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Information on EC 3.4.21.7 - plasmin and Organism(s) Homo sapiens and UniProt Accession P00747

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.7 plasmin
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P00747 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
mu-plasmin
serine protease domain of plasmin
mu-plasminogen
-
actase
-
-
-
-
delta-plasmin
-
a truncated non-glycosylated plasmin variant
fibrinase
-
-
-
-
fibrinolysin
-
-
-
-
plasminogen
serum tryptase
-
-
-
-
thrombolysin
-
-
-
-
additional information
plasminogen is a member of the peptidase S1 family
CAS REGISTRY NUMBER
COMMENTARY hide
9001-90-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-KM(O2)YR + H2O
?
show the reaction diagram
-
-
-
?
Ac-RM(O2)YR + H2O
?
show the reaction diagram
-
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
?
fibrin + H2O
soluble fibrin fragments
show the reaction diagram
MT1-matrix metalloproteinase + H2O
?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-10 + H2O
matrix metalloproteinase-10 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
show the reaction diagram
-
-
-
?
Ac-FM(O2)YK-4-nitroanilide + H2O
Ac-FM(O2)YK + 4-nitroaniline
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
peptide substrate, M(O2) i.e. L-methionine sulfone
M(O2) i.e. L-methionine sulfone
-
?
ADAMTS13 + H2O
?
show the reaction diagram
AIYRSR + H2O
AIYR + Ser-Arg
show the reaction diagram
-
-
-
?
amyloid beta peptide Abeta42 + H2O
?
show the reaction diagram
-
cleavage prevents the aggregation of Abeta42 and its cleavage products into beta-pleated sheet structure
-
?
amyloid-beta + H2O
?
show the reaction diagram
annexin A2 + H2O
?
show the reaction diagram
benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
beta2-glycoprotein I + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
Boc-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
C1 inhibitor + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
plasmin bound to pneumococci is able to cleave recombinant vascular endothelial cadherin
-
-
?
carboxypeptidase N + H2O
?
show the reaction diagram
-
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
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
chromogenic substrate S-2551 + H2O
?
show the reaction diagram
-
-
-
?
chromogranin A + H2O
catestatin + ?
show the reaction diagram
-
chromogranin A-wild-type, chromogranin A-Gly364Ser and chromogranin A-Arg374Gln completely digested with plasmin at 0.0004 mM
-
-
?
chromogranin A + H2O
hCgA-(360-373) + ?
show the reaction diagram
CIYRSR + H2O
CIYR + Ser-Arg
show the reaction diagram
-
-
-
?
complement component C3 + H2O
complement component C3a + ?
show the reaction diagram
-
-
-
-
?
complement component C3a + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C3b + H2O
?
show the reaction diagram
complement component C5 + H2O
?
show the reaction diagram
-
cleavage by plasmin produces bands of approximately 41000 Da and 30000-28000 Da
-
-
?
D-Ile-Phe-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
D-Nle-hexa-hydrotyrosyl-Lys-4-nitroanilide + H2O
D-Nle-hexa-hydrotyrosyl-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
D-Nle-hexahydrotyrosyl-Lys-4-nitroanilide + H2O
D-Nle-hexahydrotyrosyl-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
show the reaction diagram
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
D-Val-Leu-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
show the reaction diagram
D-valyl-L-leucyl-L-lysine-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
epithelial sodium channel + H2O
epithelial sodium channel gamma subunit + ?
show the reaction diagram
-
-
-
-
?
ERK1/2
?
show the reaction diagram
-
triggers activation
-
-
?
factor VIII + H2O
?
show the reaction diagram
Fibrin + H2O
?
show the reaction diagram
fibrin + H2O
soluble fibrin fragments
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fragment X
show the reaction diagram
-
fragment X generated by limited plasmin digestion of fibrinogen
-
-
?
GIVRSR + H2O
GIVR + Ser-Arg
show the reaction diagram
-
-
-
?
GIYRSR + H2O
GIYR + Ser-Arg
show the reaction diagram
-
-
-
?
Glu-plasminogen + H2O
angiostatin 4.5 (AS4.5)
show the reaction diagram
-
AS4.5 is prepared from Glu-plasminogen by plasmin digestion
-
-
?
