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
-
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
- 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
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 (Substrates Products
Substrates Products on EC 3.4.21.7 - plasmin
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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
-
-
?
chromogranin A + H2O
catestatin + ?
-
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
?
-
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
-
fragment X generated by limited plasmin digestion of fibrinogen
-
-
?
Glu-plasminogen + H2O
angiostatin 4.5 (AS4.5)
-
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
?
-
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
-
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
-
i.e. L-norleucyl-L-hexahydrotyrosyl-L-lysine-4-nitroanilide
-
-
?
STAT3
?
-
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
-
-
?
Fibrin + H2O
?
-
the activation of plasminogen in blood plasma is the central event that results in the dissolution of the fibrin clot by proteolysis
-
-
?
Fibrin + H2O
?
-
fibrin is formed from fibrinogen by thrombin, EC 3.4.21.5
-
-
?
Fibrin + H2O
?
-
fibrin is broken down through the liberation of plasmin from plasminogen via cleavage by either tissue plasminogen activator and/or urokinase plasminogen activator
-
-
?
fibrin + H2O
soluble fibrin fragments
cleavage of the Lys583-Met584 peptide bond in the Aalpha chain, followed by the cleavage of the peptide bonds Lys206-Met207 and Lys230-Ala231, also in the Aalpha chain, thus releasing a C-terminal 40-kDa fragment and generating fragment X possessing 260 kDa. Cleavage of fragment X in all three chains results in one fragment Y (160 kDa) and one fragment D (100 kDa), and further cleavage of fragment Y produces a second fragment D and fragment E (60 kDa)
-
-
?
Fibrinogen + H2O
?
-
the fibrinogen alpha-chain is degraded in low-molecular-mass fragments of approximately 63000-60000 Da
-
-
?
hemofiltrate CC chemokine 1 + H2O
[9-74] processed variant of hemofiltrate CC chemokine 1 + ?
-
-
further degradation of the active product
?
hemofiltrate CC chemokine 1 + H2O
[9-74] processed variant of hemofiltrate CC chemokine 1 + ?
-
urokinase plasminogen activator and plasmin efficiently convert hemofiltrate CC chemokine 1 into its active [9-74] processed variant
-
?
osteopontin + H2O
?
-
osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a substrate for plasmin and cathepsin D
-
-
?
osteopontin + H2O
?
-
osteopontin, purified from human milk, is cleaved at multiple sites close to its integrin-binding motifs, e.g. cleavage at Arg152-Ser153, detailed overview
-
-
?
platelet-derived growth factor-C + H2O
?
-
plasmin is the major protease responsible for processing platelet-derived growth factor-C in patients undergoing retinal surgery. Plasmin is vastly more potent (192times faster) than tissue plasminogen activator in processing the substrate
-
-
?
platelet-derived growth factor-C + H2O
?
-
plasmin is the major protease responsible for processing platelet-derived growth factor-C in rabbits with proliferative vitreoretinopathy
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
-
-
-
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
vascular endothelial growth factor + H2O
?
-
cleavage site: Arg110-/-Ala111. The mutant vascular endothelial growth factors R110A, R110Q and A111P are resistant to cleavage
-
?
vascular endothelial growth factor + H2O
?
-
in non-healing wounds plasmin cleaves and inactivates vascular endothelial growth factor VEGF165
-
?
additional information
?
-
-
complexes of streptokinase with human plasminogen can hydrolytically activate other plasminogen molecules to plasmin, which then dissolve blood clots
-
-
?
additional information
?
-
-
the plasminogen activation system is mostly recognized for its fibrinolytic activity but is also upregulated in chronic inflammatory diseases, including atherosclerosis and arthritis. Plasmin is a potent activator of human monocytes and a number of other cells. In monocytes plasmin elicits full-blown proinflammatory activation encompassing lipid mediator release, chemotaxis and induction of cytokines and other proinflammatory genes. Cell activation is dependent on the binding of the plasmin molecule via its lysine binding sites as well as on the intact catalytic center of plasmin, indicating proteolytic activation. Cell activation occurs through a yet unidentified receptor which is specific for plasmin and that, at least in monocytes, is not activated by other proteases, such as factor Va and Xa, the serine proteases thrombin, alpha-chymotrypsin, human neutrophil elastase or cathepsin G
-
?
additional information
?
