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Enzyme Nomenclature
Information on EC 3.4.21.27 - coagulation factor XIa
for references in articles please use BRENDA:EC3.4.21.27
Word Map on EC 3.4.21.27
- 3.4.21.27
- bleeding
- thrombin
- clot
- platelet
-
kininogen
-
prekallikrein
-
anticoagulant
-
kallikrein
- thrombosis
-
prothrombin
-
viii
-
fibrinogen
-
hemostasis
-
antithrombin
- hemophilia
- willebrand
-
thromboembolic
- fibrin
-
procoagulant
-
fibrinolysis
-
zymogen
- plasmin
-
antithrombotic
-
ashkenazy
- diathesis
-
jewish
- coagulopathy
- fxiia
-
kaolin
-
hageman
-
amidolytic
-
haemostatic
-
leiden
- menorrhagia
-
antifibrinolytic
- thrombophilias
- meningosepticum
-
gamma-carboxyglutamic
- drug development
-
proline-specific
-
fletcher
-
recalcified
-
thrombin-activatable
-
tranexamic
-
basque
-
anti-factor
-
c1-inhibitor
-
non-jewish
-
proline-containing
-
tenase
-
viia-tissue
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.21.27
-
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RECOMMENDED NAME
GeneOntology No.
coagulation factor XIa
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Selective cleavage of Arg-/-Ala and Arg-/-Val bonds in factor IX to form factor IXa
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
37203-61-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
36529, 36530, 36531, 36532, 36536, 36537, 36538, 36539, 36540, 36541, 649981, 650724, 652013, 652309, 652338, 667059, 667583, 667611, 667620, 669347, 669420, 669428, 683167, 683239, 683682, 684078, 710600, 717333, 717416, 717844, 717958, 718042, 718045, 731462, 731466, 731538, 731570, 731773, 732313, 732897, 732936
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
activated partial thromboplastin time is abnormal in all cases with severe or moderate FXI deficiency. FXI deficiency is not an absolute contraindication to neuraxial anesthesia
malfunction
-
FXI deficiency is a rare inherited coagulation disorder characterized by infrequent spontaneous bleeding, but increased risk of hemorrhagic complications especially after trauma or surgery
malfunction
-
a deficiency in FXI (hemophilia C) results in a more benign bleeding phenotype compared with a deficiency in either FVIII (hemophilia A) or FIX (hemophilia B). Most hemophilia C cases involve Ashkenazi Jews and result from either of 2 mutations in the FXI gene (E117X and F283L). Greater than 180 mutations are present but in lesser frequency. FXI deficiency also arises from acquired inhibitors that neutralize its activity, these patients may not respond well to FXI replacement therapy. Bleeding in those with hemophilia C is rarely spontaneous, it tends to occur in response to surgery or trauma, and especially in tissue prone to fibrinolysis (the urinary track or oral cavity). Prolonged activated partial thromboplastin time due to FXI deficiency
malfunction
-
FXI-null mice are healthy, and their reproduction follows the expected mendelian ratios without impaired fecundity. FXI-null mice are protected against oxidative iron chloride-induced carotid artery thrombosis and infusion of human FXI reverses this protection. Thrombus formation in FXI-null mice is also reduced in response to laser injury of arterioles in the cremaster muscle. FXI deletion is also effective in preserving carotid artery blood flow in response to compression injury
malfunction
-
congenital FXI deficiency is associated with a variable, mild to moderate bleeding disorder. Severe deficiency is prevalent in people of Jewish ancestry. The severe mutation Glu117Stop encodes a truncated protein, and homozygotes lack plasma FXI antigen. The more subtle missense mutation Phe283Leu causes a defect in FXI dimer formation. Most cases of FXI deficiency are associated with low plasma levels of FXI protein. Deficiency or inhibition of FXI interferes with platelet accumulation in growing thrombi. A4 domain mutations associated with FXI deficiency interfere with dimerization. FXI-deficient plasma exhibits a prolonged activated partial thromboplastin clotting time
malfunction
-
mice lacking FIX, FXI, or FXII on a background of low tissue factor expression have a severe bleeding disorder but are viable. Superimposing FIX or FXI deficiency on the low tissue factor background results in death in utero from bleeding
malfunction
-
FXI deficient humans suffer from mild hemorrhage (hemophilia C), which is characterized by trauma or soft tissue-related hemorrhage, primarily involving tissues with high fibrinolytic activity. Bleeding severity in FXI deficiency is not associated with FXI plasma levels. Addition of murine FXI to human FXI deficient plasma rescues the prolonged activated partial thromboplastin time, but with a slightly reduced activity compared with the human protein
malfunction
-
addition of murine FXI to human FXI deficient plasma rescues the prolonged activated partial thromboplastin time, but with a slightly reduced activity compared with the human protein. FXI-/- mice are healthy, fertile, and phenotypically indistinguishable from wild-type animals. Mating between heterozygous FXI+/- mice follows the expected Mendelian ratio arguing against an association of FXI deficiency and increased risk of abortion. Plasma from FXI null mice show a severely prolonged activated partial thromboplastin time compared with wild-type animals. Bleeding times in adult FXI-/- mice are indistinguishable from wild-type animals, suggesting that FXI does not significantly contribute to fibrin formation. Formation of thrombi is severely defective in FXI-/- mice. Both fibrin deposition and platelet accumulation are reduced in FXI null mice compared with wild-type. FXI deficiency increases survival and reduces leukocyte infiltration and coagulopathy
malfunction
-
patients who have a very severe FXI deficiency are prone to development of inhibitor antibodies. During major surgeries, a single low dose of recombinant activated factor VII and tranexamic acid secure normal haemostasis in patients with severe FXI deficiency who can not receive blood products
malfunction
-
factor XI deficiency can lead to delayed clot formation and decreased thrombin generation
malfunction
-
enzyme deficiency results in bleeding diathesis referred to as hemophilia C
physiological function
-
FXI is a biomarker with increased levels reported as a risk factor for venous thromboembolism and myocardial ischemia or stroke
physiological function
-
involvment of FXI in thrombosis, role for activated factor FXI in tissue infammation
physiological function
-
FXI is the zymogen of a blood coagulation protease, factor XIa (activated factor IX), that contributes to hemostasis through activation of factor IX. Almost all FXI circulate in a complex with kininogen
physiological function
-
FXI is the zymogen of a plasma protease that contributes to fibrin formation and stability by activating factor IX. Circulates in plasma in complex with high molecular weight kininogen
physiological function
-
the opossum genome has two distinct genes for both FXI and plasma kallikrein, indicating that the gene duplication event leading to separate factors occurred early in mammalian evolution
physiological function
-
78% homology to human FXI at the protein level. FXI is critical for fibrin formation in vivo. FXI may have additional functions in regulation of inflammation or tissue repair distinct from its role in coagulation
physiological function
-
presence of a single precursor of FXI and plasma kallikrein, appearance of FXI among early tetrapods
physiological function
-
activated factor XI inhibits chemotaxis of polymorphonuclear leukocytes. Coagulation factor XI participates in the intrinsic coagulation pathway upon its activation, contributing to hemostasis and thrombosis. Factor XIa attenuates N-formylmethionyl-leucyl-phenylalanine-induced Ca2+mobilization
physiological function
-
factor XIa plays its major role in promoting late thrombin formation (i.e. the thrombin required for thrombin activatable fibrinolysis inhibitor-mediated inhibition of fibrinolysis)
physiological function
-
activated factor XI increases the procoagulant activity of the extrinsic pathway by inactivating tissue factor pathway inhibitor
physiological function
-
factor XI is important in the tissue factor-independent propagation phase of clot formation, not in the initiation process
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-2-glycoprotein I + H2O
clipped beta-2-glycoprotein I
-
cleavage at Lys317-Thr318
-
-
?