GPGRVV + H2O
GPGR + Val-Val
show the reaction diagram
-
-
-
?
H-D-norleucyl-hexahydrotyrosol-lysine-para nitroanilide diacetate + H2O
?
show the reaction diagram
-
-
-
-
?
H-D-Val-Leu-Lys-p-nitroaniline dihydrochloride + H2O
?
show the reaction diagram
-
-
-
-
?
hemofiltrate CC chemokine 1 + H2O
[9-74] processed variant of hemofiltrate CC chemokine 1 + ?
show the reaction diagram
IkappaBalpha
?
show the reaction diagram
-
plasmin induces phosphorylation of IkappaBalpha, targeting the inhibitor to proteosomal degradation, consequently allowing nuclear translocation of NF-kappaB
-
-
?
inactive complement component C3b + H2O
?
show the reaction diagram
-
plasmin degrades inactive complement component C3b through cleavage at R945 generating C3dg- and C3c-like species
-
-
?
insulin + H2O
?
show the reaction diagram
-
cleavage of the Arg25-Gly and Lys29-Ala peptide bonds of the beta-chain of oxidized bovine insulin
-
-
?
JAK1
?
show the reaction diagram
-
triggers tyrosine phosphorylation
-
-
?
KKSPGRVVGGSVAH + H2O
KKSPGR + VVGGSVAH
show the reaction diagram
-
-
-
?
KQWK-4-nitroanilide + H2O
KQWK + 4-nitroaniline
show the reaction diagram
-
peptide substrate
-
-
?
KTFK-4-nitroanilide + H2O
KTFK + 4-nitroaniline
show the reaction diagram
-
peptide substrate
-
-
?
L-Ile-Phe-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
LGGSAMSRMSSLE + H2O
LGGSAMSR + MSSLE
show the reaction diagram
-
-
-
?
LGGSGANFRGKLE + H2O
LGGSGANFR + GKLE
show the reaction diagram
-
-
-
?
LGGSGAVYKAGLE + H2O
LGGSGAVYK + AGLE
show the reaction diagram
-
-
-
?
LGGSGIGRSRSLE + H2O
LGGSGIGR + SRSLE
show the reaction diagram
-
-
-
?
LGGSGIYRSRSLE + H2O
LGGSGIYR + SRSLE
show the reaction diagram
-
-
-
?
LGGSGIYRSVSLE + H2O
LGGSGIYR + SVSLE
show the reaction diagram
-
-
-
?
LGGSGIYRVRSLE + H2O
LGGSGIYR + VRSLE
show the reaction diagram
-
-
-
?
LGGSGPYRSRSLE + H2O
LGGSGPYR + SRSLE
show the reaction diagram
-
-
-
?
LGGSGTQRRLRLE + H2O
LGGSGTQR + RLRLE
show the reaction diagram
-
-
-
?
LGGSGYKIGGSLE + H2O
LGGSGYK + IGGSLE
show the reaction diagram
-
-
-
?
LGGSIRYKGKSLE + H2O
LGGSIRYK + GKSLE
show the reaction diagram
-
-
-
?
LGGSSIYRSRSLE + H2O
LGGSSIYR + SRSLE
show the reaction diagram
-
-
-
?
N-methyl-D-aspartate receptor NR2A subunit
?
show the reaction diagram
-
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 plasmin’s effect on Zn2+ inhibition
-
-
?
osteopontin + H2O
?
show the reaction diagram
p38 MAPK
?
show the reaction diagram
-
triggers phosphorylation
-
-
?
p65
?
show the reaction diagram
-
triggeres nuclear translocation
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
-
-
-
?
platelet-derived growth factor-C + H2O
?
show the reaction diagram
-
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
-
-
?
pro-brain-derived neurotrophic factor + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
matrix metalloproteinase-1 activation by the UP A/plasmin system
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
show the reaction diagram
-
-
-
-
?
protamin-heparin complex + H2O
?
show the reaction diagram
-
-
-
-
?
RQFR-4-nitroanilide + H2O
RQFR + 4-nitroaniline
show the reaction diagram
-
peptide substrate
-
-
?
RQWK-4-nitroanilide + H2O
RQWK + 4-nitroaniline
show the reaction diagram
-
peptide substrate
-
-
?
