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Information on EC 3.4.21.27 - coagulation factor XIa and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.27 coagulation factor XIa
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
activated blood-coagulation factor XI
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activated coagulation factor XIa
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activated factor XI
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FXIa
activated factor XIa
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activated FXI
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activated plasma thromboplastin antecedent
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blood coagulation factor XIa
blood-coagulation factor XI, activated
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blood-coagulation factor XIa
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coagulation factor XI
coagulation factor XIa
factor XI
factor XIa
factor XIa catalytic domain
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fXIaCD
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plasma thromboplastin antecedent
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prolyl endopeptidase
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protease factor XIa
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PTA
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recombinant human FXI370-607
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rhFXI370-607
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
37203-61-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amyloid beta-protein + H2O
?
show the reaction diagram
-
cleaves cell adhesion RHDS sequence
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
show the reaction diagram
-
-
-
-
?
beta-2-glycoprotein I + H2O
clipped beta-2-glycoprotein I
show the reaction diagram
-
cleavage at Lys317-Thr318
-
-
?
Boc-Glu(OBzl)-Ala-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Glu(OBzl)-Ala-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
show the reaction diagram
substrate S-2288
-
-
?
D-LPRANSNH-C3H7 + H2O
D-LPR + ANSNH-C3H7
show the reaction diagram
-
-
-
-
?
factor fIX + H2O
?
show the reaction diagram
-
factor IX
-
-
?
factor IX + H2O
?
show the reaction diagram
-
activation of Factor IX in the intrinsic coagulation cascade
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-
?
factor IX + H2O
activated factor IX + ?
show the reaction diagram
factor IX + H2O
factor IXa + ?
show the reaction diagram
factor IX + H2O
factor IXa + peptide
show the reaction diagram
factor IX 10-mer + H2O
?
show the reaction diagram
-
-
-
-
?
factor IX mutant G317E + H2O
?
show the reaction diagram
-
-
-
-
?
factor IX mutant G317R + H2O
?
show the reaction diagram
-
-
-
-
?
factor V + H2O
activated factor V + ?
show the reaction diagram
-
fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
-
-
?
factor VIII + H2O
activated factor VIII + ?
show the reaction diagram
-
fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
Aalpha-chain and Bbeta-chain, gamma-chain after prolonged incubation
-
-
?
kininogen + H2O
?
show the reaction diagram
L-Glu-L-Glu-L-Pro-L-Arg-4-nitroanilide + H2O
L-Glu-L-Glu-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
S-2366
-
-
?
L-pyro-Glu-Pro-Arg-4-nitroanilide + H2O
L-pyro-Glu-Pro-Arg + 4-nitroaniline
show the reaction diagram
i.e. S-2366
-
-
?
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroGlu-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroglutamyl-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
show the reaction diagram
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-7-amido-4-methylcoumarin + H2O
L-pyroglutamyl-L-prolyl-L-arginine + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
show the reaction diagram
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
?
show the reaction diagram
-
substrate S-299
-
-
?
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-arginine-p-nitroanilide + H2O
N-benzoyl-L-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-Cbz-D-arginylglycyl-L-arginyl-4-nitroanilide + H2O
N-Cbz-D-arginylglycyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
pefachrome Xa + H2O
?
show the reaction diagram
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-
?
platelet glycoprotein 1balpha + H2O
?
show the reaction diagram
binding to the A3 domain of FXI
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-
?
pro-HGF + H2O
?
show the reaction diagram
prochemerin + H2O
chemerin + ?
show the reaction diagram
-
-
-
-
?
prochemerin chem163S + H2O
chemerin chem162R + chermerin chem158K
show the reaction diagram
-
prochemerin is activated by a series of C-terminal proteolytic cleavages resulting in diverse chemerin forms with different levels of activity
-
-
?
pyroGlu-Pro-Arg-4-nitroanilide + H2O
?
show the reaction diagram
pyroGlu-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
pyroglutamoyl-prolyl-arginyl-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
?
S-2366 + H2O
?
show the reaction diagram
S2366 + H2O
L-pyroGlu-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
SN-13a + H2O
?
show the reaction diagram
-
specific substrate for factor XIa
-
-
?
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
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?
tissue factor pathway inhibitor + H2O
?
show the reaction diagram
-
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
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?
