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Information on EC 3.4.21.22 - coagulation factor IXa 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
                3.4.21.22 coagulation factor IXa
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Select one or more organisms in this record: ?
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 expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Selective cleavage of Arg-/-Ile bond in factor X to form factor Xa
Synonyms
factor ix, factor ixa, coagulation factor ix, activated factor ix, intrinsic xase, activated fix, coagulation factor ixa, factor ixabeta, activated coagulation factor ix, factor ixan, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
activated Christmas factor
-
-
-
-
activated coagulation factor IX
-
-
activated factor IX
activated FIX
-
-
blood coagulation factor IXa
-
-
Christmas factor
-
-
-
-
circulating factor IXa
-
-
coagulation factor IX
coagulation factor IXa
-
factor IX
-
-
factor IXa
factor IXaAL
-
variant protein, D47G
factor IXabeta
-
-
factor IXaCH
-
variant protein, R145H
factor IXalphabeta
-
-
factor IXaN
-
normal protein
factor XIa
-
human coagulation factor IXa
-
-
intrinsic Xase
-
additional information
the enzyme is a member of the serine protease family and shares a high degree of homology with trypsin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
additional information
-
amidolytic activity
CAS REGISTRY NUMBER
COMMENTARY hide
37316-87-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(methylsulfonyl)-D-cyclohexylalanine-Gly-Arg-7-amido-4-methylcoumarin + H2O
(methylsulfonyl)-D-cyclohexylalanine-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Pefa10
-
-
?
(methylsulfonyl)-D-cyclohexylglycine-Gly-Arg-7-amido-4-methylcoumarin + H2O
(methylsulfonyl)-D-cyclohexylglycine-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Pefa9
-
-
?
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide + H2O
4-methylsulfonyl-D-Leu-Gly-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
acetyl-L-Ala-Gly-Arg-Ser-Leu-amide + H2O
?
show the reaction diagram
-
-
-
-
?
CBS 31.39 + H2O
?
show the reaction diagram
-
i.e. CH3SO2-D-Leu-Gly-L-Arg-4-nitroanilide
-
-
?
CBS 48.03 + H2O
?
show the reaction diagram
-
i.e. CH3OCO-D-Leu-Gly-L-Arg-4-nitroanilide
-
-
?
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide + H2O
?
show the reaction diagram
CH3SO2-D-Leu-Gly-L-Arg-p-nitroanilide + H2O
CH3SO2-D-Leu-Gly-L-Arg + p-nitroaniline
show the reaction diagram
D-cyclohexylglycyl-Gly-Arg-7-amido-4-methylcoumarin + H2O
D-cyclohexylglycyl-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
D-cyclohexylglycyl-Gly-Arg-p-nitroanilide + H2O
D-cyclohexylglycyl-Gly-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
D-Leu-Phe-Gly-Arg-4-nitroanilide + H2O
D-Leu-Phe-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Leu-Phg-Arg-4-nitroanilide + H2O
D-Leu-Phg-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
factor X
?
show the reaction diagram
-
activation of factor X to factor Xa
-
-
?
factor X + H2O
?
show the reaction diagram
-
a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa
-
-
?
factor X + H2O
activated factor X + ?
show the reaction diagram
factor X + H2O
factor Xa
show the reaction diagram
Factor X + H2O
Factor Xa + ?
show the reaction diagram
factor X + H2O
fragments of factor X
show the reaction diagram
-
-
-
?
L-Leu-Gly-L-Arg-4-nitroanilide + H2O
L-Leu-Gly-L-Arg + 4-nitroaniline
show the reaction diagram
-
CBS 31.39
-
-
?
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-arginyl-p-nitroanilide + H2O
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
rFIXa, ethanol, 25% v/v enhances the activity 6fold, methanol 4fold, ethylene glycol, 25-40% v/v enhances the activity up to 20fold, glycerol, 50% v/v enhances the activity 6fold
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-cyclohexylglycyl-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
assay at 37°C
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide + H2O
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
methylsulfonyl-D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-alpha-benzyloxycarbonyl-D-arginylglycyl-L-arginine-para-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginylglycyl-L-arginine + para-nitroaniline
show the reaction diagram
-
-
-
?
Nalpha-benzyloxycarbonyl-D-Arg-Gly-Arg-4-nitroanilide + H2O
Nalpha-benzyloxycarbonyl-D-Arg-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
S-2765
-
-
?
p-aminobenzamidine + H2O
p-aminobenzoic acid + NH3
show the reaction diagram
-
-
-
?
Pefa-5523 + H2O
?
show the reaction diagram
-
-
-
-
?
Pefachrome IXa + H2O
?
show the reaction diagram
S-2366 + H2O
?
show the reaction diagram
-
-
-
-
?
Spectrofluor FIXa + H2O
(methylsulfonyl)-D-cyclohexylglycine-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
i.e. (methylsulfonyl)-D-cyclohexylglycine-Gly-Arg-7-amido-4-methylcoumarin
-
-
?
Spectrozyme FIXa + H2O
?
show the reaction diagram
-
i.e. D-Leu-phenylated Gly-L-Arg-4-nitroanilide
-
-
?
Spectrozyme FXIIa
?
show the reaction diagram
-
i.e. D-cyclohexyl-Thr-Gly-L-Arg-4-nitroanilide
-
-
?
Spectrozyme t-PA + H2O
?
show the reaction diagram
-
i.e. CH3SO2-D-cyclohexyl-Thr-Gly-L-Arg-4-nitroanilide
-
-
?
tert-butoxycarbonyl-Ile-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
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
D-Leu-Phg-Arg-4-nitroanilide + H2O
D-Leu-Phg-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
factor X
?
show the reaction diagram
-
activation of factor X to factor Xa
-
-
?
factor X + H2O
?
show the reaction diagram
-
a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa
-
-
?
factor X + H2O
activated factor X + ?
show the reaction diagram
factor X + H2O
factor Xa
show the reaction diagram
Factor X + H2O
Factor Xa + ?
