3.4.21.7: plasmin
This is an abbreviated version!
For detailed information about plasmin, go to the full flat file.
Word Map on EC 3.4.21.7
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3.4.21.7
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fibrinolysis
-
fibrinogen
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urokinase
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coagulation
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clot
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tissue-type
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thrombin
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pai-1
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endothelial
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urokinase-type
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artery
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platelet
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upa
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thrombosis
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thrombolytic
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antithrombin
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streptokinase
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heparin
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inhibitor-1
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bleeding
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infarct
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kringle
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prothrombin
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coronary
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venous
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hemorrhage
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d-dimers
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kallikrein
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anticoagulant
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stroke
-
hemostatic
-
zymogen
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thromboembolic
-
zymography
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intravascular
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thromboplastin
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aprotinin
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2-macroglobulin
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amidolytic
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thrombin-antithrombin
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hypercoagulable
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tranexamic
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lipoproteina
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procoagulant
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antifibrinolytic
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recanalization
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prekallikrein
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alteplase
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fibrinopeptide
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nutrition
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analysis
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medicine
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degradation
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pharmacology
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thrombophilia
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agriculture
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food industry
- 3.4.21.7
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fibrinolysis
- fibrinogen
- urokinase
- coagulation
- clot
-
tissue-type
- thrombin
- pai-1
- endothelial
-
urokinase-type
- artery
- platelet
- upa
- thrombosis
-
thrombolytic
- antithrombin
- streptokinase
- heparin
- inhibitor-1
- bleeding
- infarct
-
kringle
- prothrombin
- coronary
- venous
- hemorrhage
-
d-dimers
- kallikrein
-
anticoagulant
- stroke
-
hemostatic
- zymogen
-
thromboembolic
-
zymography
-
intravascular
- thromboplastin
- aprotinin
-
2-macroglobulin
-
amidolytic
-
thrombin-antithrombin
-
hypercoagulable
-
tranexamic
-
lipoproteina
-
procoagulant
-
antifibrinolytic
-
recanalization
- prekallikrein
- alteplase
-
fibrinopeptide
- nutrition
- analysis
- medicine
- degradation
- pharmacology
- thrombophilia
- agriculture
- food industry
Reaction
Preferential cleavage: Lys-/- > Arg-/-; higher selectivity than trypsin. Converts fibrin into soluble products =
Synonyms
actase, delta-plasmin, EC 3.4.4.14, fibrinase, fibrinolysin, More, mu-plasmin, mu-plasminogen, PL, plasmin, plasminogen, PLG, Plm, PLS, serum tryptase, thrombolysin
ECTree
3.4.21.7 plasminAdvanced search results
results (
results (KM Value
KM Value on EC 3.4.21.7 - plasmin
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.00589
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the absence of fatty acids
0.00817
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.065 mM stearate
0.01133
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.115 mM stearate
0.01258
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.01 mM oleate
0.02009
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.025 mM oleate
0.02337
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.175 mM stearate
0.02371
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.01 mM arachidonate
0.02749
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.045 mM oleate
0.04265
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.025 mM arachidonate
0.05751
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.045 mM arachidonate
0.05985
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.065 mM arachidonate
0.07296
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.23 mM stearate
0.1311
D-norleucyl-hexahydrotyrosyl-lysine-p-nitroanilide
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in the presence of 0.065 mM oleate
0.138
D-Val-L-Leu-L-Lys-4-nitroanilide
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deletion mutant lacking the middle portion of the protein
0.269
D-Val-L-Leu-L-Lys-4-nitroanilide
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full-length plasmin, in phosphate buffered saline, pH 7.4, at 25°C
0.325
D-Val-L-Leu-L-Lys-4-nitroanilide
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truncated delta-plasmin, in phosphate buffered saline, pH 7.4, at 25°C
0.23
D-Val-Leu-Lys-p-nitroanilide
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plasmin adsorbed onto a carbon paste electrode
additional information
additional information
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ratio of kcat/Km values is 0.063 microM/s, pH 8.0, 37°C
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additional information
additional information
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although neither plasmin nor urokinase-type plasminogen activator exhibits allosteric cooperativity, modeling shows that cooperativity occurs at the system level because of substrate competition, molecular modeling and simulation, substrate competition and bistability, overview
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additional information
additional information
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plasmin shows substrate binding site cooperativity,
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additional information
additional information
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the enzyme activity follows Michaelis-Menten kinetics
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