S-2251 + H2O
?
show the reaction diagram
-
-
-
?
S-sulfo-fibrinogen + H2O
?
show the reaction diagram
-
cleaves only Lys and Arg peptide bonds
-
-
?
Spectrozyme PL + H2O
L-norleucyl-L-hexahydrotyrosyl-L-lysine + 4-nitroaniline
show the reaction diagram
-
i.e. L-norleucyl-L-hexahydrotyrosyl-L-lysine-4-nitroanilide
-
-
?
SPGRVV + H2O
SPGR + Val-Val
show the reaction diagram
-
-
-
?
STAT3
?
show the reaction diagram
-
phosphorylates on Tyr705 and Ser727. Triggeres activation and nuclear translocation of STAT3
-
-
?
thrombin-activatable fibrinolysis inhibitor + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
plasmin increases tissue factor activity by inactivating the cell-associated tissue factor pathway inhibitor by a limited proteolysis
-
-
?
Tosyl-Arg methyl ester + H2O
?
show the reaction diagram
-
p-tosyl-Arg methyl ester
-
-
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
transforming growth factor beta 2 + H2O
?
show the reaction diagram
-
-
-
-
?
TYK2
?
show the reaction diagram
-
triggers tyrosine phosphorylation
-
-
?
vascular endothelial growth factor + H2O
?
show the reaction diagram
von Willebrand factor + H2O
?
show the reaction diagram
-
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
-
-
?
VQYK-4-nitroanilide + H2O
VQYK + 4-nitroaniline
show the reaction diagram
-
peptide substrate
-
-
?
VQYR-4-nitroanilide + H2O
VQYR + 4-nitroaniline
show the reaction diagram
-
peptide substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibrin + H2O
?
show the reaction diagram
-
-
-
?
fibrin + H2O
soluble fibrin fragments
show the reaction diagram
-
-
-
?
MT1-matrix metalloproteinase + H2O
?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-10 + H2O
matrix metalloproteinase-10 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
show the reaction diagram
-
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
show the reaction diagram
-
-
-
?
ADAMTS13 + H2O
?
show the reaction diagram
-
inactivation
-
-
?
amyloid-beta + H2O
?
show the reaction diagram
-
the plasmin pathway is induced by aggregated amyloid-beta, which can lead to amyloid-beta degradation and inhibition of amyloid-beta actions
-
?
beta2-glycoprotein I + H2O
?
show the reaction diagram
-
in human plasma beta2-glycoprotein I is proteolytically cleaved by plasmin in its domain V (nicked beta2GPI), resulting in binding to plasminogen
-
-
?
chromogranin A + H2O
hCgA-(360-373) + ?
show the reaction diagram
-
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 C3 + H2O
complement component C3a + ?
show the reaction diagram
-
-
-
-
?
complement component C3a + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C3b + H2O
?
show the reaction diagram
complement component C5 + H2O
?
show the reaction diagram
-
cleavage by plasmin produces bands of approximately 41000 Da and 30000-28000 Da
-
-
?
epithelial sodium channel + H2O
epithelial sodium channel gamma subunit + ?
show the reaction diagram
-
-
-
-
?
Fibrin + H2O
?
show the reaction diagram
fibrin + H2O
soluble fibrin fragments
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
the fibrinogen alpha-chain is degraded in low-molecular-mass fragments of approximately 63000-60000 Da
-
-
?
Glu-plasminogen + H2O
angiostatin 4.5 (AS4.5)
show the reaction diagram
-
AS4.5 is prepared from Glu-plasminogen by plasmin digestion
-
-
?
hemofiltrate CC chemokine 1 + H2O
[9-74] processed variant of hemofiltrate CC chemokine 1 + ?
show the reaction diagram
-
urokinase plasminogen activator and plasmin efficiently convert hemofiltrate CC chemokine 1 into its active [9-74] processed variant
-
?
inactive complement component C3b + H2O
?
show the reaction diagram
-
plasmin degrades inactive complement component C3b through cleavage at R945 generating C3dg- and C3c-like species
-
-
?