Boc-Glu(OBzl)-Ala-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Glu(OBzl)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
substrate S-2288
-
-
?
factor V + H2O
activated factor V + ?
-
fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
-
-
?
factor VIII + H2O
activated factor VIII + ?
-
fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
-
-
?
Fibrinogen + H2O
?
-
Aalpha-chain and Bbeta-chain, gamma-chain after prolonged incubation
-
-
?
Gly-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyro-Glu-Pro-Arg-4-nitroanilide + H2O
L-pyro-Glu-Pro-Arg + 4-nitroaniline
-
i.e. S-2366
-
-
?
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroGlu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroglutamyl-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-7-amido-4-methylcoumarin + H2O
L-pyroglutamyl-L-prolyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
?
-
substrate S-299
-
-
?
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-arginine-p-nitroanilide + H2O
N-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-Cbz-D-arginylglycyl-L-arginyl-4-nitroanilide + H2O
N-Cbz-D-arginylglycyl-L-arginine + 4-nitroaniline
-
-
-
-
?
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tissue factor pathway inhibitor + H2O
?
-
the cleavage of the protein occurs between the Kunitz (K)1 and K2 domains (Lys86/Thr87) and at the active sites of the K2 (Arg107/Gly108) and K3 (Arg199/Ala200) domains
-
-
?
Z-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
factor IX
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
-
factor IX
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
-
factor IX + H2O
activated factor IX + ?
-
-
-
-
?
factor IX + H2O
activated factor IX + ?
-
model for factor IX activation in which FXIa binds to activated platelets by one chain of the dimer, while binding to factor IX through the other
-
?
factor IX + H2O
activated factor IX + ?
-
factor XIa has a role in the intrinsic pathway of coagulation, and plays a significant role in venous thrombosis
-
-
?
factor IX + H2O
activated factor IX + ?
-
factor XIa is essential for the optimal activation of FIX
-
-
?
factor IX + H2O
activated factor IX + ?
-
two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX
-
-
?
factor IX + H2O
activated factor IX + ?
-
cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type and mutant substrate, overview
-
-
?
factor IX + H2O
activated factor IX + ?
-
cleavage of Arg145-Ala146, and Arg180-Val181, macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX-activation, mechanisms of activation, overview
-
-
?
factor IX + H2O
activated factor IX + ?
-
natural cleavage sites on FIX performed by FXIa, overview
-
-
?
factor IX + H2O
activated factor IX + ?
-
FXI is converted to the active protease by cleavage of the Arg369-Ile370 bond on each subunit. This converts the catalytic domains to the active forms, and unmasks exosites on the apple domains required for FIX binding
-
-
?
factor IX + H2O
factor IXa + ?
-
-
-
-
?
factor IX + H2O
factor IXa + ?
-
after binding to factor XIa, factor IX undergoes a single cleavage to form the intermediate factor IXalpha. FIXalpha then rebinds to the A3 domain to undergo a second cleavage, generating factor IXalphabeta
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
?
pro-HGF + H2O
?
-
HGF i. e. hepatocyte growth factor, pro-HGF is processed by cleavage at two sites: Arg494-Val 495 and Arg424-His425. Cleavage at Arg424-His425 is independent of a prior cleavage at the primary kinetically preferred Arg 494-Val495 site. The mutant substrate pro-HGF(R424A/R494E) is completely resistant to cleavage
-
?
pro-HGF + H2O
?
-
the enzyme may regulate processes that involve the HGF/c-Met pathway, such as tissue repair and angiogenesis
-
?
additional information
?
-
-
specific and saturable zinc-dependent FXIa binding is demonstrated to 250 sites per activated platelet and 6.5 sites per umbilical vein endothelial cell. No binding to HEK293 cells is detected
-
?
additional information
?
-
-
a conformational transition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain zymogen factor XI platelet binding site and exposes the factor XIa platelet binding site within the catalytic domain possibly comprising residues Cys527-Cys542
-
-
-
additional information
?
-
-
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, overview
-
-
-
additional information
?
-
-
FXI contains 4 apple domains that form a disk structure with extensive interfaces at the base of the catalytic domain. Binding of FXI to platelets requires residues in the FXI A3 domain. Platelets bind and spread on glass coated with FXI
-
-
-
additional information
?
-
-
FXI is a homodimer, with each subunit containing four apple domains and a protease domain: the apple domains form a disk structure with binding sites for platelets
-
-
-
additional information
?
-
-
platelets bind and spread on glass coated with FXI. Platelets from ApoER2-deficient mice do not bind FXI
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
factor V + H2O
activated factor V + ?
-
fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
-
-
?
factor VIII + H2O
activated factor VIII + ?
-
fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
-
-
?
pro-HGF + H2O
?
-
the enzyme may regulate processes that involve the HGF/c-Met pathway, such as tissue repair and angiogenesis
-
?
tissue factor pathway inhibitor + H2O
?
-
the cleavage of the protein occurs between the Kunitz (K)1 and K2 domains (Lys86/Thr87) and at the active sites of the K2 (Arg107/Gly108) and K3 (Arg199/Ala200) domains
-
-
?
factor IX
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
-
factor IX
?
-
activation of Factor IX in the intrinsic coagulation cascade
-
-
-
factor IX + H2O
activated factor IX + ?
-
-
-
-
?
factor IX + H2O
activated factor IX + ?
-
factor XIa has a role in the intrinsic pathway of coagulation, and plays a significant role in venous thrombosis
-
-
?
factor IX + H2O
activated factor IX + ?
-
factor XIa is essential for the optimal activation of FIX
-
-
?
factor IX + H2O
activated factor IX + ?
-
two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX
-
-
?
factor IX + H2O
factor IXa + ?
-
-
-
-
?
factor IX + H2O
factor IXa + ?