show the reaction diagram
factor X + H2O
fragments of factor X
show the reaction diagram
-
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-cyclohexylglycyl-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
assay at 37°C
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Factor VIIIa
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lithium ion
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activates slightly
additional information
factor IXa is not a Na+-binding protease
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-carbamimidoylbenzo[b]thiophen-4-yloxy)phenylacetic acid methyl ester
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(2-carbamimidoylbenzo[b]thiophen-6-yloxy)thiophen-2-ylacetic acid ethyl ester
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-
(2E)-3-[(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-10-yl]prop-2-enoic acid
-
-
(2R)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
(2R)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
(2S)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
(2S)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
(7S)-2-methyl-7-phenyl-7-[4-(4H-1,2,4-triazol-4-yl)benzamido]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-2-methyl-7-phenyl-7-[[5-(4H-1,2,4-triazol-4-yl)pyridine-2-carbonyl]amino]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-7-[2-chloro-4-(1H-tetrazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxamide
-
-
1,5-dansyl-Glu-Gly-Arg chloromethylketone
-
1-(3-chloro-4-[[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]carbamoyl]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
2,6-dichloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)-N-[(2R)-8-methyl-2-[3-(trifluoromethyl)phenyl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]benzamide
-
-
2,6-dichloro-N-((R)-2-((S)-1-hydroxyethyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2-(3,4-difluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2-(3-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2-(4-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-8-methyl-2-(3-methylphenyl)-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-8-methyl-2-[1-(propan-2-yl)-1H-1,2,3-triazol-4-yl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(3R)-3,7-dimethyl-2,3,4,9-tetrahydro-1H-carbazol-3-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2-(2-carbamimidoylbenzo[b]thiophen-4-yloxy)propionic acid methyl ester
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-(4-[3-(trifluoromethyl)-1H-pyrazol-1-yl]phenyl)propanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-[4-(4-phenyl-1H-imidazol-1-yl)phenyl]propanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-cyanophenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-methylphenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-phenoxyphenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-[(6-chloropyridazin-3-yl)sulfamoyl]phenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(5-fluoro-2-methylphenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-(2'-sulfamoylbiphenyl-4-yl)propanamide
-
-
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-[4-(5-phenyl-1H-imidazol-4-yl)phenyl]propanamide
-
-
2-(5-carbamimidoyl-1H-indol-3-yl)-N-(2'-sulfamoylbiphenyl-4-yl)acetamide
-
-
2-(5-carbamimidoyl-1H-indol-3-yl)-N-(4-ethylphenyl)-3-phenylpropanamide - 1H-benzimidazole
-
(1:1)
2-(7-carbamimidoylnaphthalen-1-yl)-N-[2-(1-ethoxyethenyl)cyclohexyl]-3-phenylpropanamide
-
-
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)-N-ethylcyclohexanecarboxamide
-
-
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylic acid
-
-
2-amidino-4-iodobenzothiophene
-
-
2-chloro-N-[(2R)-2-(3-methoxyphenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2-chloro-N-[(2R)-8-methyl-2-phenyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2-chloro-N-[(7S)-10-cyclopropyl-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[(7S)-10-[(E)-(hydroxyimino)methyl]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2,2,2-trifluoro-1-hydroxyethyl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2H-tetrazol-5-yl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[3-methyl-1-(4-methyl-2-nitrophenyl)pyrrolidin-3-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenyl-N-[4-(pyrrolidin-1-ylcarbonyl)phenyl]acetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (1,3-dimethyl-1H-pyrazol-5-yl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,4-difluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,6-difluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-fluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-methylphenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-[[(2-methylpropyl)amino]methyl]phenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1,2-oxazol-4-yl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1H-pyrazol-4-yl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3-fluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-fluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-methoxyphenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl phenylcarbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1,3-dimethyl-5-[(propan-2-ylamino)methyl]-1H-pyrazol-4-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1-methyl-3-[(methylamino)methyl]-1H-pyrazol-5-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(piperazin-1-ylmethyl)phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(methylamino)methyl]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [3-(methoxymethyl)-1-methyl-1H-pyrazol-5-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[(4-methylpiperazin-1-yl)methyl]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[2-(dimethylamino)ethoxy]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [5-[(ethylamino)methyl]-1,3-dimethyl-1H-pyrazol-4-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N,2-diphenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(2-methoxyphenyl)-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(3-methoxyphenyl)-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(4-methoxyphenyl)-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-[2-(dimethylamino)ethyl]-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]-2-(4-fluorophenyl)acetamide
-
-
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl phenylcarbamate
-
-
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
-
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
-
3-(1-[4-(1H-benzimidazol-1-yl)phenyl]-2-oxopyrrolidin-3-yl)-1-benzothiophene-5-carboximidamide
-
-
3-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-3-(4-chlorophenyl)propionic acid methyl ester
-
-
3-(2-[4-(1H-benzimidazol-1-yl)phenyl]-1-benzyl-2-oxoethyl)-1-benzothiophene-5-carboximidamide
-
-
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)propanamide
-
-
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
3-[(7R)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-4a,6,7,8,9,10a-hexahydropyrido[1,2-a]indol-10-yl]propanoic acid
-
-
3-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]benzoic acid
-
-
4-(([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)methyl)-N-[5-(methylsulfonyl)-1H-benzimidazol-2-yl]benzamide
-
-
4-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-4-(4-chlorophenyl) butyric acid methyl ester
-
-
4-(benzyloxy)-1-benzothiophene-2-carboximidamide
-
-
4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)-N,N-dimethylbenzamide
-
-
4-aminobenzamidine
-
4-cyano-2-fluoro-N-(10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)benzamide
-
-
4-phenyl-1-benzothiophene-2-sulfinimidamide
-
-
4-[phenyl(3-phenyl[1,2,4]oxadiazol-5-yl)methoxy]benzo[b]thiophene-2-carboxamidine
-
-
5-(3,4-dimethoxyphenyl)benzo[b]thiophene-2-carboxamidine
-
-
5-(benzyloxy)-1-benzothiophene-2-carboximidamide
-
-
5-phenyl-1-benzothiophene-2-carboximidamide
-
-
6-(2-phenylethoxy)-1-benzothiophene-2-carboximidamide
-
-
6-(3,4-dimethoxyphenyl)-1-benzothiophene-2-carboximidamide
-
-
6-(3-chloro-4-fluorobenzyloxy)benzo[b]thiophene-2-carboxamidine
-
-
6-(pyridin-3-ylmethoxy)-1-benzothiophene-2-carboximidamide
-
-
6-(thiophen-2-ylmethoxy)benzo[b]thiophene-2-carboxamidine
-
-
6-benzyloxybenzo[b]thiophene-2-carboxamidine
-
-
6-[(2-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(2-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(2-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(3,4-difluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(3-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(3-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(3-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(4-chloro-3-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(4-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(4-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(4-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[(4-methylbenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
-
6-[1-(4-fluorophenyl)ethoxy]-1-benzothiophene-2-carboximidamide
-
-
antithrombin
-
antithrombin III
-
aptamer
-
RNA aptamers isolated by iterative in vitro selection technique, complete inhibition at 0.00004 mM, inhibition is reversed by specific antidotes, i.e. oligonucleotides, complementary to the aptamers
-
Bovine pancreatic trypsin inhibitor
-
-
-
BPTI
Kunitz-type inhibitor, competitive, reversible inhibition, low molecular weight heparin binding to fIXa enhances reactivity of fIXa with the Kunitz-type inhibitor BPTI
-
D-Phe-Pro-Arg chloromethylketone
-
enoxaparin
competitive, reversible inhibition
ethyl 1-[4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)phenyl]-1H-imidazole-2-carboxylate
-
-
ethyl 2-([2-(5-carbamimidoyl-1,1-dioxido-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
ethyl 2-([2-(5-carbamimidoyl-1-benzofuran-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
ethyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
ethyl [(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]acetate
-
-
ethyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]acetate
-
-