N-methyl-D-aspartate receptor NR2A subunit
?
show the reaction diagram
-
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 plasmin’s effect on Zn2+ inhibition
-
-
?
osteopontin + H2O
?
show the reaction diagram
-
osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a substrate for plasmin and cathepsin D
-
-
?
tissue factor pathway inhibitor + H2O
?
show the reaction diagram
-
plasmin increases tissue factor activity by inactivating the cell-associated tissue factor pathway inhibitor by a limited proteolysis
-
-
?
vascular endothelial growth factor + H2O
?
show the reaction diagram
-
in non-healing wounds plasmin cleaves and inactivates vascular endothelial growth factor VEGF165
-
?
von Willebrand factor + H2O
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-aminohexanoate
-
Aedes aegypti trypsin inhibitor
-
-
alpha-antiplasmin
potent inhibitor
-
alpha2-antiplasmin
the main physiological inhibitor and a serpin
-
alpha2-Macroglobulin
general protease inhibitor
-
amyloid precursor-like protein 2
-
-
Aprotinin
-
bdellin
-
-
bikazin salivary inhibitor
-
-
bikunin
-
-
chicken liver trypsin inhibitor
-
-
CU-2010
potent inhibitpr
-
D-Ile-Phe-Lys
-
D-Ile-Phe-Lys-CH2Cl
-
DX-1000
-
-
histidine-rich glycoprotein
binds at sites of tissue injury and seems to act as a high-affinity receptor to immobilize plasminogen on cell surfaces
-
infestin
-
-
KD1-L17R
-
-
KM(O2)YR-H
-
Kunitz-type inhibitor 2
-
-
L-Ile-Phe-Lys
-
Leucaena-type trypsin inhibitor
-
-
neuroserpin
mainly expressed in the brain, a serpin and single-chain glycoprotein of 55 kDa containing three potential N-glycosylation sites at Asn141, Asn305, and Asn385
-
nexin 2
-
-
ONO-3307
i.e. 4-sulfamoyl phenyl-4-guanidinobenzoate methanesulfonate
plasminogen activator inhibitors 1
-
-
plasminogen activator inhibitors 2
-
-
plasminostreptin
-
-
TdPI tryptase inhibitor
-
-
textilinin-1
-
-
tissue factor pathway inhibitor-1
-
-
tissue factor pathway inhibitor-2
-
-
Tra-Tyr(O-Pic)-CONH-(C6H6)-(CH2)4-CH3
-
Tra-Tyr(O-Pic)-CONH-(C6H6)-CH2-CH3
-
Tra-Tyr(O-Pic)-CONH-(CH2)2-CH(CH3)-CH3
-
Tra-Tyr(O-Pic)-CONH-(CH2)7-COOH
-
Tra-Tyr(O-Pic)-CONH-(CH2)7-NH2
-
Tranexamic acid
-
YO-2
i.e. Tra-Tyr(O-Pic)-CONH-(CH2)7-CH3
(4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-phenyl-propionylamino]-phenyl)-acetic acid
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.63 mM
(E)-5,5'-(but-2-ene-1,4-diylbis(oxy))bis(2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4Hchromen-4-one
-
about 43% residual activity at 0.4 mM
2-(3-[3-[(6-amino-hexyl)-(2-benzyloxycarbonylamino-3-phenyl-propionyl)-amino]-2-oxo-cyclohexyl]-propionylamino)-3-(1H-indol-3-yl)-propionic acid methyl ester
-
IC50: 0.024 mM
2-[(4-Aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionic acid pyridin-2-ylmethyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0042 mM
2-[3-(3-[(6-amino-hexyl)-[2-benzyloxycarbonylamino-3-(1H-indol-3-yl)-propionyl]-amino]-2-oxo-cyclohexyl)-propionylamino]-3-(1H-indol-3-yl)-propionic acid methyl ester
-
IC50: 0.02 mM
3-(8-(4-((2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4-oxo-4H-chromen-5-yloxy)methyl)-1H-1,2,3-triazol-1-yl)heptyl)-2-(4-O-sulfonato-phenyl)quinazolin-4(3H)-one
-
about 1% residual activity at 0.4 mM
3-(8-(4-((2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4-oxo-4H-chromen-5-yloxy)methyl)-1H-1,2,3-triazol-1-yl)octyl)-2-(4-O-sulfonato-phenyl)quinazolin-4(3H)-one
4-(2-aminoethyl)benzenesulfonyl fluoride
-
-
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid heptyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.024 mM, IC50 in reaction with fibrin is 0.0039 mM
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid hexyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.018 mM, IC50 in reaction with fibrin is 0.0043 mM
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid methyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0009 mM, IC50 in reaction with fibrin is 0.0061 mM
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid octyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is above 0.1 mM, IC50 in reaction with fibrin is 0.005 mM
