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
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intravascular
- thromboplastin
- aprotinin
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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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Activating Compound
Activating Compound on EC 3.4.21.7 - plasmin
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Blood serum
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2.0% equine serum increases plasmin activity by ca.50% when assayed with N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methyl-coumarin in milk
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fragment X
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profibrinolytic effect with plasmin. Rates of plasmin formation increase with increasing fragment X concentrations. Plasmin degrades clots containing fragment X more rapidly than fibrin clots
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high molecular weight urokinase-type plasminogen activator
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induces a significant increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes
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low molecular weight urokinase-type plasminogen activator
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induces a significant increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes
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urokinase-type plasminogen activator
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cleaves plasminogen to give active plasmin
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urokinase-type plasminogen activator
converts plasminogen bound to a plasminogen receptor into plasmin
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urokinase-type plasminogen activator
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plasminogen bound to immunoglobulin-like proteins LigA and LigB is converted to proteolytic active plasmin in the presence of urokinase-type plasminogen activator
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urokinase-type plasminogen activator
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cleaves plasminogen to give active plasmin
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the increased activity of plasmin after diafiltration may be also due to elimination of small enzyme inhibitor proteins
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additional information
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activation of a low concentration of plasminogen by cell-associated plasminogen activators produces sufficient active plasmin to rapidly and efficiently process pro-brain-derived neurotrophic factor in the pericellular environment
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additional information
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ATF-urokinase-type plasminogen activator causes little, if any, increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes
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additional information
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Glu-plasminogen incubated with adherent cells, i.e. CHO-K1, HEK-293 and HMEC-1 cells, is converted into plasmin for activation by constitutively expressed tPA, i.e. tissue-type plasminogen activator, or uPA, i.e. urokinase-type plasminogen activator
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additional information
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staphylokinase, SAK, forms a 1:1 stoichiometric complex with human plasmin and switches its substrate specificity to generate a plasminogen activator complex with a crucial requirement of a positively charged and an aromatic residue, respectively, at positions 43 and 44, i.e. SAKHis43 and SAKTyr44, for optimal functioning of SAK-Pm activator complex. Role of these residues in making cation-pi and pi-pi interactions with Trp215 of plasmin and thus establishing the crucial intermolecular contacts within the active site cleft of the activator complex for the cofactor activity of staphylokinase. Molecular modeling and structure analysis, overview
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additional information
the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases
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