasma thromboplastin antecedent)
Methods Enzymol.
45
65-73
1976
Bos taurus
brenda
Fujikawa, K.; Legaz, M.E.; Kato, H.; Davie, E.W.
The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent)
Biochemistry
13
4508-4516
1974
Bos taurus
brenda
Sinha, D.; Seaman, F.S.; Walsh, P.N.
Role of calcium ions and the heavy chain of factor XIa in the activation of human coagulation factor IX
Biochemistry
26
3768-3775
1987
Homo sapiens
brenda
Kam, C.M.; Fujikawa, K.; Powers, J.C.
Mechanism-based isocoumarin inhibitors for trypsin and blood coagulation serine proteases: new anticoagulants
Biochemistry
27
2547-2557
1988
Homo sapiens
brenda
Saportio-Irwin, S.M.; Van Nostrand, W.E.
Coagulation factor XIa cleaves the RHDS sequence and abolishes the cell adhesive properties of the amyloid beta-protein
J. Biol. Chem.
270
26265-26269
1995
Homo sapiens
brenda
Naito, K.; Fujikawa, K.
Activation of human blood coagulation factor XI independent of factor XII. Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces
J. Biol. Chem.
266
7353-7358
1991
Homo sapiens
brenda
Zhang, Y.; Scandura, J.M.; Van Nostrand, W.E.; Walsh, P.N.
The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2
J. Biol. Chem.
272
26139-26144
1997
Homo sapiens
brenda
Kalwant, S.; Porter, A.G.
Purification and characterization of human brain prolyl endopeptidase
Biochem. J.
276
237-244
1991
Homo sapiens
brenda
Badellino, K.O.; Walsh, P.N.
Protease nexin II interactions with coagulation factor XIa are contained within the Kunitz protease inhibitor domain of protease nexin II and the factor XIa catalytic domain
Biochemistry
39
4769-4777
2000
Homo sapiens
brenda
Gailani, D.; Ho, D.; Sun, M.F.; Cheng, Q.; Walsh, P.N.
Model for a factor IX activation complex on blood platelets: dimeric conformation of factor XIa is essential
Blood
97
3117-3122
2001
Homo sapiens
brenda
Baglia, F.A.; Walsh, P.N.
Thrombin-mediated feedback activation of factor XI on the activated platelet surface is preferred over contact activation by factor XIIa or factor XIa
J. Biol. Chem.
275
20514-20519
2000
Homo sapiens
brenda
Baird, T.R.; Walsh, P.N.
The interaction of factor XIa with activated platelets but not endothelial cells promotes the activation of factor IX in the consolidation phase of blood coagulation
J. Biol. Chem.
277
38462-38467
2002
Homo sapiens
brenda
Peek, M.; Moran, P.; Mendoza, N.; Wickramasinghe, D.; Kirchhofer, D.
Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa
J. Biol. Chem.
277
47804-47809
2002
Homo sapiens
brenda
Jin, L.; Pandey, P.; Babine, R.E.; Weaver, D.T.; Abdel-Meguid, S.S.; Strickler, J.E.
Mutation of surface residues to promote crystallization of activated factor XI as a complex with benzamidine: an essential step for the iterative structure-based design of factor XI inhibitors
Acta Crystallogr. Sect. D
D61
1418-1425
2005
Homo sapiens
brenda
Pedicord, D.L.; Seiffert, D.; Blat, Y.
Substrate-dependent modulation of the mechanism of factor XIa inhibition
Biochemistry
43
11883-11888
2004
Homo sapiens
brenda
Sinha, D.; Badellino, K.O.; Marcinkiewicz, M.; Walsh, P.N.
Allosteric modification of factor XIa functional activity upon binding to polyanions
Biochemistry
43
7593-7600
2004
Homo sapiens
brenda
Sinha, D.; Marcinkiewicz, M.; Lear, J.D.; Walsh, P.N.
Factor XIa dimer in the activation of factor IX
Biochemistry
44
10416-10422
2005
Homo sapiens
brenda
Ogawa, T.; Verhamme, I.M.; Sun, M.F.; Bock, P.E.; Gailani, D.
Exosite-mediated substrate recognition of factor IX by factor XIa. The factor XIa heavy chain is required for initial recognition of factor IX
J. Biol. Chem.
280
23523-23530
2005
Homo sapiens
brenda
Navaneetham, D.; Jin, L.; Pandey, P.; Strickler, J.E.; Babine, R.E.; Abdel-Meguid, S.S.; Walsh, P.N.
Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2
J. Biol. Chem.
280
36165-36175
2005
Homo sapiens (P03951)
brenda
Jin, L.; Pandey, P.; Babine, R.E.; Gorga, J.C.; Seidl, K.J.; Gelfand, E.; Weaver, D.T.; Abdel-Meguid, S.S.; Strickler, J.E.
Crystal structures of the FXIa catalytic domain in complex with ecotin mutants reveal substrate-like interactions
J. Biol. Chem.
280
4704-4712
2005
Homo sapiens
brenda
Shi, T.; Giannakopoulos, B.; Iverson, G.M.; Cockerill, K.A.; Linnik, M.D.; Krilis, S.A.
Domain V of beta2-glycoprotein I binds factor XI/XIa and is cleaved at Lys317-Thr318
J. Biol. Chem.
280
907-912
2005
Homo sapiens
brenda
Rezaie, A.R.; Sun, M.F.; Gailani, D.
Contributions of basic amino acids in the autolysis loop of factor XIa to serpin specificity
Biochemistry
45
9427-9433
2006
Homo sapiens (P03951)
brenda
Miller, T.N.; Sinha, D.; Baird, T.R.; Walsh, P.N.
A catalytic domain exosite (Cys527-Cys542) in factor XIa mediates binding to a site on activated platelets
Biochemistry
46
14450-14460
2007
Homo sapiens (P03951)
brenda
Sinha, D.; Marcinkiewicz, M.; Navaneetham, D.; Walsh, P.N.
Macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX-activation
Biochemistry
46
9830-9839
2007
Homo sapiens
brenda
Schmidt, A.E.; Sun, M.F.; Ogawa, T.; Bajaj, S.P.; Gailani, D.
Functional role of residue 193 (chymotrypsin numbering) in serine proteases: influence of side chain length and beta-branching on the catalytic activity of blood coagulation factor XIa
Biochemistry
47
1326-1335
2008
Homo sapiens (P03951)
brenda
Lazarova, T.I.; Jin, L.; Rynkiewicz, M.; Gorga, J.C.; Bibbins, F.; Meyers, H.V.; Babine, R.; Strickler, J.
Synthesis and in vitro biological evaluation of aryl boronic acids as potential inhibitors of factor XIa
Bioorg. Med. Chem. Lett.
16
5022-5027
2006
Homo sapiens
brenda
Smith, S.B.; Verhamme, I.M.; Sun, M.F.; Bock, P.E.; Gailani, D.
Characterization of novel forms of coagulation factor XIa. Independence of factor XIa subunits in factor IX activation
J. Biol. Chem.
283
6696-6705
2008
Homo sapiens
brenda
Lin, J.; Deng, H.; Jin, L.; Pandey, P.; Quinn, J.; Cantin, S.; Rynkiewicz, M.J.; Gorga, J.C.; Bibbins, F.; Celatka, C.A.; Nagafuji, P.; Bannister, T.D.; Meyers, H.V.; Babine, R.E.; Hayward, N.J.; Weaver, D.; Benjamin, H.; Stassen, F.; Abdel-Meguid, S.S.; Strickler, J.E.
Design, synthesis, and biological evaluation of peptidomimetic inhibitors of factor XIa as novel anticoagulants
J. Med. Chem.
49
7781-7791
2006
Homo sapiens (P03951), Homo sapiens
brenda
Mitchell, M.J.; Dai, L.; Clarke, J.B.; Bolton-Maggs, P.H.; Savidge, G.F.; Alhaq, A.
Characterisation of five factor XI mutations
Thromb. Haemost.
97
884-889
2007
Homo sapiens
brenda
Yang, L.; Sun, M.F.; Gailani, D.; Rezaie, A.R.
Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor
Biochemistry
48
1517-1524
2009
Homo sapiens (P03951)
brenda
Kravtsov, D.V.; Matafonov, A.; Tucker, E.I.; Sun, M.F.; Walsh, P.N.; Gruber, A.; Gailani, D.
Factor XI contributes to thrombin generation in the absence of factor XII
Blood
114
452-458
2009
Homo sapiens (P03951)
brenda
Kwon, M.J.; Kim, H.J.; Bang, S.H.; Kim, S.H.