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid heptyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0014 mM, IC50 in reaction with fibrin is 0.00042 mM
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid hexyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0015 mM, IC50 in reaction with fibrin is 0.0004 mM
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid methyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.001 mM, IC50 in reaction with fibrin is 0.00078 mM
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid octyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0025 mM, IC50 in reaction with fibrin is 0.00056 mM
4-amidinophenyl methane-sulfonyl fluoride
-
abolishes plasmin-induced Ca2+ elevation by its pretreatment of plasmin
4-aminobenzamidine
-
competitive inhibition
4-aminomethylbenzamidine
-
competitive inhibition
4-carboxybenzamidine
-
competitive inhibition
479-504 peptide of factor VIII
-
blocks A2 subunit binding to Ah-plasmin by ca. 50% in a dose-dependent manner
-
484-509 peptide of factor VIII
-
blocks A2 subunit binding to Ah-plasmin by ca. 50% in a dose-dependent manner
-
489-514 peptide of factor VIII
-
weakly inhibits binding of the A2 subunit and plasmin with ca. 80% residual binding at the highest concentration (0.8 mM) of peptide
-
5,5'-(butane-1,4-diylbis(oxy))bis(2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4H-chromen-4-one
-
about 42% residual activity at 0.4 mM
6-aminohexanoic acid
A2 subunit of factor VIII
-
plasmin-catalyzed activation of factor VIII is significantly inhibited by the addition of isolated A2 subunit of factor VIII in a dose-dependent manner
-
actin
-
actin inhibition of the fibrinolytic activity of plasmin is due to its competition with fibrin for the lysine binding sites of the enzyme
AG490
-
JAK inhibitor, inhibits JAK1 but does not inhibit TYK2 phosphorylation by plasmin. Impairs plasmin-mediated phosphorylation of ERK1/2, Akt1, and the subsequent phosphorylation of IkappaBalpha, but not that of p38 MAPK. Inhibits plasmin-induced TNF-alpha release by 63% and IL-6 release by 76%
Ah-plasmin
-
immobilized Ah-plasmin inhibits the A2 binding to Ah-plasmin by ca. 80% in a dose-dependent manner
-
AKbetaBA
-
inhibits plasmin-induced TNF-alpha release by 70%. Inhibits plasmin-induced activation of NF-kappaB by 66%
alpha(2)-plasmin inhibitor
-
blocks plasmin activity
-
alpha-antitrypsin
-
-
-
alpha1 globulin
-
-
-
alpha1-protease inhibitor
-
plasmin bound to fibrin is completely protected
-
alpha2 globulin
-
-
-
alpha2-antiplasmin
-
alpha2-Macroglobulin
-
alpha2-Plasmin inhibitor
-
kringle domains K2, K3, and K5 are involved in the modulation of Plm activity
-
aminomethyl cyclohexane carboxylic acid
-
-
annexin II tetramer
-
promotes plasmin inactivation by stimulating the autoproteolytic digestion of plasmin heavy and light chains, also stimulates formation of plasmin. annexin II tetramer may function to provide the cell surface with a transient pulse of plasmin activity
-
antiplasmin
-
the inhibition of plasmin by antiplasmin can be reduced by high molecular weight fibrin degradation products with carboxy-terminal lysine residues
-
Aprotinin
arsenic acid
-
organometallic complexes composed of humic acid and arsenic acid show enhanced inhibition of plasmin activity as compared with either arsenic or humic acid alone
benzamidine
-
competitive inhibition
C1 inhibitor
-
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
-
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-(1,1-dimethyl-propylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0062 mM, IC50 in reaction with fibrin is 0.0012 mM
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-heptylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.011 mM, IC50 in reaction with fibrin is 0.0033 mM
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-hexylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.013 mM, IC50 in reaction with fibrin is 0.0027 mM
