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
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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
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hemostatic
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zymogen
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thromboembolic
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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
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tissue-type
- thrombin
- pai-1
- endothelial
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urokinase-type
- artery
- platelet
- upa
- thrombosis
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thrombolytic
- antithrombin
- streptokinase
- heparin
- inhibitor-1
- bleeding
- infarct
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kringle
- prothrombin
- coronary
- venous
- hemorrhage
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d-dimers
- kallikrein
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anticoagulant
- stroke
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hemostatic
- zymogen
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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
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Engineering
Engineering on EC 3.4.21.7 - plasmin
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P611I
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mutant enzyme has no amidolytic activity with D-Val-Leu-Lys-p-nitroanilide
additional information
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active-site modified plasmin (Ah-plasmin) lacking enzymatic activity. Factor VIII binds with higher affinity than the A2 subunit to Ah-plasmin. The intact heavy chain also binds with ca. 10fold higher affinity than the light chain. Binding affinity of the R484A mutant of A2 subunit of factor VIII to Ah-plasmin is ca. 250fold lower than that of wild-type A2. A2 mutants (K377A, K466A, and R471A) also exhibit reduced binding affinity (by 10-20fold) compared with wild-type A2
additional information
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construction of a deletion mutant of plasminogen lacking the middle portion of the molecule, resulting in kringle I attachment to the serine protease domain. After expression in Escherichia coli and purification, mutant plasminogen is effectively converted to mutant plasmin by tissue plasminogen activator. Mutant plasmin is rapidly inhibited by alpha2-antiplasmin an alpha2-macroglobulin. It demonstrates fibrinolytic potency comparable to human plasma-derived plasmin
additional information
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in L5178Y cells with knock-out of the gene for annexin A2, the mRNA level of plasminogen is not substantially changed, but the protein level of plasmin is significantly lowered. mRNA and protein levels of S100A10 and fascin are lower in annexin A2 knock-out cells than in wild-type L5178Y cells
additional information
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mice homozygotically lacking the plasminogen inhibitor Pai-1 or the plasmin inhibitor alpha2-antiplasmin show an increase in hematopoietic progenitor cell mobilization in response to granulocyte colony-stimulating factor
additional information
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truncated plasmin variants. Miniplasmin (des-kringle 1-4 plasmin) contains the kringle 5 and the catalytic domain of plasmin, whereas microplasmin (des-kringle 1-5 plasmin) is composed of the catalytic domain only. Miniplasmin (des-kringle 1-4 plasmin) is as sensitive to fatty acids as plasmin, whereas the activity of microplasmin (des-kringle 1-5 plasmin) is not affected