3.4.21.27: coagulation factor XIa
This is an abbreviated version!
For detailed information about coagulation factor XIa, go to the full flat file.
Word Map on EC 3.4.21.27
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3.4.21.27
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bleeding
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thrombin
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clot
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platelet
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thrombosis
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anticoagulant
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prothrombin
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kallikrein
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kininogen
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prekallikrein
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viii
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hemostasis
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venous
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fibrinogen
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antithrombin
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zymogen
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fibrinolysis
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procoagulant
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fibrin
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willebrand
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antithrombotic
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hemophilia
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thromboembolism
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plasmin
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ashkenazi
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fxiia
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hageman
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coagulopathy
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amidolytic
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diathesis
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haemostat
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thrombophilias
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leiden
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jewish
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antifibrinolytic
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kaolin
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proline-specific
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thrombin-activatable
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meningosepticum
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fletcher
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c1-inhibitor
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thromboelastometry
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drug development
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tenase
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medicine
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basque
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menorrhagia
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desmopressin
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tranexamic
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proline-containing
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tafi
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recalcified
- 3.4.21.27
- bleeding
- thrombin
- clot
- platelet
- thrombosis
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anticoagulant
- prothrombin
- kallikrein
- kininogen
- prekallikrein
- viii
-
hemostasis
- venous
- fibrinogen
- antithrombin
- zymogen
-
fibrinolysis
-
procoagulant
- fibrin
- willebrand
-
antithrombotic
- hemophilia
- thromboembolism
- plasmin
-
ashkenazi
- fxiia
-
hageman
- coagulopathy
-
amidolytic
- diathesis
-
haemostat
- thrombophilias
- leiden
-
jewish
-
antifibrinolytic
- kaolin
-
proline-specific
-
thrombin-activatable
- meningosepticum
-
fletcher
- c1-inhibitor
-
thromboelastometry
- drug development
-
tenase
- medicine
-
basque
- menorrhagia
- desmopressin
-
tranexamic
-
proline-containing
- tafi
-
recalcified
Reaction
Selective cleavage of Arg-/-Ala and Arg-/-Val bonds in factor IX to form factor IXa =
Synonyms
activated blood-coagulation factor XI, activated coagulation factor XIa, activated factor XI, activated factor XIa, activated FXI, activated plasma thromboplastin antecedent, blood coagulation factor XIa, blood-coagulation factor XI, activated, blood-coagulation factor XIa, coagulation factor XI, coagulation factor XIa, factor XI, factor XIa, factor XIa catalytic domain, FXI, FXIa, fXIaCD, More, plasma thromboplastin antecedent, prolyl endopeptidase, protease factor XIa, PTA, recombinant human FXI370-607, rhFXI370-607
ECTree
3.4.21.27 coagulation factor XIaAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.27 - coagulation factor XIa
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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
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
-
-
-
-
?
beta-2-glycoprotein I + H2O
clipped beta-2-glycoprotein I
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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 + ?
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fXIa cleaves COOH-terminal to R306, possibly at the fXa/plasmin cleavage site R348
-
-
?
factor VIII + H2O
activated factor VIII + ?
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fXIa initially cleaves at R740 and R372 in the heavy chain and also makes several A3 cleavages most notably at R1652 and R1721
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-
?
Fibrinogen + H2O
?
-
Aalpha-chain and Bbeta-chain, gamma-chain after prolonged incubation
-
-
?
Gly-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Glu-L-Glu-L-Pro-L-Arg-4-nitroanilide + H2O
L-Glu-L-Glu-L-Pro-L-Arg + 4-nitroaniline
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S-2366
-
-
?
L-pyro-Glu-Pro-Arg-4-nitroanilide + H2O
L-pyro-Glu-Pro-Arg + 4-nitroaniline
i.e. S-2366
-
-
?
L-pyroGlu-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroGlu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-Pro-L-Arg-4-nitroanilide + H2O
L-pyroglutamyl-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
L-pyroglutamyl-L-prolyl-L-argininyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-7-amido-4-methylcoumarin + H2O
L-pyroglutamyl-L-prolyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide + H2O
L-pyroglutamyl-L-prolyl-L-arginine + p-nitroaniline
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
?
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substrate S-299
-
-
?
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine-p-nitroanilide + H2O
methyl-sulfonyl-D-cyclo-hexyl-glycyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-arginine-p-nitroanilide + H2O
N-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-Cbz-D-arginylglycyl-L-arginyl-4-nitroanilide + H2O
N-Cbz-D-arginylglycyl-L-arginine + 4-nitroaniline
-
-
-
-
?
platelet glycoprotein 1balpha + H2O
?
binding to the A3 domain of FXI
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-
?
prochemerin chem163S + H2O
chemerin chem162R + chermerin chem158K
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prochemerin is activated by a series of C-terminal proteolytic cleavages resulting in diverse chemerin forms with different levels of activity
-
-
?
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Glu(O-benzyl)-Ala-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
tissue factor pathway inhibitor + H2O
?
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the cleavage of the protein occurs between the Kunitz (K)1 and K2 domains (Lys86/Thr87) and at the active sites of the K2 (Arg107/Gly108) and K3 (Arg199/Ala200) domains
-
-
?
Z-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
factor IX + H2O
?
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activation of Factor IX in the intrinsic coagulation cascade
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-
?
factor IX + H2O
?
-
activation of Factor IX in the intrinsic coagulation cascade
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-
?
factor IX + H2O
activated factor IX + ?
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683239, 684078, 717416, 717844, 718042, 718045, 752615, 752757, 752995, 753069, 754510, 754516, 755585
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-
?
factor IX + H2O
activated factor IX + ?
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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
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?
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 + ?
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factor XIa is essential for the optimal activation of FIX
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-
?
factor IX + H2O
activated factor IX + ?
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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
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-
?
factor IX + H2O
activated factor IX + ?
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cleavage at Ala145 and Ala180, activity of wild-type and mutant enzymes with wild-type and mutant substrate, overview
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-
?
factor IX + H2O
activated factor IX + ?
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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 + ?
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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
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?
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
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?
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
-
-
?