-
after binding to factor XIa, factor IX undergoes a single cleavage to form the intermediate factor IXalpha. FIXalpha then rebinds to the A3 domain to undergo a second cleavage, generating factor IXalphabeta
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
fondaparinux pentasaccharide, all catalytic domains exhibit similar inhibition to catalytic domain-wild-type by antithrombin in the absence and presence of fondaparinux
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Zn2+
-
in the presence of zinc ions, kininogen is required for optimal FXI binding to GP1b on activated platelets in suspension, enhancing the binding stoichiometry by approximately 2fold
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2,4-dibromo-3-[[(4-carbamimidamidobutyl)carbamoyl]oxy]-6-hydroxyphenyl)acetic acid
-
-
(2,4-dibromo-6-[[(4-carbamimidamidobutyl)carbamoyl]oxy]-3-hydroxyphenyl)acetic acid
-
-
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
-
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
-
(2S)-2-([[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]amino)-N-[(2S)-1-[[(2S)-5-carbamimidamido-1-oxo-1-(1,3-thiazol-2-yl)pentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]-2-(4-hydroxyphenyl)ethanamide
-
-
(2S)-2-([[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]amino)-N-[(2S)-1-[[(2S)-5-carbamimidamido-1-oxo-1-(1,3-thiazol-2-yl)pentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]-2-(pyridin-3-yl)ethanamide
-
-
(3R)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
-
-
(3R)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
-
-
(3S)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
-
-
(3S)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
-
-
(4S,7S)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,12,13,14,15-dodecahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
-
-
(4S,7S,10S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-10-phenyl-4,5,7,8,10,11,14,15-octahydro-1H-[1,4,7]triazacyclohexadecino[10,9-b]indole-3,6,9(2H)-trione
-
-
(4S,7S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,14,15-decahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
-
-
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
-
-
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5,6,7,8-tetrahydroisoquinoline-6-carboxamide
-
-
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]isoquinoline-6-carboxamide
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2,6-difluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2-fluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chlorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-fluorobenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methoxybenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methylbenzyl)urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[2-(aminomethyl)-5-chlorobenzyl]urea
-
-
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(trifluoromethyl)benzyl]urea
-
-
2'-[(6-carbamimidoyl-1-ethyl-1H-indol-3-yl)methyl]-4-methyl-5'-[[(5-methylpyrazin-2-yl)methyl]carbamoyl]biphenyl-2-carboxylic acid
-
-
2,4-dibromo-3-([(4-carbamimidamidobutyl) carbamoyl]oxy)-6-hydroxyphenyl acetic acid
-
clavatadine A
2-(2-amino-2-oxoethyl)-3,5-dibromo-4-hydroxyphenyl (4-carbamimidamidobutyl)carbamate
-
clavatadine B
2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
-
2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
-
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-L-arginyl-L-valyl-L-arginyl)-1,3-thiazole
-
-
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N5-carbamoyl-L-ornithyl-L-valyl-L-arginyl)-1,3-thiazole
-
-
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
-
-
3'-[(2S,4R)-6-carbamimidoyl-4-methyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]-4-carbamoyl-5'-[(3-methylbutanoyl)amino]biphenyl-2-carboxylic acid
-
-
3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
-
3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1,2-benzoxazole-6-carboxamide
-
-
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1H-indazole-6-carboxamide
-
-
3-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
3-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(pyridin-3-yl)-L-alanyl]amino]benzoic acid
-
-
3-[[N2-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(pyrazin-2-ylmethyl)-L-asparaginyl]amino]benzoic acid
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N,N-dimethylbenzamide
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N-methylbenzamide
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-bromo-1H-imidazol-4-yl)-benzamide
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-chloro-1H-imidazol-4-yl)-benzamide
-
-
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-fluoro-1H-imidazol-4-yl)-benzamide
-
-
4-(2-(S-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzoic acid
-
-
4-[(N-[(2E)-3-[2-(aminomethyl)-5-chlorophenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
4-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]benzoic acid
-
-
4-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-tryptophyl)amino]benzoic acid
-
-
4-[(N2-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[2-(morpholin-4-yl)ethyl]-L-asparaginyl)amino]benzoic acid
-
-
4-[[(2S)-2-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-4-(methylsulfonyl)butanoyl]amino]benzoic acid
-
-
4-[[N-[(2E)-3-[3-chloro-2-fluoro-6-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(1-ethyl-5-methyl-1H-pyrazol-3-yl)-L-alanyl]amino]benzoic acid
-
-
4-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(thiophen-2-yl)-L-alanyl]amino]benzoic acid
-
-
5-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino]thiophene-2-carboxylic acid
-
-
5-[[3-(ethoxycarbonyl)-5-hydroxy-6-methoxy-1-benzofuran-2-yl]methoxy]-6-methoxy-2-methyl-1-benzofuran-3-carboxylic acid
-
-
amyloid beta-precursor protein Kunitz domain
-
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
-
diisopropylfluorphosphate
-
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
disodium 3-([[3,5-dicyano-6-nitro-4-(4-phenoxyphenyl)pyridin-2-yl]sulfanyl]acetyl)benzene-1,2-diyl disulfate
-
-
disodium 4-[[3-(1,3-dioxo-5-[[4-(sulfonatooxy)phenyl]carbamoyl]-1,3-dihydro-2H-isoindol-2-yl)benzoyl]amino]phenyl sulfate
-
-
ethyl 2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
-
ethyl 2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
-
ethyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-10-methyl-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecine-2-carboxylate
-
-
ethyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-15-[(methoxycarbonyl)amino]-2,3,4,5,6,7-hexahydro-1H-8,12-(metheno)-1,9-benzodiazacyclotetradecine-2-carboxylate
-
-
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]leucinate
-
-
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]phenylalaninate
-
-
ethyl [(4E)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-1,6,7,9-tetrahydro-11,8-(azeno)-2,9-benzodiazacyclotridecin-2(3H)-yl]acetate
-
-
fractionated heparin of 64 disaccharide units
-
70-80% saturable maximal inhibition at 37°C
-
methyl (4-[2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[2-[(benzyl[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)methyl]-5-chloro-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[5-chloro-2-[(1S)-1-([N-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
-
methyl (4-[[N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-(1-methyl-1H-pyrazol-3-yl)-L-alanyl]amino]phenyl)carbamate
-
-
methyl 2-[(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)amino][1,2,4]triazolo[1,5-a]pyridine-6-carboxylate
-
-
methyl 4-(2-((S)-1-(trans-4-(aminomethyl)-cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-benzoate
-
-
methyl 7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-14-[(methoxycarbonyl)amino]-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecine-2-carboxylate
-
-
methyl [(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 [(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 [1-(N-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-L-phenylalanyl)-1,2,3,4-tetrahydroquinolin-6-yl]carbamate
-
-
methyl [10-chloro-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-(trifluoromethyl)-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [2-(4-chloro-1-methyl-1H-pyrazol-3-yl)-7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-10-methyl-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-(3-methyloxetan-3-yl)-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14-yl]carbamate
-
-
methyl [7-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-3,3-difluoro-4-oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,5,9-benzotriazacyclotridecin-14-yl]carbamate
-
-
N-(3-amino-1H-indol-6-yl)-Nalpha-([[5-chloro-2-(1H-tetrazol-1-yl)phenyl]sulfinyl]acetyl)-L-phenylalaninamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1-(3-aminopropyl)cyclohexanecarboxamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2,6-difluoro-4-methoxybenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methoxybenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methylbenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)-2-fluorobenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)benzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylbenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5-chloro-2-fluorobenzamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-pyrazol-1-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(4H-1,2,4-triazol-4-yl)phenyl]glycinamide