Severe factor XI deficiency in a Korean woman with a novel missense mutation (Val498Met) and duplication G mutation in exon 13 of the F11 gene
Blood Coagul. Fibrinolysis
19
679-683
2008
Homo sapiens (P03951), Homo sapiens
brenda
Wang, J.; Wang, X.; Dai, J.; Ding, Q.; Fu, Q.; Wang, H.; Shen, L.; Li, D.
A case of factor XI deficiency caused by compound heterozygous F11 gene mutation
Haemophilia
15
603-606
2009
Homo sapiens (P03951)
brenda
Buchanan, M.S.; Carroll, A.R.; Wessling, D.; Jobling, M.; Avery, V.M.; Davis, R.A.; Feng, Y.; Xue, Y.; Oster, L.; Fex, T.; Deinum, J.; Hooper, J.N.; Quinn, R.J.
Clavatadine A, a natural product with selective recognition and irreversible inhibition of factor XIa
J. Med. Chem.
51
3583-3587
2008
Homo sapiens (P03951)
brenda
Butenas, S.; Undas, A.; Gissel, M.T.; Szuldrzynski, K.; Zmudka, K.; Mann, K.G.
Factor XIa and tissue factor activity in patients with coronary artery disease
Thromb. Haemost.
99
142-149
2008
Homo sapiens
brenda
Singh, A.; Harnett, M.J.; Connors, J.M.; Camann, W.R.
Factor XI deficiency and obstetrical anesthesia
Anesth. Analg.
108
1882-1885
2009
Homo sapiens (P03951)
brenda
Franchini, M.; Manzato, F.; Salvagno, G.L.; Montagnana, M.; Lippi, G.
The use of desmopressin in congenital factor XI deficiency: a systematic review
Ann. Hematol.
88
931-935
2009
Homo sapiens (P03951), Homo sapiens
brenda
Schumacher, W.A.; Luettgen, J.M.; Quan, M.L.; Seiffert, D.A.
Inhibition of factor XIa as a new approach to anticoagulation
Arterioscler. Thromb. Vasc. Biol.
30
388-392
2010
Oryctolagus cuniculus, Mus musculus, Rattus norvegicus, Homo sapiens (P03951), Homo sapiens
brenda
Emsley, J.; McEwan, P.A.; Gailani, D.
Structure and function of factor XI
Blood
115
2569-2577
2010
Mus musculus, Homo sapiens (P03951)
brenda
Gailani, D.; Smith, S.B.
Structural and functional features of factor XI
J. Thromb. Haemost.
7 Suppl 1
75-78
2009
Homo sapiens (P03951)
brenda
Renne, T.; Oschatz, C.; Seifert, S.; Mueller, F.; Antovic, J.; Karlman, M.; Benz, P.M.
Factor XI deficiency in animal models
J. Thromb. Haemost.
7 Suppl 1
79-83
2009
Canis lupus familiaris, Felis catus, Mus musculus, Ornithorhynchus anatinus, Didelphis sp., Homo sapiens (P03951)
brenda
Maas, C.; Meijers, J.C.; Marquart, J.A.; Bakhtiari, K.; Weeterings, C.; de Groot, P.G.; Urbanus, R.T.
Activated factor V is a cofactor for the activation of factor XI by thrombin in plasma
Proc. Natl. Acad. Sci. USA
107
9083-9087
2010
Homo sapiens (P03951)
brenda
Livnat, T.; Tamarin, I.; Mor, Y.; Winckler, H.; Horowitz, Z.; Korianski, Y.; Bar-Zakay, B.; Seligsohn, U.; Salomon, O.
Recombinant activated factor VII and tranexamic acid are haemostatically effective during major surgery in factor XI-deficient patients with inhibitor antibodies
Thromb. Haemost.
102
487-492
2009
Homo sapiens
brenda
Hanessian, S.; Larsson, A.; Fex, T.; Knecht, W.; Blomberg, N.
Design and synthesis of macrocyclic indoles targeting blood coagulation cascade Factor XIa
Bioorg. Med. Chem. Lett.
20
6925-6928
2010
Homo sapiens
brenda
Luszczak, J.; Undas, A.; Gissel, M.; Olszowska, M.; Butenas, S.
