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Information on EC 3.4.21.7 - plasmin
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3.4.21.7 plasminSpecify your search results
Word Map
- 3.4.21.7
-
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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Preferential cleavage: Lys-/- > Arg-/-; higher selectivity than trypsin. Converts fibrin into soluble products
Synonyms
plasminogen, plasmin, fibrinolysin, actase, thrombolysin, fibrinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
actase
-
-
-
-
EC 3.4.4.14
-
-
formerly
-
fibrinase
fibrinolysin
plasmin
plasminogen
serum tryptase
-
-
-
-
thrombolysin
-
-
-
-
additional information
plasminogen is a member of the peptidase S1 family
fibrinase
-
-
-
-
fibrinolysin
-
-
-
-
plasmin
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Lys-/- > Arg-/-; higher selectivity than trypsin. Converts fibrin into soluble products
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
9001-90-5
-
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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
Ac-FM(O2)YK-4-nitroanilide + H2O
Ac-FM(O2)YK + 4-nitroaniline
-
peptide substrate, M(O2) i.e. L-methionine sulfone
M(O2) i.e. L-methionine sulfone
-
?
Ac-KM(O2)FR-4-nitroanilide + H2O
Ac-KM(O2)FR + 4-nitroaniline
-
peptide substrate, M(O2) i.e. L-methionine sulfone
M(O2) i.e. L-methionine sulfone
-
?
Ac-KM(O2)YR-4-nitroanilide + H2O
Ac-KM(O2)YR + 4-nitroaniline
-
peptide substrate, M(O2) i.e. L-methionine sulfone
M(O2) i.e. L-methionine sulfone
-
?
Ac-RM(O2)WR-4-nitroanilide + H2O
Ac-RM(O2)WR + 4-nitroaniline
-
peptide substrate, M(O2) i.e. L-methionine sulfone
M(O2) i.e. L-methionine sulfone
-
?
Ac-RM(O2)YR-4-nitroanilide + H2O
Ac-RM(O2)YR + 4-nitroaniline
-
peptide substrate, M(O2) i.e. L-methionine sulfone
M(O2) i.e. L-methionine sulfone
-
?
alpha-lactalbumin + H2O
?
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
alphaS-casein + H2O
?
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
amyloid beta peptide Abeta42 + H2O
?
-
cleavage prevents the aggregation of Abeta42 and its cleavage products into beta-pleated sheet structure
-
?
beta-lactoglobulin + H2O
?
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
beta2-glycoprotein I + H2O
?
-
in human plasma beta2-glycoprotein I is proteolytically cleaved by plasmin in its domain V (nicked beta2GPI), resulting in binding to plasminogen
-
-
?
Boc-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
Boc-Glu-Lys-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
C1 inhibitor + H2O
?
-
the C1-inhibitor in its native state inhibits plasmin without significant degradation. If the C1-inhibitor is in a denatured polymeric state as can easily occur during storage, or as produced by heating of the native protein, it will be extensively degraded by plasmin
-
?
cadherin + H2O
?
-
plasmin bound to pneumococci is able to cleave recombinant vascular endothelial cadherin
-
-
?
carboxypeptidase N + H2O
?
-
plasmin cleaves the 83 kDa subunit of carboxypeptidase N between Arg457 and Ser458 and after prolonged incubation between Arg218 and Arg219. The small 55 kDa is cleaved to a 48 kDa product. The cleavage enhances the activity of carboxypeptidase N to 150% of the uncleaved enzyme
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-
?
chromogranin A + H2O
catestatin + ?
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chromogranin A-wild-type, chromogranin A-Gly364Ser and chromogranin A-Arg374Gln completely digested with plasmin at 0.0004 mM
-
-
?
complement component C5 + H2O
?
-
cleavage by plasmin produces bands of approximately 41000 Da and 30000-28000 Da
-
-
?
D-Nle-hexa-hydrotyrosyl-Lys-4-nitroanilide + H2O
D-Nle-hexa-hydrotyrosyl-Lys + 4-nitroaniline
-
-
-
?
D-Nle-hexahydrotyrosyl-Lys-4-nitroanilide + H2O
D-Nle-hexahydrotyrosyl-Lys + 4-nitroaniline
-
-
-
?
D-valyl-L-leucyl-L-lysine-4-nitroanilide + H2O
D-valyl-L-leucyl-L-lysine + 4-nitroaniline
-
-
-
-
?
epithelial sodium channel + H2O
epithelial sodium channel gamma subunit + ?
-
-
-
-
?
epithelial sodium channel gamma subunit + H2O
?
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plasmin activates epithelial sodium channels in association with inducing cleavage of the gamma subunit at gammaLys194, a site distal to the furin site. A gammaK194A mutant epithelial sodium channel subunit prevents both plasmin-dependent activation of epithelial sodium channel and plasmin-dependent production of a unique 70-kDa carboxyl-terminal gamma subunit cleavage fragment
-
-
?
fibrinogen + H2O
fragment X
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fragment X generated by limited plasmin digestion of fibrinogen
-
-
?
Glu-plasminogen + H2O
angiostatin 4.5 (AS4.5)
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AS4.5 is prepared from Glu-plasminogen by plasmin digestion
-
-
?
H-D-norleucyl-hexahydrotyrosol-lysine-para nitroanilide diacetate + H2O
?
-
-
-
-
?
hemofiltrate CC chemokine 1 + H2O
[9-74] processed variant of hemofiltrate CC chemokine 1 + ?
IkappaBalpha
?
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plasmin induces phosphorylation of IkappaBalpha, targeting the inhibitor to proteosomal degradation, consequently allowing nuclear translocation of NF-kappaB
-
-
?
inactive complement component C3b + H2O
?