-
-
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]benzene-1,4-dicarboxamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2,2-dimethylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(2,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(4-chlorobenzyl)carbamoyl]-L-leucinamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorophenyl)sulfonyl]amino]methyl)-L-phenylalaninamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(4-fluorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylacetyl)amino]methyl]-L-phenylalaninamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylcarbonyl)amino]methyl]-L-phenylalaninamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(phenylcarbamoyl)amino]methyl]-L-phenylalaninamide
-
-
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]propyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
-
N-[(1S)-2-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]amino]-1-cyclohexyl-2-oxoethyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
-
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-carboxamide
-
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-3-oxo-3,4-dihydro-2H-1,4-benzothiazine-7-carboxamide
-
-
N-[(2S)-1-([2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]amino)-1-oxo-3-phenylpropan-2-yl]-4-hydroxy-2-oxo-1,2,3,4-tetrahydroquinoline-6-carboxamide
-
-
N-[(3,4-dichlorobenzyl)carbamoyl]-L-leucyl-N-[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]-L-phenylalaninamide
-
-
N-[2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]-Na-(imidazo[1,2-a]pyrimidin-2-ylcarbonyl)-L-phenylalaninamide
-
-
N-[2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]ethyl]-Nalpha-(1H-indazol-3-ylcarbonyl)-L-phenylalaninamide
-
-
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-(pent-4-enoylamino)acetyl]-L-leucinamide
-
-
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-[[(2S)-2-phenylpent-4-enoyl]amino]acetyl]-L-leucinamide
-
-
N2-(benzylcarbamoyl)-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
-
N2-acetyl-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
-
N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N1-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-aspartamide
-
-
N2-[[1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
-
-
Na-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-3-fluoro-N-[4-(1H-tetrazol-5-yl)phenyl]-L-phenylalaninamide
-
-
Na-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[4-(1H-tetrazol-5-yl)phenyl]-L-phenylalaninamide
-
-
Na-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N2-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tyrosinamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(1,2,3,4-tetrahydroisoquinolin-6-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(1-oxo-2,3-dihydro-1H-isoindol-5-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(2-oxoazepan-3-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-(6-fluoro-1,3-benzothiazol-2-yl)-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]-N-[4-[(methoxycarbonyl)amino]cyclohexyl]-L-phenylalaninamide
-
-
Nalpha-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tryptophanamide
-
-
protease nexin-2
-
highly specific and potent inhibitor of FXIa, is about 775fold more potent than basic pancreatic trypsin inhibitor in FXIa inhibition, provides single-step slow equilibration inhibition
-
sodium 2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-3-(methoxycarbonyl)-1-benzofuran-5-yl sulfate
-
-
sodium 2-[[(3-carboxy-6-methoxy-2-methyl-1-benzofuran-5-yl)oxy]methyl]-3-(ethoxycarbonyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-(propan-2-yloxy)-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-6-methoxy-1-benzofuran-5-yl sulfate
-
-
sodium 3-(ethoxycarbonyl)-6-methoxy-2-[([6-methoxy-2-methyl-3-[(prop-2-en-1-yloxy)carbonyl]-1-benzofuran-5-yl]oxy)methyl]-1-benzofuran-5-yl sulfate
-
-
sodium 6-ethoxy-3-(ethoxycarbonyl)-2-([[3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl]oxy]methyl)-1-benzofuran-5-yl sulfate
-
; most potent inhibitor
sodium 6-methoxy-3-(methoxycarbonyl)-2-([[6-methoxy-3-(methoxycarbonyl)-2-methyl-1-benzofuran-5-yl]oxy]methyl)-1-benzofuran-5-yl sulfate
-
-
trans-4-(aminomethyl)-N-((S)-1-(4-(3-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-1-(4-(4-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-1-(5-oxo-1-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-2-phenylethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(2-phenyl-1H-imidazol-4-yl)ethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-1,2,4-triazol-5-yl)ethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-pyrazol-5-yl)ethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-(4-sulfamoylphenyl)-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(5-phenyloxazol-2-yl)ethyl)cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-methyl-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-2-phenylpyridin-4-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(1-oxido-5-phenylpyridin-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(5-chloro-4-phenyl-1H-imidazol-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(5-fluoro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-amino-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-chloro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-hydroxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(6-methoxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-(biphenyl-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[1-[6-(methylamino)-4-phenylpyridin-2-yl]-2-phenylethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(2-phenylpyridin-4-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyrimidin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(5-phenylpyridin-3-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
-
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyrimidin-4-yl)ethyl]cyclohexanecarboxamide
-
-
trans-N-((S)-1-(4-(3-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
reversible enzyme inhibition
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-fluoro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-((S)-1-(4-(4-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylcyclohexanecarboxamide
-
-
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]cyclohexane-1,4-dicarboxamide
-
-
trans-N-[1-[3-(3-amino-1H-indazol-6-yl)phenyl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)-6-oxo-1,6-dihydropyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)pyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
trans-N-[1-[5-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
-
[4-[(N-[3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]propanoyl]-L-phenylalanyl)amino]phenyl]acetic acid
-
-
4-aminobenzamidine
-
a reversible serine protease inhibitor, competitive versus substrate S-2366, noncompetitive versus substrate factor IX, inhibition of wild-type enzyme and recombinant peptide FXI/E361-V607
4-aminobenzamidine
-
beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview
protease nexin 2
-
the major interactions required for factor XIa inhibition are localized to the catalytic domain of factor XIa and the Kunitz domain of protease nexin II
-
protease nexin 2
-
activated platelet surface has littlke or no direct effect on the rate of factor IX activation by factor Xia and the reaction proceeds at uninhibited rates when protease nexin 2 is present. Factor Xia-catalyzed FIX activation is completely inhibited by protease nexin 2 in solution or in the presence of umbilical vein endothelial cells
-
additional information
-
the recombinant catalytic domain Ile370-Val607 of FXIa inhibits the binding of factor XIa to the platelets with a Ki of 3.5 nM, whereas the recombinant factor XI heavy chain does not
-
additional information
-
inhibitor design and synthesis, overview, inhibitor in vitro anticoagulant activity in human plasma
-
additional information
-
heparin accelerates inhibition of factor XIa. Heparin enhances antithrombin inhibition of catalytic domain-wild-type 212fold, but only 37-94fold for catalytic domain mutants
-
additional information
-
Arg184 may be part of a switch that holds FXI in an inactive conformation in the zymogen
-
additional information
-
potent activated factor VII inhibition with insect-derived serine protease inhibitor, but this protein is only 10fold selective over activated factor X. Inhibition by FXI neutralizing antibodies, which allow preexisting activated factor XI to remain active
-
additional information
-
a monoclonal antibody against FXI or activated factor XI reduces thrombus formation in balloon-injured iliac arteries
-
additional information
-
ketoarginine-based peptidomimetics are irreversible inhibitors of actived factor XI and form a covalent bond to the catalytic serine of the enzyme. Intravenous infusion is efficacious in a rat model of venous thrombosis. A pyridyl analog in a rat mesenteric bleeding model at a 4fold efficacious dose does not alter bleeding time