Z-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
factor IX + H2O
?
show the reaction diagram
-
activation of Factor IX in the intrinsic coagulation cascade
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?
factor IX + H2O
activated factor IX + ?
show the reaction diagram
factor IX + H2O
factor IXa + ?
show the reaction diagram
factor V + H2O
activated factor V + ?
show the reaction diagram
-
fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
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-
?
factor VIII + H2O
activated factor VIII + ?
show the reaction diagram
-
fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
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?
pro-HGF + H2O
?
show the reaction diagram
-
the enzyme may regulate processes that involve the HGF/c-Met pathway, such as tissue repair and angiogenesis
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?
prochemerin + H2O
chemerin + ?
show the reaction diagram
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?
prochemerin chem163S + H2O
chemerin chem162R + chermerin chem158K
show the reaction diagram
-
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
?
show the reaction diagram
-
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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(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
-
-
1-[2-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl]guanidine
-
-
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzyl]guanidine
-
-
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]guanidine
-
-
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-alkoxy-4-chloro-7-guanidinoisocoumarin
-
-
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-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)aniline
-
-
4-aminobenzamidine
4-chloro-3-isothiureidoalkoxyisocoumarin
-
-
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
-
-
alpha1-protease inhibitor
-
-
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
-
anti-thrombin III
-
-
-
antithrombin
-
Aprotinin
-
-
basic pancreatic trypsin inhibitor
competitive inhibition
-
basic pancreatic trypsin inhibitor mutant K15R
-
-
benzamidine
BMS-262084
-
boronic acid
-
-
C1 inhibitor
-
-
-
C1-inhibitor
-
clavatadine A
-
-
D-Phe-Pro-Arg-CH2Cl
-
irreversibly inhibits both active sites of the enzyme
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
dextran sulfate M 10000
-
51% saturable maximal inhibition at 37°C
-
dextran sulfate M 500000
-
86% saturable maximal inhibition at 37°
-
diisopropyl fluorophosphate
-
-
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
-
-
ecotin
-
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
-
-
factor fIX
-
factor IX
-
factor fIXai
-
factor IXai
-
fractionated heparin of 64 disaccharide units
-
70-80% saturable maximal inhibition at 37°C
-
hypersulfated heparin
-
54% saturable maximal inhibition at 37°C
-
leupeptin
-
-
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
-
nexin-2
-
heparin potentiates the inhibition
-
p-aminobenzamidine
-
-
PN-2
-
-
-
protease hexin II
-
-
-
protease nexin 2
-
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
-
protease nexin-2 mutant F34A
-
-
protease nexin-2 mutant M17A
-
-
protease nexin-2 mutant P13A
-
-
protease nexin-2 mutant R15K
-
-
protease nexin-2 mutant R20A
-
-
protease nexin-2 mutant S19A
-
-
protein Z dependent protease inhibitor
-
-
S-2366
-
noncompetitive inhibition versus factor IX
serpins
inhibition of autolysis of fXIa
-
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
-
-
sulfated pentagalloyl beta-D-glucopyranoside
-
-
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
-
-
Zn2+
-
partially
[4-(carbamimidamidomethyl)phenyl]boronic acid
-
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
-
activated factor VII
-
-
activated factor XI
-
-
activated factor XII
-
alpha-thrombin
cleaves FXI at the Arg369-Ile370 bond
-
desmopressin
Dextran sulfate
-
33nM
-
Factor XII
-
-
-
factor XIIa
-
FXIa
-
-
-
FXIIa
-
-
-
kininogen
-
-
-
meizothrombin
cleaves FXI at the Arg369-Ile370 bond
-
Protein disulfide isomerase
-
reduction of the enzyme by protein disulfide isomerase enhances its cleavage activity
-
thrombin
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
benzyloxycarbonyl-Gly-Pro-4-nitroanilide
-
-
0.34
D-Ile-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
0.09
factor fIX
-
FXIa
-
0.00012 - 0.151
factor IX
-
0.3
factor IX 10-mer
-
at pH 7.4 and 37°C
-
0.00038
factor IX mutant G317E
-
at 25°C, pH not specified in the publication
-
0.00035
factor IX mutant G317R
-
at 25°C, pH not specified in the publication
-
0.205 - 0.852
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
0.45 - 0.59
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
0.552 - 0.993
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
0.4 - 352
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
0.000103
prochemerin chem163S
-
at pH 7.4 and 37°C
-
0.26 - 0.4
pyroGlu-Pro-Arg-4-nitroanilide
0.56
pyroGlu-Pro-Arg-p-nitroanilide
-
-
0.225 - 0.384
S-2366
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
110.2
D-Ile-Pro-Arg-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 37°C
0.49
factor fIX
-
fXIa
-
0.00065 - 5.8
factor IX
-
0.083
factor IX 10-mer
-
at pH 7.4 and 37°C
-
8
Factor XI
-
pH 7.3, 37°C
-
5.8 - 201
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
250 - 430
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide
98 - 148
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