ethyl [4-[([2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethoxy]carbonyl)amino]-3,5-dimethyl-1H-pyrazol-1-yl]acetate
-
-
FIX1-47 peptide
-
benzoylphenylalanine containing peptide, 0.038 mM, 50% inhibition
-
Glu-Gly-Arg chloromethylketone
-
heparin
-
in the presence of 0.3 mM bovine pancreatic trypsin inhibitor
methyl (1R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl (1S,2R)-2-(2-[(2R)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl (1S,2R)-2-(2-[(2S)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl (1S,2R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
methyl 2-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
methyl 3-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)propanoate
-
-
methyl 4-[[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]methyl]benzoate
-
-
methyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-chlorophenyl)acetate
-
-
methyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-fluorophenyl)acetate
-
-
N-(2-amino-2-oxoethyl)-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
N-(4-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]phenyl)benzamide
-
-
N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
N-1H-benzimidazol-2-yl-3-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
N-1H-benzimidazol-2-yl-4-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
N-benzyl-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
N-benzyl-2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylacetamide
-
-
N-[(3R)-1-(3-amino-4,5-dichloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-2-oxo-1,2-dihydropyrimidin-5-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-5-oxo-1,5-dihydro-4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-6-oxo-1,6-dihydropyridin-3-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1H-imidazo[4,5-b]pyridin-1-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-2-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-5-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[3-(difluoromethyl)-4H-1,2,4-triazol-4-yl]benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[4-(2-hydroxyethyl)-1H-imidazol-1-yl]benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-4-(1H-benzimidazol-1-yl)-2-chlorobenzamide
-
N-[(3R)-1-(3-amino-4-fluoro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-5-methyl[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(7S)-10-(5-aminopyridin-3-yl)-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
N-[1-(3-amino-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[1-(3-amino-5-methyl-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[1-(3-amino[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[2-(5,6-dimethyl-1H-benzimidazol-2-yl)ethyl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1-methyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(6-carbamimidoyl-1H-indol-1-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-naphthalen-1-ylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)butanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-2-methylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-(4-[(phenylsulfonyl)amino]phenyl)propanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-cyclohexylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-naphthalen-2-ylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-pyridin-3-ylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)butanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
N-[4-(1H-benzimidazol-2-yl)phenyl]-2-benzyl-3-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
N-[4-(1H-benzimidazol-2-yl)phenyl]-3-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
Na+
200 mM in the absence of Ca2+, 185 mM in the presence of 5 mM Ca2+
PN2-KPI
Kunitz-type inhibitor, competitive, reversible inhibition
-
Polyethylene glycol
-
inhibition with increasing concentration
Rb+
-
slightly inhibiting in presence of Ca2+
RB006
-
-
-
recombinant full-length tissue factor pathway inhibitor
-
-
-
supersulfated low molecular weight heparin
-
inhibits the intrinsic tenase (factor IXa-factor VIIIa) complex in an antithrombin-independent manner by 90% when using factor X as substrate. Supersulfated low molecular weight heparin is 32fold more potent than unmodified low molecular weight heparin in the inhibition of factor X activation by the intrinsic tenase complex
-
TFPI-K1
Kunitz-type inhibitor, competitive, reversible inhibition
-
unmodified low molecular weight heparin
-
-
-
[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-fluorophenyl)acetic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dicaproyl-sn-glycero-3-phospho-L-serine
-
up-regulates the catalytic activity of the enzyme
1,2-propanediol
-
25-40% v/v, up to 20fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa
1,3-Propanediol
1,4-Butanediol
-
affect the activity only to a slight extent, rFIXa
anionic phospholipid
highly activating
-
cofactor VIIIa
-
-
-
diethylene glycol
-
increases the activity 2fold
emicizumab
-
factorIXa/factorX bispecific antibody. Emicizumab functions as a cofactor to promote the factor IXa-catalyzed factor X activation
-
enoxaparin
-
in the presence of bovine pancreatic trypsin inhibitor
ethanol
-
25% v/v, 6fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa, alcohols modify the conformation of FIXa rendering the active-site cleft more easily accessible to tripeptide substrates with a hydrophobic residue in the P3-position
ethylene glycol
factor FVIIa
in complex with tissue factor and Ca2+
-
factor FVIIIa
-
factor FXIa
in presence of 5 mM CaCl2
-
factor IX
-
concentrations of approximately 100 nM, physiological levels in plasma, increases the activation of factor X catalyzed by factor IXa by increasing the affinity of the factor X for the intrinsic factor X activation complex
-
factor IX-specific antibodies
-
antibosies specific for human factor I, e.g. 198A1, 198B3, and 224F3, enhance the factor IXa activity mimicking the stimulatory effect of FVIIIa, and thus can replace FVIIIa as cofactor in the FX activation reaction, overview
-
factor VIIa/tissue factor
-
-
-
factor VIII
-
in modified form, established in the activation of factor X
-
Factor VIIIa
-
Factor XIa
-
factor XIa proteolytically activates factor IX by an exosite- and Ca2+-mediated release-rebind mechanism. XIa cleaves IX after Arg145, forming IXalpha, and then after Arg180, forming IXabeta
-
FIXa
-
12.5 nM in Tris buffered saline/Ca2+ for 2 h at 37 °C
-
FVIII
-
in absence of FVIIIa decreased catalytic activity of enzyme FIXa
-
GIGAVLKVLTTGLPALISSWIKRKRQQ
-
approx. 600fold lower km, slight increase in kcat
glycerol
-
50% v/v, 6fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa
heparin
i-erythritol
-
50% v/v, 1.5fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa
low molecular weight heparin
-
enhances the activity of factor IXa (0.01 mM used in assay conditions)
-
methanol
-
25% v/v, 4fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa, alcohols modify the conformation of FIXa rendering the active-site cleft more easily accessible to tripeptide substrates with a hydrophobic residue in the P3-position
phosphatidylserine
-
up-regulates the catalytic activity of the enzyme
Phospholipid
phospholipid membrane
-
Phospholipids
platelet factor 3
-
in vivo, established in the activation of factor X
-
tert-butanol
-
up to 10% v/v, increase of the activity, higher concentrations lead to a drastic activity decrease, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa, alcohols modify the conformation of FIXa rendering the active-site cleft more easily accessible to tripeptide substrates with a hydrophobic residue in the P3-position
tissue factor
-
-
-
TRYLRIHPQSWVHQIALRMEV
-
approx. 600fold lower km, slight increase in kcat, optimal activation in the presence of 0.5-1 mM Ca2+
vitamin K
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 8.7
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
1.7 - 3.2
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
2.3
CH3SO2-D-Leu-Gly-L-Arg-p-nitroanilide
-
0.000001 - 0.38
Factor X
-
1.2 - 2.3
L-Leu-Gly-L-Arg-4-nitroanilide
3.62
methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
1.43
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
5.99
methylsulfonyl-D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 3.38
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
18.5 - 21.9
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
13.2
CH3SO2-D-Leu-Gly-L-Arg-p-nitroanilide
-
0.00011 - 1999
Factor X
-
17.5 - 21.4
L-Leu-Gly-L-Arg-4-nitroanilide
2.01
methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
5.67
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
6.11
methylsulfonyl-D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011 - 0.00037
D-Leu-Phg-Arg-4-nitroanilide
0.83 - 54500
Factor X
-
9.3 - 14.6
L-Leu-Gly-L-Arg-4-nitroanilide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005
(2-carbamimidoylbenzo[b]thiophen-4-yloxy)phenylacetic acid methyl ester
-
pH and temperature not specified in the publication
0.000003
(2-carbamimidoylbenzo[b]thiophen-6-yloxy)thiophen-2-ylacetic acid ethyl ester
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0000008
(2E)-3-[(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-10-yl]prop-2-enoic acid
-
pH and temperature not specified in the publication
0.00048
(2R)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.000018
(2R)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.01422
(2S)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.00082
(2S)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.0000006
(7S)-2-methyl-7-phenyl-7-[4-(4H-1,2,4-triazol-4-yl)benzamido]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000025
(7S)-2-methyl-7-phenyl-7-[[5-(4H-1,2,4-triazol-4-yl)pyridine-2-carbonyl]amino]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000086
(7S)-7-[2-chloro-4-(1H-tetrazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000006
(7S)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000012
(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxamide
-