-
plasmin degrades inactive complement component C3b through cleavage at R945 generating C3dg- and C3c-like species
-
-
?
insulin + H2O
?
-
cleavage of the Arg25-Gly and Lys29-Ala peptide bonds of the beta-chain of oxidized bovine insulin
-
-
?
kappa-casein + H2O
?
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
lactoferrin + H2O
?
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
Lys-Thr-Phe-Lys-Gly-Gly-Gly-Gly-Gly-Gly-Cys + H2O
Lys-Thr-Phe-Lys + Gly-Gly-Gly-Gly-Gly-Gly-Cys
-
-
-
-
?
N-methyl-D-aspartate receptor NR2A subunit
?
-
plasmin cleaves the native NR2A amino-terminal domain, removing the functional high affinity Zn2+ binding site. Plasmin also cleaves recombinant NR2A amino-terminal domain at lysine 317, thereby producing a 40 kDa fragment, consistent with plasmin-induced NR2A cleavage fragmentsobserved in rat brain preparations. Zn2+ inhibition of agonist-evoked N-methyl-D-aspartate receptor currents of NR1/NR2A-transfected HEK 293 cells and cultured cortical neurons is significantly reduced by plasmin treatment. Mutating the plasmin cleavage site Lys317 on NR2A to alanine blocks plasmins effect on Zn2+ inhibition
-
-
?
N-succinyl-L-alanyl-L-phenylalanyl-L-lysyl-7-amido-4-methylcoumarin + H2O
N-succinyl-L-alanyl-L-phenylalanyl-L-lysine + 7-amino-4-methylcoumarin
-
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
?
-
plasmin is a specific and efficient activator of pro-brain-derived neurotrophic factor. The pro-form is rapidly processed to an 18 kDa fragment at a low concentration of plasmin. This C-terminal fragment is equivalent in size to the furin-processed, mature form of wild-type brain-derived neurotrophic factor. The proteolytic cleavage site is Arg125-Val126, within the consensus furin-cleavage motif
-
-
?
pro-matrix metalloproteinase-1 + H2O
active matrix metalloproteinase-1
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matrix metalloproteinase-1 activation by the UP A/plasmin system
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
-
-
-
?
pro-matrix metalloproteinase-10 + H2O
matrix metalloproteinase-10 + ?
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
-
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
-
-
-
?
probrain derived neurotrophic factor + H2O
mature brain derived neurotrophic factor
-
-
-
-
?
Spectrozyme PL + H2O
L-norleucyl-L-hexahydrotyrosyl-L-lysine + 4-nitroaniline
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i.e. L-norleucyl-L-hexahydrotyrosyl-L-lysine-4-nitroanilide
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-
?
STAT3
?
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phosphorylates on Tyr705 and Ser727. Triggeres activation and nuclear translocation of STAT3
-
-
?
thrombin-activatable fibrinolysis inhibitor + H2O
?
-
mutant variants with variants in the amino acids surrounding the scissile R92-A93 bond such as P91S, R92K, and S90P exhibit specific impairment of activation by plasmin
-
-
?
tissue factor pathway inhibitor + H2O
?
-
plasmin increases tissue factor activity by inactivating the cell-associated tissue factor pathway inhibitor by a limited proteolysis
-
-
?
von Willebrand factor + H2O
?
-
the enzyme cleaves von Willebrand factor at K1491-R149. Globular von Willebrand factor is resistant to plasmin cleavage under static conditions, but is readily cleaved by plasmin under shear
-
-
?
amyloid-beta + H2O
?
-
the plasmin pathway is induced by aggregated amyloid-beta, which can lead to amyloid-beta degradation and inhibition of amyloid-beta actions
-
?
annexin A2 + H2O
?
-
interaction of plasmin with annexin A2 results in the stimulation of ERK1/2 and p38 MAPK, cyclooxygenase-2, and PGE(2), leading to increased matrix metalloproteinase-1 production
-
-
?
annexin A2 + H2O
?
-
stimulation of macrophages with plasmin leads to cleavage of ca. 6% of annexin A2 yielding a proteolytic fragment of ca. 33 kDa
-
-
?
beta-casein + H2O
?
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
Boc-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
chromogranin A + H2O
hCgA-(360-373) + ?
-
the product hCgA-(360-373) is a bioactive fragment that inhibits nicotinic-mediated catecholamine release. The plasminogen/plasmin system through its interaction with chromogranin A may play a major role in catecholaminergic function
-
?
complement component C3b + H2O
?
-
the enzyme inactivates the C3b molecule for complement C3b amplification
-
-
?
complement component C3b + H2O
?
-
cleavage by plasmin produces bands of 46000 Da, 40000 Da, 30000 Da and 17000 Da
-
-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
-
-
-
-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
-
-
-
-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
-
i.e. S-2251
-
-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
-
i.e. S2251
-
-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
-
chromogenic substrate S2251
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
hydrolysis by the plasmin-staphylokinase complex is twofold lower than in the case of the plasmin(ogen)-streptokinase complex
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
-
?
factor VIII + H2O
?
-
cleaves the heavy chain of factor VIII into two terminal products, A137336 and A2 subunits, by limited proteolysis at Lys36, Arg336, Arg372, and Arg740. The 80-kDa light chain is converted into a 67-kDa subunit by cleavage at Arg1689 and Arg1721
-
-
?
factor VIII + H2O
?
-
plasmin catalyzes activation or inactivation of factor VIII. The A2 domain of factor VIII, in particular residue Arg484, contributes to a unique plasmin-interactive site within the heavy chain that promotes plasmin docking during cofactor inactivation cleavage of the heavy chain
-
-
?