-
-
plasmin does not induce phosphorylation of JAK2 or JAK3. Does not activate SAP/JNK. Does not trigger activation and nuclear translocation ofSTAT1, STAT5A, or STAT5B
-
-
?
additional information
?
-
-
plasmin is 3-4fold less efficient in processing of the chromogranin A-Pro370Leu variant as compared to wild-type and the other varinats due to less efficient cleavage between Arg373-Arg374
-
-
?
additional information
?
-
-
plasmin triggeres phosphorylation of ERK1/2 in a concentration-dependent manner, but not of Akt
-
-
?
additional information
?
-
-
addition of plasmin to fibroblast-like cells from dental pulp induces an increase in the intracellular Ca2+ concentration, which may be inhibited by inhibition of receptor PAR-1. Plasmin stimulates the expression of interleukin-8 mRNA and prostaglandin E2 release
-
-
?
additional information
?
-
-
both plasmin and thrombin increase cell surface tissue factor activity in human pleural mesothelial cells by 3- to 4fold. Plasmin-induced tissue factor activity is not dependent on the de novo synthesis of tissue factor. In HUVEC, plasmin has a minimal effect on unperturbed HUVEC whereas it markedly increases tissue factor activity of activated HUVEC. Plasmin treatment neither affects anionic phospholipid levels at the cell surface nor releases protein disulfide isomerase
-
-
?
additional information
?
-
-
intravitreal plasmin injection increases the rate of vitreous removal in rabbits
-
-
?
additional information
?
-
-
plasmin can differentially modulate platelet aggregation in response to intrinsic heterogeneities within the insulin-like growth factor/insulin-like growth factor binding protein complexes
-
-
?
additional information
?
-
-
adherence of plasmin-coated encapsulated or unencapsulated pneumococci induces sporadic disruption of EaHy or A549 monolayer cell junctions
-
-
?
additional information
?
-
-
protein context, as well as the identity of amino acids at protease cleavage sites, dictate protease specificity
-
-
?
additional information
?
-
-
plasmin selectively cleaves arginyl-X and lysyl-X peptide bonds in many target proteins
-
-
?
additional information
?
-
rather broad specificity of plasmin in vivo catalyzing the inactivation and degradation of matrix proteins such as collagens, fibronectin, and laminins, and components of the blood coagulation cascade such as coagulation factor FVa, von Willebrand factor, and thrombospondin
-
-
?
additional information
?
-
-
subsite interactions of plasmin with substrates and inhibitors through computational docking analysis using the structure with PDB ID 1BML for plasmin in complex with streptokinase and no ligand molecules, molecular dynamic simulation of plasmin, overview. D/L-Ile-Phe-Lys substrate-binding modes
-
-
?
additional information
?
-
-
plasmin, possessing various substrate binding sites, shows substrate binding site cooperativity, molecular modeling of the plasmin-Ac-RM(O2)YR-H complex
-
-
?
additional information
?
-
-
staphylokinase forms a 1:1 stoichiometric complex with human plasmin and switches its substrate specificity to generate a plasminogen activator complex
-
-
?
additional information
?
-
-
substrate competition with urokinase-type plasminogen activator and bistability, overview
-
-
?
additional information
?
-
-
plasmin may serve as an endogenous PAR1 activator that can increase Ca2+ concentration, in astrocytes and potentiate N-methyl-D-aspartate receptor synaptic currents in CA1 pyramidal neurons
-
-
?
additional information
?
-
-
role for plasmin in augmenting hematopoietic progenitor cell mobilization in response to granulocyte colony-stimulating factor
-
-
?
additional information
?
-
-
steroid-treated ovariectomized mice deficient in tissue inhibitor of metalloprotease-1 and exposed to estrogen show a significant increase in plasmin activity. Increase is probably due to reduced expression of plasmin inhibitors serpinb7 and serpinb2
-
-
?
additional information
?
-
-
potentiates TLR2 and TLR4 signalling in RAW264.7 macrophages. Enhances endogenous production of TNFalpha and activation of an NF-kappaB reporter plasmid
-
-
?