pH and temperature not specified in the publication
0.0000063 - 0.0000348
1-(3-chloro-4-[[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]carbamoyl]phenyl)-1H-benzimidazole-5-carboxylic acid
0.0000045
2,6-dichloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)-N-[(2R)-8-methyl-2-[3-(trifluoromethyl)phenyl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]benzamide
-
pH and temperature not specified in the publication
0.0000125
2,6-dichloro-N-((R)-2-((S)-1-hydroxyethyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000102 - 0.0000121
2,6-dichloro-N-[(2R)-10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.0000102
2,6-dichloro-N-[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000105
2,6-dichloro-N-[(2R)-2-(3,4-difluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000031 - 0.0000066
2,6-dichloro-N-[(2R)-2-(3-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.0000042
2,6-dichloro-N-[(2R)-2-(4-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000018
2,6-dichloro-N-[(2R)-8-methyl-2-(3-methylphenyl)-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.000005
2,6-dichloro-N-[(2R)-8-methyl-2-[1-(propan-2-yl)-1H-1,2,3-triazol-4-yl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000117 - 0.0002676
2,6-dichloro-N-[(3R)-3,7-dimethyl-2,3,4,9-tetrahydro-1H-carbazol-3-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.00515
2-(2-carbamimidoylbenzo[b]thiophen-4-yloxy)propionic acid methyl ester
-
pH and temperature not specified in the publication
0.0001
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-(4-[3-(trifluoromethyl)-1H-pyrazol-1-yl]phenyl)propanamide
-
-
0.00039
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-[4-(4-phenyl-1H-imidazol-1-yl)phenyl]propanamide
-
-
0.00173
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-cyanophenyl)-3-phenylpropanamide
-
-
0.00058
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-methylphenyl)-3-phenylpropanamide
-
-
0.00025
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-phenoxyphenyl)-3-phenylpropanamide
-
-
0.00093
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-[(6-chloropyridazin-3-yl)sulfamoyl]phenyl)-3-phenylpropanamide
-
-
0.0096
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(5-fluoro-2-methylphenyl)-3-phenylpropanamide
-
-
0.00066
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-(2'-sulfamoylbiphenyl-4-yl)propanamide
-
-
0.00027
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-[4-(5-phenyl-1H-imidazol-4-yl)phenyl]propanamide
-
-
0.0067
2-(5-carbamimidoyl-1H-indol-3-yl)-N-(2'-sulfamoylbiphenyl-4-yl)acetamide
-
-
0.00031
2-(5-carbamimidoyl-1H-indol-3-yl)-N-(4-ethylphenyl)-3-phenylpropanamide - 1H-benzimidazole
-
(1:1)
0.00024
2-(7-carbamimidoylnaphthalen-1-yl)-N-[2-(1-ethoxyethenyl)cyclohexyl]-3-phenylpropanamide
-
-
0.00043
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)-N-ethylcyclohexanecarboxamide
-
-
0.0035
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylic acid
-
-
0.00095
2-amidino-4-iodobenzothiophene
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000003
2-chloro-N-[(2R)-2-(3-methoxyphenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000021 - 0.0000069
2-chloro-N-[(2R)-8-methyl-2-phenyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.0000051 - 0.0000084
2-chloro-N-[(7S)-10-cyclopropyl-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
0.0000024 - 0.0000029
2-chloro-N-[(7S)-10-[(E)-(hydroxyimino)methyl]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
0.0000026 - 0.0000055
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2,2,2-trifluoro-1-hydroxyethyl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
0.0000024
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2H-tetrazol-5-yl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.00029
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenyl-N-[4-(pyrrolidin-1-ylcarbonyl)phenyl]acetamide
-
pH and temperature not specified in the publication
0.00001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (1,3-dimethyl-1H-pyrazol-5-yl)carbamate
-
pH and temperature not specified in the publication
0.000007
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,4-difluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000007
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,6-difluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-fluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-methylphenyl)carbamate
-
pH and temperature not specified in the publication
0.000002
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-[[(2-methylpropyl)amino]methyl]phenyl)carbamate
-
pH and temperature not specified in the publication
0.000012
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1,2-oxazol-4-yl)carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1H-pyrazol-4-yl)carbamate
-
pH and temperature not specified in the publication
0.000025
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3-fluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-fluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-methoxyphenyl)carbamate
-
pH and temperature not specified in the publication
0.00001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl phenylcarbamate
-
pH and temperature not specified in the publication
0.000003
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1,3-dimethyl-5-[(propan-2-ylamino)methyl]-1H-pyrazol-4-yl]carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1-methyl-3-[(methylamino)methyl]-1H-pyrazol-5-yl]carbamate
-
pH and temperature not specified in the publication
0.000004
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
pH and temperature not specified in the publication
0.000003
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(piperazin-1-ylmethyl)phenyl]carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000003
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(methylamino)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000009
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [3-(methoxymethyl)-1-methyl-1H-pyrazol-5-yl]carbamate
-
pH and temperature not specified in the publication
0.00001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[(4-methylpiperazin-1-yl)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000004
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[2-(dimethylamino)ethoxy]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [5-[(ethylamino)methyl]-1,3-dimethyl-1H-pyrazol-4-yl]carbamate
-
pH and temperature not specified in the publication
0.00017
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N,2-diphenylacetamide
-
pH and temperature not specified in the publication
0.00014
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(2-methoxyphenyl)-2-phenylacetamide
-
pH and temperature not specified in the publication
0.00013
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(3-methoxyphenyl)-2-phenylacetamide
-
pH and temperature not specified in the publication
0.00014
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(4-methoxyphenyl)-2-phenylacetamide
-
pH and temperature not specified in the publication
0.001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-[2-(dimethylamino)ethyl]-2-phenylacetamide
-
pH and temperature not specified in the publication
0.00198
2-[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]-2-(4-fluorophenyl)acetamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0000155
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl phenylcarbamate
-
pH and temperature not specified in the publication
0.0000044
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
pH and temperature not specified in the publication
0.0000081
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.0049
3-(1-[4-(1H-benzimidazol-1-yl)phenyl]-2-oxopyrrolidin-3-yl)-1-benzothiophene-5-carboximidamide
-
-
0.000028
3-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-3-(4-chlorophenyl)propionic acid methyl ester
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000063
3-(2-[4-(1H-benzimidazol-1-yl)phenyl]-1-benzyl-2-oxoethyl)-1-benzothiophene-5-carboximidamide
-
-
0.000074
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)propanamide
-
-
0.000075
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
0.0000027 - 0.0000138
3-[(7R)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-4a,6,7,8,9,10a-hexahydropyrido[1,2-a]indol-10-yl]propanoic acid
0.000059
3-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]benzoic acid
-
-
0.00066
4-(([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)methyl)-N-[5-(methylsulfonyl)-1H-benzimidazol-2-yl]benzamide
-
-
0.000036
4-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-4-(4-chlorophenyl) butyric acid methyl ester
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0015
4-(benzyloxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00037
4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)-N,N-dimethylbenzamide
-
pH and temperature not specified in the publication
2
4-cyano-2-fluoro-N-(10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)benzamide
-
pH and temperature not specified in the publication
0.0016
4-phenyl-1-benzothiophene-2-sulfinimidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00027
4-[phenyl(3-phenyl[1,2,4]oxadiazol-5-yl)methoxy]benzo[b]thiophene-2-carboxamidine
-
pH and temperature not specified in the publication
0.0059
5-(3,4-dimethoxyphenyl)benzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0019
5-(benzyloxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.008
5-phenyl-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0216
6-(2-phenylethoxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0008 - 0.0242
6-(3,4-dimethoxyphenyl)-1-benzothiophene-2-carboximidamide
0.000031
6-(3-chloro-4-fluorobenzyloxy)benzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00035
6-(pyridin-3-ylmethoxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00035
6-(thiophen-2-ylmethoxy)benzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0038
6-benzyloxybenzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0072