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activated factor IX
-
autoactivation, cleavage of FXI at the Arg369-Ile370 bond. activated factor IX is part of a feedback loop that sustains thrombin generation through FIX activation to consolidate coagulation
-
activated factor XII
-
FXI activation proceeds through an intermediate with only one activated submit
-
activated factor XII
-
activated factor XII-mediated activation of FXI appears to play a central role in formation of pathologic thrombi in murine thrombosis models
-
desmopressin
-
increase of both FXI activity (up to 31%) and antigen levels 60 min after infusion. Also contradictory results with a lack of rise of FXI levels after infusion
Factor XII
-
FXI is activated by factor XII during ischemia reperfusion injury and within the growing thrombus according to the classical intrinsic pathway cascade
-
thrombin
-
FXI activation proceeds through an intermediate with only one activated submit
-
thrombin
-
thrombin generated early in coagulation by the tissue factor pathway activates FXI creating a positive feedback loop that sustains coagulation following inactivation of the factor VIIa/tissue factor complex by tissue factor pathway inhibitor
-
thrombin
-
activated factor V is a cofactor for the activation of factor XI by thrombin. Depletion of factor V, or the addition of activated protein C, decreases the activation of the intrinsic pathway by thrombin in plasma. Factor XI binds to factor V with multiple binding sites. Addition of FVIIIa, kininogen, or protein S does not influence the formation of activated factor XI
-
thrombin
-
activates FXI. FXI activation by thrombin is enhanced by charged substances, such as dextran sulfate or heparin. Thrombin binds to the A1 domain of FXI, with residues Glu66, Lys83, and Gln84 forming part of the binding site. The dimer is required for optimal FXI activation by thrombin
-
additional information
-
activation of factor XI by thrombin and autoactivation to factor XIa
-
additional information
-
platelets may play a role in FXI activation. FXI binding to platelets is not enhanced by kininogen
-
additional information
-
FXI monomers are activated poorly, dimeric form is needed for activation. As FXI lacks a Gla domain, the dimeric structure may represent an alternative solution to the problem of tethering a prothrombotic molecule to a cellular surface in flowing blood in the vicinity of a wound
-
additional information
-
in blood challenged with low concentrations of tissue factor, factor XI can be activated independently of factor XII
-
additional information
-
antibody 14E11 exerts an inhibitory effect on fXI activation, but not fXIa activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
factor IX
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.205
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.268
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.292
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.315
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.336
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.339
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.383
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.4
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.525
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.538
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.603
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.828
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.852
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.552
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K170A/R171A/R173A mutant
0.655
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K170A mutant
0.757
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-wild type
0.764
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K179A mutant
0.81
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-R173A mutant
0.812
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-R171A mutant
0.829
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K175A mutant
0.26
pyroGlu-Pro-Arg-4-nitroanilide
-
recombinant wild-type enzyme, pH 7.5, 37°C
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of isolated subunits with each one active site, stoichiometry of FIX and FIXalphabeta binding to FXIa, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
factor IX
-
in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; kcat less than 0.2 s-1, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; kcat less than 0.2 s-1, mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; kcat less than 0.2 s-1, mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; kcat less than 0.2 s-1, mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; kcat less than 0.2 s-1, mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.73
factor IX
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
5.8
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
7
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
8
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
14
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
21
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
29
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
30
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
42
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
58
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
86
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
95
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
201
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
98
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K170A mutant
115
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K170A/R171A/R173A mutant; fXIa-catalytic domain-R171A mutant
116
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K179A mutant
117
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-K175A mutant; fXIa-catalytic domain-R173A mutant
119
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-catalytic domain-wild type
148
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide
-
fXIa-R37Q mutant; fXIa-wild type
0.268
pyroGlu-Pro-Arg-4-nitroanilide
-
pH 7.4, 37°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000005
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
at 25°C, pH not specified in the publication
0.0000012
(2E)-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enamide
-
at 25°C, pH not specified in the publication
0.00000215
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5,6,7,8-tetrahydroisoquinoline-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000019
1-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]isoquinoline-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000023
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2,6-difluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000057
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chloro-2-fluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000054
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(3-chlorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000031
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-fluorobenzyl)urea
-
at 25°C, pH not specified in the publication
0.000075
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methoxybenzyl)urea
-
at 25°C, pH not specified in the publication
0.000053
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-(5-chloro-2-methylbenzyl)urea
-
at 25°C, pH not specified in the publication
0.0000058
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[2-(aminomethyl)-5-chlorobenzyl]urea
-
at 25°C, pH not specified in the publication
0.00024
1-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-3-[5-chloro-2-(trifluoromethyl)benzyl]urea
-
at 25°C, pH not specified in the publication
0.000275
2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
at pH 7.4 and 37°C
0.00015
2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)acetic acid
-
at pH 7.4 and 37°C
0.0000002
3'-[(2S,4R)-6-carbamimidoyl-4-methyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]-4-carbamoyl-5'-[(3-methylbutanoyl)amino]biphenyl-2-carboxylic acid
-
at pH 7.4 and 37°C
0.0011
3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
at pH 7.4 and 37°C
0.000125
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1,2-benzoxazole-6-carboxamide
-
at 25°C, pH not specified in the publication
0.000058
3-amino-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1H-indazole-6-carboxamide
-
at 25°C, pH not specified in the publication
0.00286
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N,N-dimethylbenzamide
-
at pH 7.4 and 37°C
0.00035
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)-N-methylbenzamide
-
at pH 7.4 and 37°C
0.00003
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzamide
-
at pH 7.4 and 37°C
0.000009
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-bromo-1H-imidazol-4-yl)-benzamide
-
at pH 7.4 and 37°C
0.000004
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-chloro-1H-imidazol-4-yl)-benzamide
-
at pH 7.4 and 37°C
0.00003
4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-5-fluoro-1H-imidazol-4-yl)-benzamide
-
at pH 7.4 and 37°C
0.00059
4-(2-(S-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)benzoic acid