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-nonylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0083 mM, IC50 in reaction with fibrin is 0.0013 mM
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-octylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.007 mM, IC50 in reaction with fibrin is 0.0018 mM
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-pentylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.01 mM, IC50 in reaction with fibrin is 0.0013 mM
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(1,1-dimethyl-propylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.085 mM, IC50 in reaction with fibrin is 0.019 mM
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(4-butyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.009 mM, IC50 in reaction with fibrin is 0.0023 mM
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(4-hexyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.006 mM, IC50 in reaction with fibrin is 0.0035 mM
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(4-pentyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.009 mM, IC50 in reaction with fibrin is 0.0047 mM
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-propylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0092 mM, IC50 in reaction with fibrin is 0.002 mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(1,1-dimethyl-propylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.013 mM, IC50 in reaction with fibrin is 0.0017 mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(3-methyl-butylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00046 mM, IC50 in reaction with fibrin is 0.000056 mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-butyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00079 mM, IC50 in reaction with fibrin is 0.00009 mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-ethyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00063 mM, IC50 in reaction with fibrin is 0.000098 mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-hexyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00049 mM, IC50 in reaction with fibrin is 0.00024 mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-methoxymethyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00023 mM, IC50 in reaction with fibrin is mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-pentyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00057 mM, IC50 in reaction with fibrin is 0.00007 mM
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(pyridin-4-ylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00098 mM, IC50 in reaction with fibrin is 0.00017 mM
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-heptylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0011 mM, IC50 in reaction with fibrin is 0.00043 mM
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-hexylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0012 mM, IC50 in reaction with fibrin is 0.00038 mM
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-nonylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
-
potent and selective inhibitor for plasmin, IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0005 mM, IC50 in reaction with fibrin is 0.0001 mM
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-pentylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.011 mM, IC50 in reaction with fibrin is 0.0001 mM
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-[(pyridin-2-ylmethyl)-carbamoyl]-ethyl}-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0015 mM, IC50 in reaction with fibrin is 0.00052 mM
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-[(pyridin-4-ylmethyl)-carbamoyl]-ethyl}-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is0.0053 mM, IC50 in reaction with fibrin is 0.0014 mM
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-[benzyl-carbamoyl]-ethyl}-phenyl ester 2-bromo-benzyl ester
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0011 mM, IC50 in reaction with fibrin is 0.0003 mM
Cholesterol sulfate
-
reduces plasmin activity in a dose-dependent manner
cis-parinaric acid
-