6-[(2-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.023
6-[(2-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0269
6-[(2-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00045
6-[(3,4-difluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0009
6-[(3-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00068
6-[(3-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00045
6-[(3-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000075
6-[(4-chloro-3-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00045
6-[(4-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0007
6-[(4-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00025
6-[(4-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0009
6-[(4-methylbenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0113
6-[1-(4-fluorophenyl)ethoxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.037 - 0.7
Bovine pancreatic trypsin inhibitor
-
0.00042
ethyl 1-[4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)phenyl]-1H-imidazole-2-carboxylate
-
pH and temperature not specified in the publication
0.00853
ethyl 2-([2-(5-carbamimidoyl-1,1-dioxido-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.0019
ethyl 2-([2-(5-carbamimidoyl-1-benzofuran-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.00012
ethyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.0119
ethyl [(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0038
ethyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000011
ethyl [4-[([2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethoxy]carbonyl)amino]-3,5-dimethyl-1H-pyrazol-1-yl]acetate
-
pH and temperature not specified in the publication
0.0005
methyl (1R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.00028
methyl (1S,2R)-2-(2-[(2R)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.0413
methyl (1S,2R)-2-(2-[(2S)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.00031
methyl (1S,2R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.00014
methyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.00034
methyl 2-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.0084
methyl 3-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)propanoate
-
pH and temperature not specified in the publication
0.0113
methyl 4-[[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]methyl]benzoate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00002
methyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-chlorophenyl)acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00004
methyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-fluorophenyl)acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00028
N-(2-amino-2-oxoethyl)-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
0.00027
N-(4-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]phenyl)benzamide
-
-
0.00078
N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.0019
N-1H-benzimidazol-2-yl-3-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
0.00093
N-1H-benzimidazol-2-yl-4-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
0.032
N-benzyl-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
0.00039
N-benzyl-2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylacetamide
-
pH and temperature not specified in the publication
0.0000016
N-[(7S)-10-(5-aminopyridin-3-yl)-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
9
N-[2-(5,6-dimethyl-1H-benzimidazol-2-yl)ethyl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.00036
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1-methyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.000063
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.0003
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(6-carbamimidoyl-1H-indol-1-yl)-3-phenylpropanamide
-
-
0.00023
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-naphthalen-1-ylpropanamide
-
-
0.000098
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.00024
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)butanamide
-
-
0.00075
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-2-methylpropanamide
-
-
0.00013
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-(4-[(phenylsulfonyl)amino]phenyl)propanamide
-
-
0.0038
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-cyclohexylpropanamide
-
-
0.000098
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-naphthalen-2-ylpropanamide
-
-
0.0012
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-pyridin-3-ylpropanamide
-
-
0.00024
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
0.00016
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)butanamide
-
-
0.00048
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
0.00013
N-[4-(1H-benzimidazol-2-yl)phenyl]-2-benzyl-3-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
0.00025
N-[4-(1H-benzimidazol-2-yl)phenyl]-3-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
0.025 - 0.813
Na+
0.0000025 - 0.00017
supersulfated low molecular weight heparin
-
0.00001 - 0.00147
unmodified low molecular weight heparin
-
0.000021
[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-fluorophenyl)acetic acid
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
additional information
additional information
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022
2-chloro-N-[3-methyl-1-(4-methyl-2-nitrophenyl)pyrrolidin-3-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000047
N-[(3R)-1-(3-amino-4,5-dichloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000032
N-[(3R)-1-(3-amino-4-chloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000036
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-2-oxo-1,2-dihydropyrimidin-5-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000015
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-5-oxo-1,5-dihydro-4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000018
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-6-oxo-1,6-dihydropyridin-3-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000013
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1H-imidazo[4,5-b]pyridin-1-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000033
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000031
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.003
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-2-yl)benzamide
Homo sapiens
IC50 above 0.003 mM, at pH 8.0 and 25°C
0.000026
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-5-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000045
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[3-(difluoromethyl)-4H-1,2,4-triazol-4-yl]benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000013
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[4-(2-hydroxyethyl)-1H-imidazol-1-yl]benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000032
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-4-(1H-benzimidazol-1-yl)-2-chlorobenzamide
Homo sapiens
at pH 8.0 and 25°C
0.000172
N-[(3R)-1-(3-amino-4-fluoro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000041
N-[(3R)-1-(3-amino-5-methyl[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000098
N-[1-(3-amino-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000018 - 0.000062
N-[1-(3-amino-5-methyl-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
0.000089
N-[1-(3-amino[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 7.4
-
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
factor IXa binds specifically to the surface of endothelial cells
Manually annotated by BRENDA team
additional information
-
binding of a subpopulation of platelets to the enzyme is activated by the protease-activated receptor-1, PAR-1, requirring both release of calcium from internal stores and influx of extracellular calcium, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
factor IXa is a critical enzyme for the formation of stable blood clots
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FA9_HUMAN
461
0
51778
Swiss-Prot
Secretory Pathway (Reliability: 2)
Q19UG2_HUMAN
182
0
20589
TrEMBL
other Location (Reliability: 1)
A0A8F0WQF6_HUMAN
461
0
51819
TrEMBL
Secretory Pathway (Reliability: 2)
Q19UG5_HUMAN
182
0
20649
TrEMBL
other Location (Reliability: 1)
A0A8F0WPL7_HUMAN
461
0
51692
TrEMBL
Secretory Pathway (Reliability: 2)
Q19UH8_HUMAN
182
0
20634
TrEMBL
other Location (Reliability: 1)
Q19UI5_HUMAN
182
0
20621
TrEMBL
other Location (Reliability: 1)
Q19UG9_HUMAN
182
0
20677
TrEMBL
other Location (Reliability: 1)
Q19UG8_HUMAN
182
0
20631
TrEMBL
other Location (Reliability: 1)
Q19UI1_HUMAN
182
0
20680
TrEMBL
other Location (Reliability: 1)
Q19UI4_HUMAN
182
0
20589
TrEMBL
other Location (Reliability: 1)
Q19UG4_HUMAN
182
0
20707
TrEMBL
other Location (Reliability: 1)
Q19UH9_HUMAN
182
0
20635
TrEMBL
other Location (Reliability: 1)
A0A8F0WPP1_HUMAN
461
0
51942
TrEMBL
Secretory Pathway (Reliability: 2)
Q19UJ0_HUMAN
182
0
20679
TrEMBL
other Location (Reliability: 1)
Q19UG3_HUMAN
182
0
20679
TrEMBL
other Location (Reliability: 1)
F2RM35_HUMAN
461
0
51712
TrEMBL
Secretory Pathway (Reliability: 4)
F2RM37_HUMAN
461
0
51744
TrEMBL
Secretory Pathway (Reliability: 2)
Q19UH5_HUMAN
182
0
20621
TrEMBL
other Location (Reliability: 1)
Q19UI3_HUMAN
182
0
20692
TrEMBL
other Location (Reliability: 1)
Q19UG1_HUMAN
182
0
20726
TrEMBL
other Location (Reliability: 1)
Q19UG6_HUMAN
181
0
20535
TrEMBL
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
-
1 * 27000 + 1 * 17000, SDS-PAGE
18000
-
1 * 28000 + 1 * 18000, SDS-PAGE
27000
-
1 * 27000 + 1 * 17000, SDS-PAGE
28000
-
1 * 28000 + 1 * 18000, SDS-PAGE
44000
-
non reducing SDS-PAGE
56000
x * 56000, SDS-PAGE
57000
6000
-
x * 6000, SDS-PAGE
70000
-
value about, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
the fully active enzyme consists of a light and a heavy chain held together by a single disulfie bond
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
activated mutant K98T, sitting drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 18-24% (w/v) PEG6000
hanging drop vapor diffusion method, using 0.25 M ammonium acetate, 19.5% (w/v) PEG 3350