Activated factor XI and tissue factor in aortic stenosis: links with thrombin generation
Blood Coagul. Fibrinolysis
22
473-479
2011
Homo sapiens
brenda
Cheng, Q.; Tucker, E.; Pine, M.; Sisler, I.; Matafonov, A.; Sun, M.; White-Adams, T.; Smith, S.; Hanson, S.; McCarty, O.; Renne, T.; Gruber, A.; Gailani, D.
A role for factor XIIa-mediated factor XI activation in thrombus formation in vivo
Blood
116
3981-3989
2010
Mus musculus
brenda
Navaneetham, D.; Sinha, D.; Walsh, P.N.
Mechanisms and specificity of factor XIa and trypsin inhibition by protease nexin 2 and basic pancreatic trypsin inhibitor
J. Biochem.
148
467-479
2010
Homo sapiens (P03951)
brenda
Su, Y.C.; Miller, T.N.; Navaneetham, D.; Schoonmaker, R.T.; Sinha, D.; Walsh, P.N.
The role of factor XIa (FXIa) catalytic domain exosite residues in substrate catalysis and inhibition by the Kunitz protease inhibitor domain of protease nexin 2
J. Biol. Chem.
286
31904-31914
2011
Homo sapiens
brenda
Itakura, A.; Verbout, N.G.; Phillips, K.G.; Insall, R.H.; Gailani, D.; Tucker, E.I.; Gruber, A.; McCarty, O.J.
Activated factor XI inhibits chemotaxis of polymorphonuclear leukocytes
J. Leukoc. Biol.
90
923-927
2011
Homo sapiens
brenda
Whelihan, M.F.; Orfeo, T.; Gissel, M.T.; Mann, K.G.
Coagulation procofactor activation by factor XIa
J. Thromb. Haemost.
8
1532-1539
2010
Homo sapiens
brenda
Carrieri, C.; Galasso, R.; Semeraro, F.; Ammollo, C.; Semeraro, N.; Colucci, M.
The role of thrombin activatable fibrinolysis inhibitor and factor XI in platelet-mediated fibrinolysis resistance: A thromboelastographic study in whole blood
J. Thromb. Haemost.
9
154-162
2011
Homo sapiens
brenda
Fradera, X.; Kazemier, B.; Carswell, E.; Cooke, A.; Oubrie, A.; Hamilton, W.; Dempster, M.; Krapp, S.; Nagel, S.; Jestel, A.
High-resolution crystal structures of factor XIa coagulation factor in complex with nonbasic high-affinity synthetic inhibitors
Acta Crystallogr. Sect. F
68
404-408
2012
Homo sapiens (P03951)
brenda
Pinto, D.J.; Smallheer, J.M.; Corte, J.R.; Austin, E.J.; Wang, C.; Fang, T.; Smith, L.M.; Rossi, K.A.; Rendina, A.R.; Bozarth, J.M.; Zhang, G.; Wei, A.; Ramamurthy, V.; Sheriff, S.; Myers, J.E.; Morin, P.E.; Luettgen, J.M.; Seiffert, D.A.; Quan, M.L.; Wexler, R.R.
Structure-based design of inhibitors of coagulation factor XIa with novel P1 moieties
Bioorg. Med. Chem. Lett.
25
1635-1642
2015
Homo sapiens
brenda
Corte, J.; Fang, T.; Hangeland, J.; Friends, T.; Rendina, A.; Luettgen, J.; Bozarth, J.; Barbera, F.; Rossi, K.; Wei, A.; Ramamurthy, V.; Morin, P.; Seiffert, D.; Wexler, R.; Quan, M.
Pyridine and pyridinone-based factor XIa inhibitors
Bioorg. Med. Chem. Lett.
25
925-930
2015
Homo sapiens
brenda
Puy, C.; Tucker, E.I.; Matafonov, A.; Cheng, Q.; Zientek, K.D.; Gailani, D.; Gruber, A.; McCarty, O.J.
Activated factor XI increases the procoagulant activity of the extrinsic pathway by inactivating tissue factor pathway inhibitor
Blood
125
1488-1496
2015
Homo sapiens
brenda
Cho, J.; Kim, J.; Jung, S.; Kang, N.
Characterization of binding mode for human coagulation factor XI (FXI) inhibitors
Bull. Korean Chem. Soc.
34
1212-1220
2013
Homo sapiens
-
brenda
Ataullakhanov, F.; Dashkevich, N.; Negrier, C.; Panteleev, M.