-
at pH 7.4 and 37°C
0.000627
basic pancreatic trypsin inhibitor
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.0000041
basic pancreatic trypsin inhibitor mutant K15R
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00063
ethyl 2-(3-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
at pH 7.4 and 37°C
0.000495
ethyl 2-(4-(2-((S)-1-(trans-4-(aminomethyl)cyclohexanecarboxamido)-2-phenylethyl)-1H-imidazol-4-yl)phenyl)-acetate
-
at pH 7.4 and 37°C
0.0000067
methyl (4-[2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000027
methyl (4-[5-chloro-2-[(1S)-1-([(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl]amino)-2-phenylethyl]-1H-imidazol-4-yl]phenyl)carbamate
-
at 25°C, pH not specified in the publication
0.0000019
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
0.00000149
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-1-(3-aminopropyl)cyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
0.000065
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2,6-difluoro-4-methoxybenzamide
-
at 25°C, pH not specified in the publication
0.00028
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methoxybenzamide
-
at 25°C, pH not specified in the publication
0.0002
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-2-fluoro-4-methylbenzamide
-
at 25°C, pH not specified in the publication
0.00000103
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)-2-fluorobenzamide
-
at 25°C, pH not specified in the publication
0.00000116
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)benzamide
-
at 25°C, pH not specified in the publication
0.00039
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylbenzamide
-
at 25°C, pH not specified in the publication
0.00053
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-5-chloro-2-fluorobenzamide
-
at 25°C, pH not specified in the publication
0.00045
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-pyrazol-1-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.0000015
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.000046
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-N2-[5-chloro-2-(4H-1,2,4-triazol-4-yl)phenyl]glycinamide
-
at 25°C, pH not specified in the publication
0.00031
N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]benzene-1,4-dicarboxamide
-
at 25°C, pH not specified in the publication
0.00000081
protease nexin-2
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000492
protease nexin-2 mutant F34A
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000081
protease nexin-2 mutant M17A
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000296
protease nexin-2 mutant P13A
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.0000113
protease nexin-2 mutant R15K
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000283
protease nexin-2 mutant R20A
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00000093
protease nexin-2 mutant S19A
-
in 50 mM Tris, 150 mM NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, pH 7.5, at 37°C
-
0.00112
trans-4-(aminomethyl)-N-((S)-1-(4-(3-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00023
trans-4-(aminomethyl)-N-((S)-1-(4-(4-cyanophenyl)-1H-imidazol-2-yl)-2-phenylethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.003074
trans-4-(aminomethyl)-N-((S)-1-(5-oxo-1-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-2-phenylethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00164
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(2-phenyl-1H-imidazol-4-yl)ethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00098
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-1,2,4-triazol-5-yl)ethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00694
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(3-phenyl-1H-pyrazol-5-yl)ethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00134
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-(4-sulfamoylphenyl)-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00012
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00144
trans-4-(aminomethyl)-N-((S)-2-phenyl-1-(5-phenyloxazol-2-yl)ethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.000479
trans-4-(aminomethyl)-N-[1-(1-methyl-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00253
trans-4-(aminomethyl)-N-[1-(1-oxido-2-phenylpyridin-4-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00169
trans-4-(aminomethyl)-N-[1-(1-oxido-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.001063
trans-4-(aminomethyl)-N-[1-(1-oxido-5-phenylpyridin-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000012
trans-4-(aminomethyl)-N-[1-(5-chloro-4-phenyl-1H-imidazol-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00032
trans-4-(aminomethyl)-N-[1-(5-fluoro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000227
trans-4-(aminomethyl)-N-[1-(6-amino-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000206
trans-4-(aminomethyl)-N-[1-(6-chloro-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000113
trans-4-(aminomethyl)-N-[1-(6-hydroxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000949
trans-4-(aminomethyl)-N-[1-(6-methoxy-4-phenylpyridin-2-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000936
trans-4-(aminomethyl)-N-[1-(biphenyl-3-yl)-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00086
trans-4-(aminomethyl)-N-[1-[6-(methylamino)-4-phenylpyridin-2-yl]-2-phenylethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000433
trans-4-(aminomethyl)-N-[2-phenyl-1-(2-phenylpyridin-4-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00012
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000377
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.01142
trans-4-(aminomethyl)-N-[2-phenyl-1-(4-phenylpyrimidin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.00033
trans-4-(aminomethyl)-N-[2-phenyl-1-(5-phenylpyridin-3-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.03021
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyridin-2-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000331
trans-4-(aminomethyl)-N-[2-phenyl-1-(6-phenylpyrimidin-4-yl)ethyl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000545
trans-N-((S)-1-(4-(3-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.0000003
trans-N-((S)-1-(4-(3-amino-1H-indazol-6-yl)-5-fluoro-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.0004
trans-N-((S)-1-(4-(4-(2-amino-2-oxoethyl)phenyl)-1H-imidazol-2-yl)-2-phenylethyl)-4-(aminomethyl)cyclohexanecarboxamide
-
at pH 7.4 and 37°C
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
0.000068
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-methylcyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
0.0029
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]cyclohexane-1,4-dicarboxamide
-
at 25°C, pH not specified in the publication
0.000021
trans-N-[1-[3-(3-amino-1H-indazol-6-yl)phenyl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000037
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)-6-oxo-1,6-dihydropyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.000013
trans-N-[1-[4-(3-amino-1H-indazol-6-yl)pyridin-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000032
trans-N-[1-[5-(3-amino-1H-indazol-6-yl)-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
0.0000211
4-aminobenzamidine
-
mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000245
4-aminobenzamidine
-
mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000362
4-aminobenzamidine
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000396
4-aminobenzamidine
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000416
4-aminobenzamidine
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000419
4-aminobenzamidine
-
mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000497
4-aminobenzamidine
-
mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000513
4-aminobenzamidine
-
wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000714
4-aminobenzamidine
-
mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0000739
4-aminobenzamidine
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.000079
4-aminobenzamidine
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.0001529
4-aminobenzamidine
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
0.06
4-aminobenzamidine
-
37°C, recombinant wild-type enzyme, versus substrate S-2366
0.085
4-aminobenzamidine
-
37°C, recombinant peptide FXI/E361-V607, versus substrate S-2366
0.086
4-aminobenzamidine
-
37°C, recombinant peptide FXI/E361-V607, versus substrate factor IX
0.095
4-aminobenzamidine
-
37°C, recombinant wild-type enzyme, versus substrate factor IX
0.52
Aprotinin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, free FXIa
1.43
leupeptin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, free FXIa
209
leupeptin
-
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, FXIa-FIX complex
0.000001
protease nexin 2
-
mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000011
protease nexin 2
-
mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000013
protease nexin 2
-
mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000014
protease nexin 2
-
mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000015
protease nexin 2
-
mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C; wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.0000047