67 - 117
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide
0.91
prochemerin chem163S
-
at pH 7.4 and 37°C
-
0.268 - 145
pyroGlu-Pro-Arg-4-nitroanilide
350
pyroGlu-Pro-Arg-p-nitroanilide
-
-
113 - 121
S-2366
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17
factor IX 10-mer
-
at pH 7.4 and 37°C
-
530000
prochemerin chem163S
-
at pH 7.4 and 37°C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0000211 - 0.095
4-aminobenzamidine
0.52 - 10.42
Aprotinin
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
1.43 - 209
leupeptin
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
0.000001 - 0.0000047
protease nexin 2
-
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
-
0.42 - 0.425
S-2366
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
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
0.0257
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzyl]guanidine
Homo sapiens
-
-
0.0059
1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]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
-
-
0.0773
benzamidine
Homo sapiens
-
-
0.0000028
BMS-262084
Homo sapiens
at pH 7.4 and 37°C
0.12
boronic acid
Homo sapiens
-
-
0.0013
clavatadine A
Homo sapiens
-
0.027
clavatadine B
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
0.022
[4-(carbamimidamidomethyl)phenyl]boronic acid
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.83
-
-
additional information
-
cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type andmutant substrate, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FA11_HUMAN
625
0
70109
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
136100
-
nonglycosylated, cysteinylated FXI dimer, MALDI-TOF mass spectrometry
146400
-
FXI, SDS-PAGE
160000
30000
-
method not mentioned
35000
-
x * 35000, x * 48000, SDS-PAGE, 2 chains
362500
catalytic domain, wild-type, SDS-PAGE
48000
-
x * 35000, x * 48000, SDS-PAGE, 2 chains
68000
-
2 * 68000, SDS-PAGE
72626
-
1 * 72626, mutant FXI/G326C, SDS-PAGE
72630
-
mutant FXI/G326C, SDS-PAGE
73210
-
2 * 73210, FXI, SDS-PAGE
79600
-
1 * 79600, SDS-PAGE
80000
85600
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
monomer
polymer
-
x * 35000, x * 48000, SDS-PAGE, 2 chains
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
the enzyme bears five N-glycosylation consensus sites per monomer
proteolytic modification
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 method
hanging drop vapor diffusion
hanging drop vapour 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C147S
-
inactive
C321S
-
the mutant shows wild type activity
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
C500S
inactive
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
FXI/G326C
-
mutant of FXI with Gly326 residue mutated to Cys326
G104R
this mutation in the PK A2 domain associated with CRM+ PK deficiency causes decreased kininogen binding
G155E
is a rare example of a mutation causing CRM+ FXI deficieny
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
P520L
-
site-directed mutagenesis, similar to the wild-ype enzyme
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
R37Q
fXIa-R37Q mutant
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
S248A
binds platelets with reduced affinity compared with wild-type
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
S248Q
binds platelets with reduced affinity compared with wild-type
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
factor XIa-triggered thrombin generation assays are not affected by glycoPEGylation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
affinity chromatography with antibody 5F7, gel filtration
-
antibody-affinity chromatography by using the calcium-dependent anti-human fIX monoclonal IgG SB 249417
-
immobilized Zn2-chelate chromatography and cation exchange chromatography
-
light chain
-
method not mentioned
native enzyme from plasma and recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity chromatography with elution by benzamidine
-
Ni-NTA column chromatography
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNAs in expression vector pJVCMV are used to transfect HEK-293 cells
expressed in baby hamster kidney cells
-
expressed in HEK293 cells
-
expressed in Pichia pastoris
expressed in Pichia pastoris strain X-33
-
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
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
-
individual apple domains of FXI with a tPA-tag
recombinant human fXI is expressed in HEK-293 cells
stable expression of wild-type and mutant enzymes in HEK-293 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kalwant, S.; Porter, A.G.
Purification and characterization of human brain prolyl endopeptidase
Biochem. J.
276
237-244
1991
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Pedicord, D.L.; Seiffert, D.; Blat, Y.
Substrate-dependent modulation of the mechanism of factor XIa inhibition
Biochemistry
43
11883-11888
2004
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Emsley, J.; McEwan, P.A.; Gailani, D.
Structure and function of factor XI
Blood
115
2569-2577
2010
Mus musculus, Homo sapiens (P03951)
Manually annotated by BRENDA team
Gailani, D.; Smith, S.B.
Structural and functional features of factor XI
J. Thromb. Haemost.
7 Suppl 1
75-78
2009
Homo sapiens (P03951)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Meijers, J.
Prochemerin processing by factor XIa
Blood
131
275-276
2018
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team