of a recombinant two-domain construct of fIXa in complex with p-benzamidine. The 99-loop on Tyr99 plays a major role in substrate interaction, it may be rearranged in the factor X activation complex
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D47G
-
factor IXaAL, causes lower rates of factor X activation, Asp47 and the cleavage of Arg145-Ala146 are important structural features required for specific, high affinity factor IXa binding to platelets in the presence of factors VIIIa and factor X
E186A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
E410A
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
E410H
-
the mutant with reduced hydrolytic activity and increased in-vitro clotting activity has 2.5fold enhanced affinity for the cofactor FVIIIa and induces 5.2fold higher thrombin generation compared to the wild type enzyme
E410L
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
E410N
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
FIXagamma225P
mutant enzyme
G94R
-
33% of wild-type vmax
Gla-domainless factor IXa
20000times lower kacat for factor X hydrolysis than wild-type
H185A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
K126A
K132A
K265A
-
no change in binding of anti fIX monoclonal antibodies CLB-fIX 14 and CLB-fIX 13
K98A
site-directed mutagenesis,
K98T
the variant demonstrates a 2fold improvement in kcat/KM value for Pefa9 as compared to the wild type enzyme
K98T/R150A/I213V
the mutations result in a 4fold increase in kinetic efficiency compared with the wild type enzyme
N129A
N178A
N346D
-
no change in binding of anti fIX monoclonal antibodies CLB-fIX 14, no binding of anti fIX monoclonal antibody CLB-fIX 13
R143A
4times lower kcat for factor X hydrolysis than wild-type Gla-domainless factor IXa
R145H
-
factor IXaCH, causes lower rates of factor X activation, Asp47 and the cleavage of Arg145-Ala146 are important structural features required for specific, high affinity factor IXa binding to platelets in the presence of factors VIIIa and factor X
R147A
3times lower kcat for factor X hydrolysis than wild-type Gla-domainless factor IXa
R150
similar kcat for factor X hydrolysis as wild-type Gla-domainless factor IXa
R150A
the mutation reduces potential autolysis in the 148-loop during production and leads to reduced activity compared to the wild type enzyme
R150A/I213V
the variant shows increases in the catalytic efficiency for amidolytic activity when the target substrate is either Pefa9 or Pefa10 with 1.5fold and 1.2fold increases, respectively
R165A
R170A
-
the mutation slightly (0.5fold) reduces supersulfated low molecular weight heparin affinity
R188A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
R233A
-
the mutation dramatically (14fold) reduces supersulfated low molecular weight heparin affinity
R333Q
activation of factor X is not impaired
R94D
-
slight increase in vmax
rFIXa104A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa105A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa107A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa89A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa90A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa91A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa94A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
V16I/I21/V R150A
the variant results in a negligible increase in activity compared with the V16I/R150A variant
V16I/K98T/I213V
the mutations result in a 4fold increase in kinetic efficiency compared with the wild type enzyme
V16I/K98T/I213V/R150A
the mutations result in a 6fold increase in kinetic efficiency compared with the wild type enzyme
V16I/K98T/R150A
the mutant shows enhancements in activity leading to a 2.5fold increased kinetic efficiency compared with the wild type enzyme
V16I/K98T/Y177T/I213V
the variant reduces the kinetic efficiency to the 4fold increase that is also observed with the K98T/R150A/I213V variant
V16I/R150A
the variant shows no increase in the kcat/KM value for Pefa9 as compared to the wild type enzyme
Y450C
-
the mutant shows about 5% activity compared to the wild type enzyme
Y450F
-
the mutant shows about 25% activity compared to the wild type enzyme
Y450S
-
the mutant shows about 5% activity compared to the wild type enzyme
Y94F/A95aK/K98T/Y177F
-
mutation, higher clotting activity than wild type FIXa
Y94F/A95aK/K98T/Y177F/I213V/E219G
-
about 6fold increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T
-
increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T/Y177F
-
increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T/Y177F/I213V/E219G
-
about 17fold increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22°C, recombinant human FIX in soybean seeds, 6 years, no loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
combination of anion exchange and affinity/cation exchange chromatography
-
DEAE-Sepharose column chromatography and HiTrap Q column chromatography
-
gel filtration
heparin Sepharose column chromatography and Q Sepharose column chromatography
HiPrep Q column chromatography and Superdex 75 gel filtration
HiTrap Q column chromatography and HiTrap heparin column chromatography
-
ion exchange chromatography on Q-Sepharose
ion-exchange chromatography
-
method not mentioned
-
Ni-NTA column chromatography, gel filtration
-
Q-Sepharose of column, affinity purification with heparin sepharose, gel filtration
recombinant factor IXa
-
recombinant fIXa
-
recombinant wild-type and mutant enzymes from HEK-293 cells by anion exchange and heparin affinity chromatography
recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity and anion exchange chromatogaphy
recombinant wild-type and mutant factor IXa, immunoaffinity chromatography using HPC4 monoclonal antibodies
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Star (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli DH5alpha cells
-
expressed in Escherichia coli NiCo21(DE3) cells
expressed in HEK-293 cells
-
expressed in HEK293 cells
expressed in Huh-7 cells
-
expressed in human embryonic kidney 293 cell line
-
expressed in modified HEK-293 cell line Flp-In-293
-
expressed in transgenic seeds of Glycine max
expression in CHO cells
-
expression in Escherichia coli BL21
expression in HEK 293 cells
-
expression in HEK293 cells
expression of wild-type and mutant enzymes in HEK-293 cells
stable expression of wild-type and mutant enzymes in HEK-293 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thompson, A.R.
Structure, function and molecular defects of factor IX
Blood
67
565-572
1986
Homo sapiens
Manually annotated by BRENDA team
Osterud, B.; Bouma, B.N.; Griffin, J.H.
Human blood coagulation factor IX
J. Biol. Chem.
253
5946-5951
1978
Homo sapiens
Manually annotated by BRENDA team
Sturzebecher, J.; Kopetzki, E.; Bode, W.; Hopfner, K.P.
Dramatic enhancement of the catalytic activity of coagulation factor IXa by alcohols
FEBS Lett.
412
295-300
1997
Homo sapiens
Manually annotated by BRENDA team
London, F.S.; Walsh, P.N.
Zymogen factor IX potentiates factor IXa-catalyzed activation
Biochemistry
39
9850-9858
2000
Homo sapiens
Manually annotated by BRENDA team
Hopfner, K.P.; Lang, A.; Karcher, A.; Sichler, K.; Kopetzki, E.; Barndstetter, H.; Huber, R.; Bode, W.; Engh, R.A.
Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding
Structure Fold. Des.
7
989-996
1999
Homo sapiens
Manually annotated by BRENDA team
Fay, P.J.; Koshibu, K.; Mastri, M.
The A1 and the A2 subunits of factor VIIIa synergistically stimulate factor IXa catalytic activity
J. Biol. Chem.
274
15401-15406
1999
Homo sapiens
Manually annotated by BRENDA team
Ahmed, S.S.; Rawala-Sheikh, R.; Monroe, D.M.; Roberts, H.R.; Walsh, P.N.
Comparative platelet binding and kinetic studies with normal and variant factor IXa molecules
J. Biol. Chem.
265
20907-20911
1990
Homo sapiens
Manually annotated by BRENDA team
Blostein, M.D.; Rigby, A.C.; Furie, B.C.; Furie, B.; Gilbert, G.E.
Amphipathic helices support function of blood coagulation factor IXa
Biochemistry
39
12000-12006
2000
Homo sapiens
Manually annotated by BRENDA team
Falls, L.A.; Furie, B.; Furie, B.C.
Role of phosphatidylethanolamine in assembly and function of the factor IXa-factor VIIIa complex on membrane surfaces
Biochemistry
39
13216-13222
2000
Homo sapiens
Manually annotated by BRENDA team
Ahmad, S.S.; Walsh, P.N.
Coordinate binding studies of the substrate (factor X) with the cofactor (factor VIII) in the assembly of the factor X activating complex on the activated platelet surface
Biochemistry
41
11269-11276
2002
Homo sapiens
Manually annotated by BRENDA team
Bedsted, T.; Swanson, R.; Chuang, Y.J.; Bock, P.E.; Bjork, I.; Olson, S.T.
Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites
Biochemistry
42
8143-8152
2003
Homo sapiens
Manually annotated by BRENDA team
Bajaj, S.P.; Schmidt, A.E.; Mathur, A.; Padmanabhan, K.; Zhong, D.; Mastri, M.; Fay, P.J.
Factor IXa:factor VIIIa interaction. helix 330-338 of factor ixa interacts with residues 558-565 and spatially adjacent regions of the a2 subunit of factor VIIIa
J. Biol. Chem.
276
16302-16309
2001
Homo sapiens (P00740)
Manually annotated by BRENDA team
Wilkinson, F.H.; London, F.S.; Walsh, P.N.
Residues 88-109 of factor IXa are important for assembly of the factor X activating complex
J. Biol. Chem.
277
5725-5733
2002
Homo sapiens
Manually annotated by BRENDA team
Yang, L.; Manithody, C.; Olson, S.T.; Rezaie, A.R.
Contribution of basic residues of the autolysis loop to the substrate and inhibitor specificity of factor IXa
J. Biol. Chem.
278
25032-25038
2003
Homo sapiens (P00740)
Manually annotated by BRENDA team
Blostein, M.D.; Furie, B.C.; Rajotte, I.; Furie, B.
The Gla domain of factor IXa binds to factor VIIIa in the tenase complex
J. Biol. Chem.
278
31297-31302
2003
Homo sapiens
Manually annotated by BRENDA team
Wiebe, E.M.; Stafford, A.R.; Fredenburgh, J.C.; Weitz, J.I.
Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide
J. Biol. Chem.
278
35767-35774
2003
Homo sapiens
Manually annotated by BRENDA team
Rohlena, J.; Kolkman, J.A.; Boertjes, R.C.; Mertens, K.; Lenting, P.J.