protease nexin 2
-
mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C
-
0.42
S-2366
-
37°C, recombinant peptide FXI/E361-V607, versus substrate factor IX
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
at 25°C, pH not specified in the publication
0.00000031
trans-N-[(1S)-1-[4-(3-amino-1H-indazol-6-yl)-5-chloro-1H-imidazol-2-yl]-2-phenylethyl]-4-(aminomethyl)cyclohexanecarboxamide
-
pH and temperature not specified in the publication
additional information
additional information
-
second-order inhibition rate constants, wild-type and mutant enzymes with different inhibitors, overview
-
additional information
additional information
-
competition for platelet binding by the wild-type enzyme and mutants, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000132
(3R)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
Homo sapiens
-
pH 7.4, 37°C
0.000533
(3R)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
Homo sapiens
-
pH 7.4, 37°C
0.00001
(3S)-3-(4-bromophenyl)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-1-cyclohexyl-2-oxoethyl]butanamide
Homo sapiens
-
pH 7.4, 37°C
0.000028
(3S)-N-[(1S)-2-[[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]amino]-2-oxo-1-(pyridin-3-ylmethyl)ethyl]-3-(4-fluorophenyl)butanamide
Homo sapiens
-
pH 7.4, 37°C
0.1759
(4S,7S)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,12,13,14,15-dodecahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.1358
(4S,7S,10S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-10-phenyl-4,5,7,8,10,11,14,15-octahydro-1H-[1,4,7]triazacyclohexadecino[10,9-b]indole-3,6,9(2H)-trione
Homo sapiens
-
pH and temperature not specified in the publication
0.7678
(4S,7S,12Z)-18-chloro-7-cyclohexyl-4-(2-methylpropyl)-1,2,4,5,7,8,10,11,14,15-decahydro[1,2,5,8]thiatriazacyclohexadecino[11,10-b]indole-3,6-dione 9,9-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000076 - 0.0002
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
0.0073
1-[2-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl]guanidine
Homo sapiens
-
-
0.000007
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-L-arginyl-L-valyl-L-arginyl)-1,3-thiazole
Homo sapiens
-
pH 7.4, 37°C
0.00003
2-(N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N5-carbamoyl-L-ornithyl-L-valyl-L-arginyl)-1,3-thiazole
Homo sapiens
-
pH 7.4, 37°C
0.0014
2-carbamimidamido-1-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]ethyl pyridine-3-carboxylate
Homo sapiens
-
-
0.000403
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]leucinate
Homo sapiens
-
pH 7.4, 37°C
0.000258
ethyl N-[[(3S,6S,9S)-14-amino-3-benzyl-14-imino-6-(1-methylethyl)-4,7-dioxo-9-(1,3-thiazol-2-ylcarbonyl)-2,5,8,13-tetraazatetradec-1-yl]carbamoyl]phenylalaninate
Homo sapiens
-
pH 7.4, 37°C
0.0092
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2,2-dimethylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.000045
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(2,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.000063
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.000114
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-N2-[(4-chlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.000093
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
-
pH 7.4, 37°C
0.0026
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(3,4-dichlorophenyl)sulfonyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
-
pH 7.4, 37°C
0.00016
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-([[(4-fluorobenzyl)carbamoyl]amino]methyl)-L-phenylalaninamide
Homo sapiens
-
pH 7.4, 37°C
0.0023
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylacetyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
-
pH 7.4, 37°C
0.0022
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(furan-2-ylcarbonyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
-
pH 7.4, 37°C
0.00192
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-Nalpha-[[(phenylcarbamoyl)amino]methyl]-L-phenylalaninamide
Homo sapiens
-
pH 7.4, 37°C
0.00092
N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]propyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.00034
N-[(1S)-2-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]amino]-1-cyclohexyl-2-oxoethyl]-N2-[(3,4-dichlorobenzyl)carbamoyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.00071
N-[(3,4-dichlorobenzyl)carbamoyl]-L-leucyl-N-[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]-L-phenylalaninamide
Homo sapiens
-
pH 7.4, 37°C
0.1031
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-(pent-4-enoylamino)acetyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1459
N-[[5-chloro-2-(prop-2-en-1-yl)-1H-indol-3-yl]methyl]-N2-[(2R)-2-cyclohexyl-2-[[(2S)-2-phenylpent-4-enoyl]amino]acetyl]-L-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
N2-(benzylcarbamoyl)-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.027
N2-acetyl-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.000356
N2-[(benzyloxy)carbonyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.000008
N2-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N1-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-aspartamide
Homo sapiens
-
pH 7.4, 37°C
0.00001
N2-[[1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-leucinamide
Homo sapiens
-
pH 7.4, 37°C
0.000006
Na-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N2-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tyrosinamide
Homo sapiens
-
pH 7.4, 37°C
0.000029
Nalpha-[[(1R)-1-(4-bromophenyl)ethyl]carbamoyl]-N-[(1S)-1-[[(1S)-4-carbamimidamido-1-(1,3-thiazol-2-ylcarbonyl)butyl]carbamoyl]-2-methylpropyl]-L-tryptophanamide
Homo sapiens
-
pH 7.4, 37°C
0.000076
(S)-2-(3-(3,4-dichlorobenzyl)ureido)-N-((2S,3S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxopentan-2-yl)-4-methylpentanamide
Homo sapiens
-
pH 7.4, 37°C
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
Homo sapiens
-
pH 7.4, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type andmutant substrate, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
additional information
-
the enzyme binds to platelets, a conformational transition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain zymogen factor XI platelet binding site and exposes the factor XIa platelet binding site within the catalytic domain possibly comprising residues Cys527-Cys542, overview
additional information
-
hemophilia C (deficiency in FXI) is present in both sexes
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
160000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
-
macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa are required for mediation of formation of the Michaelis complex required for factor IX-activation, overview
dimer
-
two forms of activated factor XI are generated during coagulation, and each half of a factor XIa dimer behaves as an independent enzyme with respect to factor IX
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the enzyme bears five N-glycosylation consensus sites per monomer
proteolytic modification
proteolytic modification
-
the enzyme shows activation by autolysis involving residues of the autolysis loops, overview
proteolytic modification
-
factor XI is activated to factor XIIa at 37°C, a conformational transition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain zymogen factor XI platelet binding site and exposes the factor XIa platelet binding site within the catalytic domain possibly comprising residues Cys527-Cys542
proteolytic modification
-
FXI activation proceeds through an intermediate with one activated subunit, limited digestion by incubating with FXIIa or thrombin
proteolytic modification
-
factor XI is activated to factor XIa by site-specific cleavage of zymogen factor XI by thrombin, factor XIIa, or autoactivation
proteolytic modification
-
the zymogen FXI is activated by proteolytic cleavage to FXIa
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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
-
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
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
antibody-affinity chromatography by using the calcium-dependent anti-human fIX monoclonal IgG SB 249417
-
native enzyme from plasma and recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity chromatography with elution by benzamidine
-
recombinant mutant enzyme C362S/C482S from HEK-293 cells by immunoaffinity chromatography
-
recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity chromatography
-
recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity, cation exchange, and heparin affinity chromatography
-
SP-Sepharose column chromatography, Heparin HiTrap column chromatography and Superdex 75 column chromatography
-
Zn2+-chelating Sepharose column chromatography and SP Sepharose column chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of mutant enzyme C362S/C482S in HEK-293 cells and secretion of recombinant protein to the medium
-
expression of the catalytic domain rhFXI370-60 of mutant S434A/T475A/C482S/K437A
-
expression of the peptide comprising 237 amino acids at the C-terminal end of FXI, peptide FXI/E361-V607, in Pichia pastoris strain X33
-