more than 60% inhibition of pro-matrix metalloproteinase-3 activation at 0.05 mM
CO
-
CO elicits hypofibrinolysis by enhancing alpha2-antiplasmin activity and decreasing plasmin activity
D-Ile-Phe-Lys-CN
-
-
D-Ile-Phe-Lys-NH2
-
-
D-Leu-Lys-benzylamide
-
weak inhibitor of amidolytic activity
D-Phe-Lys-benzylamide
-
inhibition of fibrinolytic activity, no inhibition of amidolytic activity
diisopropyl fluorophosphate
-
does not block binding of hepatocytes from mice to immobilized plasmin, but blocks active site of plasmin and its ability to phosphorylate ERK1/2
discreplasminin
-
isolated from Tityus discrepans scorpion venom. Peptide with a relative molecular weight of less than 6000 Da and a pI value of 8.0. Discreplasminin strongly inhibits plasmin and moderately inhibits tissue plasminogen activator
-
disodium 2-methoxy-4-[(1E)-3-[4-methyl-2-(sulfonatooxy)phenyl]-3-oxoprop-1-en-1-yl]phenyl sulfate
-
about 73% residual activity at 0.4 mM
disodium 2-methoxy-6-[(1E)-3-oxo-3-[2-(sulfonatooxy)phenyl]prop-1-en-1-yl]phenyl sulfate
-
about 40% residual activity at 0.4 mM
disodium 3,5-dimethoxy-2-[(2E)-3-[3-methoxy-4-(sulfonatooxy)phenyl]prop-2-enoyl]phenyl sulfate
-
about 40% residual activity at 0.4 mM
disodium 3,5-dimethoxy-2-[(2E)-3-[4-methoxy-3-(sulfonatooxy)phenyl]prop-2-enoyl]phenyl sulfate
-
about 75% residual activity at 0.4 mM
disodium 3-(4-oxo-3-[[1-(4-[4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
-
about 40% residual activity at 0.4 mM
disodium 3-(acetyloxy)-5-(4-oxo-3-[4-[4-([4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]butyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
-
about 84% residual activity at 0.4 mM
disodium 3-[4-oxo-3-[3-[4-([4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]propyl]quinazolin-2(4H)-yl]phenyl sulfate
-
about 35% residual activity at 0.4 mM
disodium 4-(4-oxo-3,4-dihydroquinazolin-2-yl)benzene-1,3-diyl disulfate
-
about 77% residual activity at 0.4 mM
disodium 4-(4-oxo-3-[5-[5-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]pentyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
disodium 4-(4-oxo-3-[[1-(10-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]decyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
-
about 5% residual activity at 0.4 mM
disodium 4-(4-oxo-3-[[1-(12-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]dodecyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
disodium 4-(4-oxo-3-[[1-(7-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]heptyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
-
about 30% residual activity at 0.4 mM
disodium 4-[(2E)-3-(2-methoxyphenyl)prop-2-enoyl]benzene-1,3-diyl disulfate
-
about 39% residual activity at 0.4 mM
disodium 4-[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]benzene-1,3-diyl disulfate
-
about 31% residual activity at 0.4 mM
disodium 4-[4-oxo-3-[11-[4-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]undecyl]quinazolin-2(4H)-yl]phenyl sulfate
-
about 3% residual activity at 0.4 mM
disodium 4-[4-oxo-3-[8-[4-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]octyl]quinazolin-2(4H)-yl]phenyl sulfate
-
about 7% residual activity at 0.4 mM
disodium 4-[4-oxo-3-[9-[4-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]nonyl]quinazolin-2(4H)-yl]phenyl sulfate
-
about 7% residual activity at 0.4 mM
disodium 4-[4-oxo-6-(sulfonatooxy)-4H-chromen-2-yl]phenyl sulfate
-
about 85% residual activity at 0.4 mM
elaidic acid
-
60% inhibition of pro-matrix metalloproteinase-3 activation at 0.05 mM
epsilon-aminocaproic acid
Fibrin
-
inhibits hydrolysis of D-Val-Leu-Lys-p-nitroanilide
fibrinogen
-
fragment X
-
competitive inhibitor of plasmin chromogenic activity
-
human aprotinin analogue
-
-
-
human plasma protein inhibitors
-
-
-
humic acid
-
0.02-0.48 mg/ml, up to 95% inhibition, natural and synthetic. Organometallic complexes composed of humic acid and arsenic acid show enhanced inhibition of plasmin activity as compared with either arsenic or humic acid alone
hydroxyethyl starch 130
-