Residues Phe342-Asn346 of activated coagulation factor IX contribute to the interaction with low density lipoprotein receptor-related protein
J. Biol. Chem.
278
9394-9401
2003
Homo sapiens
Manually annotated by BRENDA team
Rusconi, C.P.; Scardino, E.; Layzer, J.; Pitoc, G.A.; Ortel, T.L.; Monroe, D.; Sullenger, B.A.
RNA aptamers as reversible antagonists of coagulation factor IXa
Nature
419
90-94
2002
Homo sapiens
Manually annotated by BRENDA team
Panteleev, M.A.; Saenko, E.L.; Ananyeva, N.M.; Ataullakhanov, F.I.
Kinetics of Factor X activation by the membrane-bound complex of Factor IXa and Factor VIIIa
Biochem. J.
381
779-794
2004
Homo sapiens
Manually annotated by BRENDA team
Yang, X.; Walsh, P.N.
An ordered sequential mechanism for Factor IX and Factor IXa binding to platelet receptors in the assembly of the Factor X-activating complex
Biochem. J.
390
157-167
2005
Homo sapiens
Manually annotated by BRENDA team
Neuenschwander, P.F.
Exosite occupation by heparin enhances the reactivity of blood coagulation factor IXa
Biochemistry
43
2978-2986
2004
Homo sapiens
Manually annotated by BRENDA team
Batt, D.G.; Qiao, J.X.; Modi, D.P.; Houghton, G.C.; Pierson, D.A.; Rossi, K.A.; Luettgen, J.M.; Knabb, R.M.; Jadhav, P.K.; Wexler, R.R.
5-Amidinoindoles as dual inhibitors of coagulation factors IXa and Xa
Bioorg. Med. Chem. Lett.
14
5269-5273
2004
Homo sapiens
Manually annotated by BRENDA team
Qiao, J.X.; Cheng, X.; Modi, D.P.; Rossi, K.A.; Luettgen, J.M.; Knabb, R.M.; Jadhav, P.K.; Wexler, R.R.
5-Amidinobenzo[b]thiophenes as dual inhibitors of factors IXa and Xa
Bioorg. Med. Chem. Lett.
15
29-35
2005
Homo sapiens
Manually annotated by BRENDA team
Lu, G.; Broze, G.J.; Krishnaswamy, S.
Formation of factors IXa and Xa by the extrinsic pathway: differential regulation by tissue factor pathway inhibitor and antithrombin III
J. Biol. Chem.
279
17241-17249
2004
Homo sapiens
Manually annotated by BRENDA team
Butenas, S.; Orfeo, T.; Gissel, M.T.; Brummel, K.E.; Mann, K.G.
The significance of circulating factor IXa in blood
J. Biol. Chem.
279
22875-22882
2004
Homo sapiens
Manually annotated by BRENDA team
Yang, X.; Chang, Y.J.; Lin, S.W.; Walsh, P.N.
Identification of residues Asn89, Ile90, and Val107 of the factor IXa second epidermal growth factor domain that are essential for the assembly of the factor X-activating complex on activated platelets
J. Biol. Chem.
279
46400-46405
2004
Homo sapiens (P00740)
Manually annotated by BRENDA team
Schmidt, A.E.; Stewart, J.E.; Mathur, A.; Krishnaswamy, S.; Bajaj, S.P.
Na+ site in blood coagulation factor IXa: effect on catalysis and factor VIIIa binding
J. Mol. Biol.
350
78-91
2005
Homo sapiens (P00740)
Manually annotated by BRENDA team
Ndonwi, M.; Broze, G.; Bajaj, S.P.
The first epidermal growth factor-like domains of factor Xa and factor IXa are important for the activation of the factor VII-tissue factor complex
J. Thromb. Haemost.
3
112-118
2005
Homo sapiens
Manually annotated by BRENDA team
London, F.S.; Marcinkiewicz, M.; Walsh, P.N.
PAR-1-stimulated factor IXa binding to a small platelet subpopulation requires a pronounced and sustained increase of cytoplasmic calcium
Biochemistry
45
7289-7298
2006
Homo sapiens
Manually annotated by BRENDA team
Misenheimer, T.M.; Buyue, Y.; Sheehan, J.P.
The heparin-binding exosite is critical to allosteric activation of factor IXa in the intrinsic tenase complex: the role of arginine 165 and factor X
Biochemistry
46
7886-7895
2007
Homo sapiens
Manually annotated by BRENDA team
Neuenschwander, P.F.; Williamson, S.R.; Nalian, A.; Baker-Deadmond, K.J.
Heparin modulates the 99-loop of factor IXa: effects on reactivity with isolated Kunitz-type inhibitor domains
J. Biol. Chem.
281
23066-23074
2006
Homo sapiens (P00740)
Manually annotated by BRENDA team
Gale, A.J.; Radtke, K.P.; Cunningham, M.A.; Chamberlain, D.; Pellequer, J.L.; Griffin, J.H.
Intrinsic stability and functional properties of disulfide bond-stabilized coagulation factor VIIIa variants
J. Thromb. Haemost.
4
1315-1322
2006
Homo sapiens
Manually annotated by BRENDA team
Scheiflinger, F.; Dockal, M.; Rosing, J.; Kerschbaumer, R.J.
Enhancement of the enzymatic activity of activated coagulation factor IX by anti-factor IX antibodies
J. Thromb. Haemost.
6
315-322
2008
Homo sapiens
Manually annotated by BRENDA team
Yang, L.; Gopalakrishna, K.; Manithody, C.; Rezaie, A.R.
Expression, purification and characterization of factor IX derivatives using a novel vector system
Protein Expr. Purif.
50
196-202
2006
Homo sapiens (P00740)
Manually annotated by BRENDA team
Gopalakrishna, K.; Rezaie, A.R.
The influence of sodium ion binding on factor IXa activity
Thromb. Haemost.
95
936-941
2006
Homo sapiens
Manually annotated by BRENDA team
Zoegg, T.; Brandstetter, H.
Activation mechanisms of coagulation factor IX
Biol. Chem.
390
391-400
2009
Homo sapiens
Manually annotated by BRENDA team
Yang, Y.H.; Chien, D.; Wu, M.; FitzGerald, J.; Grossman, J.M.; Hahn, B.H.; Hwang, K.K.; Chen, P.P.
Novel autoantibodies against the activated coagulation factor IX (FIXa) in the antiphospholipid syndrome that interpose the FIXa regulation by antithrombin
J. Immunol.
182
1674-1680
2009
Homo sapiens
Manually annotated by BRENDA team
Becker, R.C.; Oney, S.; Becker, K.C.; Sullenger, B.
Antidote-controlled antithrombotic therapy targeting factor IXa and von Willebrand factor
Ann. N. Y. Acad. Sci.
1175
61-70
2009
Homo sapiens
Manually annotated by BRENDA team
Gettins, P.G.; Olson, S.T.
Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement
FEBS Lett.
583
3397-3400
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, W.H.; Kim, J.S.; Kim, J.S.; Yoon, Y.; Lee, G.M.
Effect of Ca2+ and Mg2+ concentration in culture medium on the activation of recombinant factor IX produced in Chinese hamster ovary cells
J. Biotechnol.
142
275-278
2009
Homo sapiens
Manually annotated by BRENDA team
Hartmann, R.; Dockal, M.; Kammlander, W.; Panholzer, E.; Nicolaes, G.A.; Fiedler, C.; Rosing, J.; Scheiflinger, F.
Factor IX mutants with enhanced catalytic activity
J. Thromb. Haemost.
7
1656-1662
2009
Homo sapiens
Manually annotated by BRENDA team
Zgg, T.; Brandstetter, H.
Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa
Structure
17
1669-1678
2009
Homo sapiens (P00740), Homo sapiens
Manually annotated by BRENDA team
Hosseini, S.; Zomorodipour, A.; Jalal, R.; Sabouni, F.; Ataei, F.