expression of wild-type and mutant enzymes in HEK-293 cells and secretion of recombinant protein to the medium
-
genetic location on chromosome 4q35, stable expression of wild-type and mutant enzymes in BHK-570 cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
antisense oligonucleotide produces near-complete inhibition of hepatic FXI mRNA
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C362S/C482S
C398Y
-
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
E98A
-
the mutant has normal Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
E98D
-
the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
E98V
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
G104R
-
this mutation in the PK A2 domain associated with CRM+ PK deficiency causes decreased kininogen binding
G193A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193D
-
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 1.6-36fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193E
-
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193K
-
site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 35-478fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G193V
-
site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites
G400V
-
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
I151A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
K145A
-
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K148A
-
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K149A
-
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
K170A
-
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K170A/R171A/R173A
-
catalytic domain with residues 170, 171, and 173 changed to alanine is designated CD-KRR/A
K175A
-
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K179A
-
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
K192A
-
the mutant has normal Km value for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
K192E
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
K192Q
-
the mutant has increased Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis
K192R
-
the mutant has decreased Km and kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
M102T
-
site-directed mutagenesis,missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
M18I
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
R144A
-
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R144A/K145A/R147A/K148A/K149A
-
site-directed mutagenesis of an autolysis loop residues, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R144A/K145A/R147A/R149A
-
contains Ala substitutions for Arg-144, Lys-145, Arg-147, and Arg-149 (residues 504, 505, 507, and 509, respectively, in fXI numbering)
R147A
-
site-directed mutagenesis of an autolysis loop residue, the mutant shows altered sensitivity to inhibition by serpins compared to the wild-type enzyme
R171A
-
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
R173A
-
replaced the basic residues of the fXIa 170 loop (Lys-170, Arg-171, Arg-173, Lys-175, and Lys-179, chymotrypsin numbering) with Ala, using an expression system that allows separation of the fXIa catalytic domain from noncatalytic domains
R3704A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
R378C
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
S225F
-
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
S248N
-
binds platelets with 5fold reduced affinity compared with wild-type, the A3 domain is probably not affected significantly, as FXI-Asn248 is secreted, activated by activated factor XII, and activates FIX similar to wild-type activated factor IX. Is associated with bleeding and defective FXI binding to platelets but does not affect the activated partial thromboplastin time assay, which does not contain platelets
S434A/K437A/T475A/C482S
-
to improve crystallizability a quadrupole mutant is generated
S434A/T475A/C482S/K437A
-
site-directed mutagenesis, crystal structure determination with bound benzylamidine
T575M
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is normally secreted from the transfected cell, but shows negligible factor IX activation activity
W569S
-
exhibits a dominant negative effect when coexpressed with wild-type FXI and is associated with FXI deficiency that may be inherited in a dominant manner
Y133S
-
site-directed mutagenesis, missense mutation identified from large scale screening, the mutant enzyme is not secreted from the transfected cell resulting in a cross-reactive material negative phenotype
Y143A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with normal value of Ki
Y5901A
-
the mutant has normal Km and impaired kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis, and is inhibited by protease nexin 2 with increased value of Ki
Y5901V
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the mutant has normal Km and decreased kcat values for L-pyroGlu-L-Pro-L-Arg-4-nitroanilide hydrolysis, the mutant has deficient kcat values for factor IX hydrolysis and is not inhibited by protease nexin 2
additional information
C362S/C482S
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site-directed mutagenesis, the mutant shows increased platelet binding compared to the wild-type enzyme
additional information
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FXIa/PKA4 is made by replacing the FXI A4 domain with the A4 domain from prekallikrein. A dimeric version of FXI/PKA4 (FXI/PKA4-Gly326) is prepared as a control. Activated FXIa/PKA4 and FXIa/PKA4-Gly326 activate factor IX with kinetic parameters similar to that of FXIa. FXI/PKA4 and FXIa/PKA4-Gly326 have coagulant activity similar to FXI. FXIa/PKA4, FXIa/PKA4-Gly326 and FXIa have similar affinities for activated platelets. The dimeric proteins FXI and FXI/PKA4-Gly326 promote coagulation similarly, however, monomeric FXIa/PKA4 has greatly reduced activity. The activated monomeric FXIa/PKA4 activates factor IX poorly in the presence of activated platelets
additional information
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chimeric recombinant enzyme mutants rFXI-PKA3 and rFXIa-PKA3, with fusion of FXI to the Apple 3 domain of prekallikrein, show unaffected platelet binding compared to the wild-type enzyme, overview
additional information
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construction of FXI with a single catalytic active site, construction of recombinant FXI with the A4 domain replaced by the A4 domain from plasma prekallikrein, i.e. FXI/PKA4, overview
additional information
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mutations in the fXIa 170 helix are introduced into a modified human fXI cDNA (fXI-Ser-362,482), which contains serine substitutions for Cys-362 and Cys-482
additional information
two different mutations, c.1546 G>A (Val498Met) and c.1560dupG (Tyr503ValfsX32) in the F11 gene
additional information
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factor XI deficiency caused by compound heterozygous F11 gene mutation
additional information
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FXI with substitutions for Cys321 still form stable dimers. The Cys321-Cys321 interchain bond forms poorly in FXI with a single alanine substitution of Leu284, Ile290, or Tyr329
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
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activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
drug development
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activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
drug development
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activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
drug development
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activated factor XI inhibition as a viable method to increase the ratio of benefit to risk in an antithrombotic drug
medicine
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the enzyme may be a suitable target for the development of an antithrombotic therapy
medicine
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diagnosis of FXI deficiency may be considered in patients with delayed postoperative bleeding and prolonged activated partial thromboplastin time, especially in a demographically high-risk population, such as Ashkenazi Jews. Women with severe FXI deficiency and prolonged activated partial thromboplastin time can be managed with fresh frozen plasma transfusion before neuraxial anesthesia
medicine
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treatment options for FXI-deficient patients include virus-inactivated fresh frozen plasma, plasma-derived FXI concentrates, and activated recombinant FVII. Potential role of desmopressin for either treatment of bleeding episodes or the prevention of postoperative bleeding in patients with milder FXI defects. A single desmopressin infusion is sufficient to provide an efficient perioperative hemostasis
medicine
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therapeutically targeting FXI may offer a strategy for preventing or treating arterial thrombosis that is not associated with the high rate of hemorrhage that accompanies many currently used anticoagulants. Pharmacological FXI inhibitors may be beneficial in septic disease
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