Factor XI and traveling waves: The key to understanding coagulation in hemophilia?
Expert Rev. Hematol.
6
111-113
2013
Homo sapiens
brenda
Argade, M.D.; Mehta, A.Y.; Sarkar, A.; Desai, U.R.
Allosteric inhibition of human factor XIa: discovery of monosulfated benzofurans as a class of promising inhibitors
J. Med. Chem.
57
3559-3569
2014
Homo sapiens
brenda
Hangeland, J.J.; Friends, T.J.; Rossi, K.A.; Smallheer, J.M.; Wang, C.; Sun, Z.; Corte, J.R.; Fang, T.; Wong, P.C.; Rendina, A.R.; Barbera, F.A.; Bozarth, J.M.; Luettgen, J.M.; Watson, C.A.; Zhang, G.; Wei, A.; Ramamurthy, V.; Morin, P.E.; Bisacchi, G.S.; Subramaniam, S.; Arunachalam, P.; Mathur, A.; Seiffert, D.
Phenylimidazoles as potent and selective inhibitors of coagulation factor XIa with in vivo antithrombotic activity
J. Med. Chem.
57
9915-9932
2014
Homo sapiens (P03951)
brenda
Faid, V.; Denguir, N.; Chapuis, V.; Bihoreau, N.; Chevreux, G.
Site-specific N-glycosylation analysis of human factor XI: Identification of a noncanonical NXC glycosite
Proteomics
14
2460-2470
2014
Homo sapiens
brenda
Gailani, D.; Geng, Y.; Verhamme, I.; Sun, M.; Bajaj, S.; Messer, A.; Emsley, J.
The mechanism underlying activation of factor IX by factor XIa
Thromb. Res.
133
S48-S51
2014
Homo sapiens
-
brenda
Liu, W.; Hashimoto, T.; Yamashita, T.; Hirano, K.
Coagulation factor XI induces Ca2+ response and accelerates cell migration in vascular smooth muscle cells via proteinase-activated receptor 1
Am. J. Physiol. Cell Physiol.
316
C377-C392
2019
Rattus norvegicus
brenda
Leiderman, K.; Chang, W.C.; Ovanesov, M.; Fogelson, A.L.
Synergy between tissue factor and exogenous factor XIa in initiating coagulation
Arterioscler. Thromb. Vasc. Biol.
36
2334-2345
2016
Homo sapiens
brenda
Lu, Q.; Yang, L.; Manithody, C.; Wang, X.; Rezaie, A.R.
Expression and characterization of Gly-317 variants of factor IX causing variable bleeding in hemophilia B patients
Biochemistry
54
3814-3821
2015
Homo sapiens
brenda
Wang, C.; Corte, J.R.; Rossi, K.A.; Bozarth, J.M.; Wu, Y.; Sheriff, S.; Myers, J.E.; Luettgen, J.M.; Seiffert, D.A.; Wexler, R.R.; Quan, M.L.
Macrocyclic factor XIa inhibitors
Bioorg. Med. Chem. Lett.
27
4056-4060
2017
Homo sapiens
brenda
Meijers, J.
Prochemerin processing by factor XIa
Blood
131
275-276
2018
Homo sapiens
brenda
Ge, X.; Yamaguchi, Y.; Zhao, L.; Bury, L.; Gresele, P.; Berube, C.; Leung, L.L.; Morser, J.
Prochemerin cleavage by factor XIa links coagulation and inflammation
Blood
131
353-364
2018
Homo sapiens
brenda
Waters, E.K.; Hilden, I.; Sorensen, B.B.; Ezban, M.; Holm, P.K.
Thrombin generation assay using factor XIa to measure factors VIII and IX and their glycoPEGylated derivatives is robust and sensitive
J. Thromb. Haemost.
13
2041-2052
2015
Homo sapiens
brenda
Zucker, M.; Seligsohn, U.; Yeheskel, A.; Mor-Cohen, R.
An allosteric disulfide bond is involved in enhanced activation of factor XI by protein disulfide isomerase
J. Thromb. Haemost.
14
2202-2211
2016
Homo sapiens
brenda
Al-Horani, R.A.; Gailani, D.; Desai, U.R.
Allosteric inhibition of factor XIa. Sulfated non-saccharide glycosaminoglycan mimetics as promising anticoagulants
Thromb. Res.
136
379-387
2015
Homo sapiens
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.21.27)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