A study of the expression of functional human coagulation factor IX in keratinocytes using a nonviral vector regulated by K14 promoter
Appl. Biochem. Biotechnol.
162
1599-1611
2010
Homo sapiens
Manually annotated by BRENDA team
Misenheimer, T.M.; Sheehan, J.P.
The regulation of factor IXa by supersulfated low molecular weight heparin
Biochemistry
49
9997-10005
2010
Homo sapiens
Manually annotated by BRENDA team
Yang, L.; Manithody, C.; Qureshi, S.H.; Rezaie, A.R.
Role of the residues of the 39-loop in determining the substrate and inhibitor specificity of factor IXa
J. Biol. Chem.
285
28488-28495
2010
Homo sapiens
Manually annotated by BRENDA team
Wang, S.; Beck, R.; Blench, T.; Burd, A.; Buxton, S.; Malic, M.; Ayele, T.; Shaikh, S.; Chahwala, S.; Chander, C.; Holland, R.; Merette, S.; Zhao, L.; Blackney, M.; Watts, A.
Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors in thrombosis
J. Med. Chem.
53
1465-1472
2010
Homo sapiens
Manually annotated by BRENDA team
Wang, S.; Beck, R.; Burd, A.; Blench, T.; Marlin, F.; Ayele, T.; Buxton, S.; Dagostin, C.; Malic, M.; Joshi, R.; Barry, J.; Sajad, M.; Cheung, C.; Shaikh, S.; Chahwala, S.; Chander, C.; Baumgartner, C.; Holthoff, H.P.; Murray, E.; Blackney, M.; Giddings, A.
Structure based drug design: development of potent and selective factor IXa (FIXa) inhibitors
J. Med. Chem.
53
1473-1482
2010
Homo sapiens
Manually annotated by BRENDA team
Chang, L.; Yang, C.; Chua, A.; Lin, Y.; Lai, S.
Sustained release of transgenic human factor IX: Preparation, characterization, and in vivo efficacy
Mol. Pharm.
8
1767-1774
2011
Homo sapiens
Manually annotated by BRENDA team
Johnson, D.J.; Langdown, J.; Huntington, J.A.
Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex
Proc. Natl. Acad. Sci. USA
107
645-650
2010
Homo sapiens (P00740)
Manually annotated by BRENDA team
Wu, H.; Xu, X.; Zhang, L.; Shen, D.; Peng, L.; Zhang, Y.; Song, J.
Mg(II)-induced binding of factor IX-binding protein from the venom of Agkistrodon Halys Pallas with factor Xa
Toxicon
55
1358-1364
2010
Homo sapiens
Manually annotated by BRENDA team
Cunha, N.; Murad, A.; Ramos, G.; Maranhao, A.; Brgido, M.; Araujo, A.; Lacorte, C.; Aragao, F.; Covas, D.; Fontes, A.; Souza, G.; Vianna, G.; Rech, E.
Accumulation of functional recombinant human coagulation factor IX in transgenic soybean seeds
Transgenic Res.
20
841-855
2011
Homo sapiens (P00740), Homo sapiens
Manually annotated by BRENDA team
Venkateswarlu, D.
Structural insights into the interaction of blood coagulation co-factor VIIIa with factor IXa: a computational protein-protein docking and molecular dynamics refinement study
Biochem. Biophys. Res. Commun.
452
408-414
2014
Homo sapiens
Manually annotated by BRENDA team
Branchini, A.; Campioni, M.; Mazzucconi, M.; Biondo, F.; Mari, R.; Bicocchi, M.; Bernardi, F.; Pinotti, M.
Replacement of the Y450 (c234) phenyl ring in the carboxyl-terminal region of coagulation factor IX causes pleiotropic effects on secretion and enzyme activity
FEBS Lett.
587
3249-3253
2013
Homo sapiens
Manually annotated by BRENDA team
Sullenger, B.; Woodruff, R.; Monroe, D.M.
Potent anticoagulant aptamer directed against factor IXa blocks macromolecular substrate interaction
J. Biol. Chem.
287
12779-12786
2012
Homo sapiens
Manually annotated by BRENDA team
Geng, Y.; Verhamme, I.M.; Messer, A.; Sun, M.F.; Smith, S.B.; Bajaj, S.P.; Gailani, D.
A sequential mechanism for exosite-mediated factor IX activation by factor XIa
J. Biol. Chem.
287
38200-38209
2012
Homo sapiens
Manually annotated by BRENDA team
Bloem, E.; Meems, H.; van den Biggelaar, M.; Mertens, K.; Meijer, A.B.
A3 domain region 1803-1818 contributes to the stability of activated factor VIII and includes a binding site for activated factor IX
J. Biol. Chem.
288
26105-26111
2013
Homo sapiens
Manually annotated by BRENDA team
Wakabayashi, H.; Fay, P.J.
Replacing the factor VIII C1 domain with a second C2 domain reduces factor VIII stability and affinity for factor IXa
J. Biol. Chem.
288
31289-31297
2013
Homo sapiens
Manually annotated by BRENDA team
Neuenschwander, P.F.; Deadmond, K.J.; Zepeda, K.; Rutland, J.
Correlation of factor IXa subsite modulations with effects on substrate discrimination
J. Thromb. Haemost.
10
382-389
2012
Homo sapiens
Manually annotated by BRENDA team
Majumder, R.; Koklic, T.; Sengupta, T.; Cole, D.; Chattopadhyay, R.; Biswas, S.; Monroe, D.; Lentz, B.R.
Soluble phosphatidylserine binds to two sites on human factor IXa in a Ca2+ dependent fashion to specifically regulate structure and activity
PLoS ONE
9
e100006
2014
Homo sapiens
Manually annotated by BRENDA team
Kristensen, L.H.; Olsen, O.H.; Blouse, G.E.; Brandstetter, H.
Releasing the brakes in coagulation factor IXa by co-operative maturation of the substrate-binding site
Biochem. J.
473
2395-2411
2016
Homo sapiens (P00740)
Manually annotated by BRENDA team
Meng, D.; Andre, P.; Bateman, T.J.; Berger, R.; Chen, Y.H.; Desai, K.; Dewnani, S.; Ellsworth, K.; Feng, D.; Geissler, W.M.; Guo, L.; Hruza, A.; Jian, T.; Li, H.; Metzger, J.; Parker, D.L.; Reichert, P.; Sherer, E.C.; Smith, C.J.; Sonatore, L.M.; Tschirret-Guth, R.; Wu, J.; Xu, J.; Zhang, T.; Campeau, L.C.; Orr,
Development of a novel tricyclic class of potent and selective FIXa inhibitors
Bioorg. Med. Chem. Lett.
25
5437-5443
2015
Homo sapiens
Manually annotated by BRENDA team
Sakurada, I.; Endo, T.; Hikita, K.; Hirabayashi, T.; Hosaka, Y.; Kato, Y.; Maeda, Y.; Matsumoto, S.; Mizuno, T.; Nagasue, H.; Nishimura, T.; Shimada, S.; Shinozaki, M.; Taguchi, K.; Takeuchi, K.; Yokoyama, T.; Hruza, A.; Reichert, P.; Zhang, T.; Wood, H.B.; Nakao, K.; Furusako, S.
Discovery of novel aminobenzisoxazole derivatives as orally available factor IXa inhibitors
Bioorg. Med. Chem. Lett.
27
2622-2628
2017
Homo sapiens (P00740)
Manually annotated by BRENDA team
Kitazawa, T.; Shima, M.
Emicizumab, a humanized bispecific antibody to coagulation factors IXa and X with a factor VIIIa-cofactor activity
Int. J. Hematol.
111
20-30
2018
Homo sapiens
Manually annotated by BRENDA team
Perot, E.; Enjolras, N.; Le Quellec, S.; Indalecio, A.; Girard, J.; Negrier, C.; Dargaud, Y.
Expression and characterization of a novel human recombinant factor IX molecule with enhanced in vitro and in vivo clotting activity
Thromb. Res.
135
1017-1024
2015
Homo sapiens
Manually annotated by BRENDA team