plasma diluted with hydroxyethyl starch 130 has a significant more than 25% attenuation of plasmin-mediated decreases in the maximum rate of thrombus generation and total thrombus generation compared with 0.9% NaCl diluted and undiluted plasma. Enhances fibrinolysis by diminishing alpha2-antiplasmin-plasmin interactions
-
L-lysine
-
-
LEKTI
-
potent noncompetitive inhibitor, recombinant LEKTI is purified using a baculovirus/insect cell expression system
Leu-Lys-benzylamide
-
inhibition of fibrinolytic activity, no inhibition of amidolytic activity
Lima bean trypsin inhibitor
-
-
-
Lys-Met(sulfone)-Tyr-Arg
-
shows 25fold selectivity for plasmin over plasma kallikrein
mAb413
-
antibody of A2 subunit, that blocks plasmin-catalyzed factor VIII heavy chain cleavage at Arg336 and Arg372, but not at Arg740. This antibody does not affect plasmin-catalyzed cleavage of the light chain
-
MG-132
-
prevents facilitation of degradation of Bim(EL) by plasmin in hepatocytes from mice pretreated with cycloheximide
MgCl2
-
0.01 M and above
N-(trans-4-aminomethylcyclohexanecarbonyl)-Tyr(O-2-bromobenzyloxycarbonyl)-octylamide
-
potent and selective inhibitor for plasmin, IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00023 mM, IC50 in reaction with fibrin is 0.0008 mM
N-oleoyl heparin
-
noncompetitive inhibition
-
N-[(1S)-5-amino-1-cyanopentyl]-3-([3-[1-(4-fluorobenzyl)-1H-indol-3-yl]propanoyl]amino)-4-(pyridin-4-ylmethoxy)benzamide
-
molecular modeling
N-[(1S)-5-amino-1-cyanopentyl]-3-[(naphthalen-1-ylacetyl)amino]-4-(pyridin-4-ylmethoxy)benzamide
-
-
N-[(1S)-5-amino-1-cyanopentyl]-3-[(naphthalen-2-ylacetyl)amino]-4-(pyridin-4-ylmethoxy)benzamide
-
-
N-[(1S)-5-amino-1-cyanopentyl]-3-[[(4-fluorophenyl)acetyl]amino]-4-(pyridin-4-ylmethoxy)benzamide
-
-
N-[(1S)-5-amino-1-cyanopentyl]-3-[[3-(1H-indol-3-yl)propanoyl]amino]-4-(pyridin-4-ylmethoxy)benzamide
-
-
N-[(1S)-5-amino-1-cyanopentyl]-4-(pyridin-4-ylmethoxy)benzamide
-
-
Nalpha-[[trans-4-(aminomethyl)cyclohexyl]carbonyl]-N-hexyl-O-(pyridin-4-ylmethyl)-L-tyrosinamide
-
binding mode
natural aprotinin
-
-
-
octasodium [(ethane-1,2-diyl)bis(oxy)[4-oxo-3,7-bis(sulfonatooxy)-4H-1-benzopyran-5,2-diyl]benzene-4,1,2-triyl] tetrasulfate
octasodium [(propane-1,3-diyl)bis(oxy)[4-oxo-3,7-bis(sulfonatooxy)-4H-1-benzopyran-5,2-diyl]benzene-1,2,4-triyl] tetrasulfate
-
about 30% residual activity at 0.4 mM
oleic acid
-
59% inhibition of pro-matrix metalloproteinase-3 activation at 0.05 mM
Pancreatic trypsin inhibitor
-
-
-
PD98059
-
MEK inhibitor, completely abolishes plasmin-induced phosphorylation of ERK1/2 at 0.05 mM
pefabloc
-
-
Pentamidine
-
competitive inhibition
pentasodium (2R)-2-[3,4-bis(sulfonatooxy)phenyl]-3,4-dihydro-2H-1-benzopyran-3,6,7-triyl trisulfate
-
about 32% residual activity at 0.4 mM
pentasodium 2-[3,4-bis(sulfonatooxy)phenyl]-4-oxo-5-[[1-(10-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]decyl)-1H-1,2,3-triazol-4-yl]methoxy]-4H-1-benzopyran-3,7-diyl disulfate
-
about 5% residual activity at 0.4 mM
pentasodium 2-[3-[2,5-bis(sulfonatooxy)phenyl]propanoyl]-5,8-bis(sulfonatooxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxylate
-
about 73% residual activity at 0.4 mM
pentasodium 2-[3-[2,5-bis(sulfonatooxy)phenyl]propanoyl]-6,7-bis(sulfonatooxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxylate
-
about 60% residual activity at 0.4 mM
pentasodium 2-[4-[2,5-bis(sulfonatooxy)phenyl]butanoyl]-5,8-bis(sulfonatooxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxylate
-
about 78% residual activity at 0.4 mM
pentasodium 2-[4-[2,5-bis(sulfonatooxy)phenyl]butanoyl]-6,7-bis(sulfonatooxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxylate
-
about 80% residual activity at 0.4 mM
pentasodium 2-[[2,5-bis(sulfonatooxy)phenyl]acetyl]-6,7-bis(sulfonatooxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxylate
-
about 75% residual activity at 0.4 mM
pentasopentasodium 2-[[2,5-bis(sulfonatooxy)phenyl]acetyl]-6,7-bis(sulfonatooxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxylatedium 2-[[2,5-bis(sulfonatooxy)phenyl]acetyl]-6,7-bis(sulfonatooxy)-1,2,3,4-tetrahydroisoquinoline-3-carboxylate
-
about 70% residual activity at 0.4 mM
peptide GHRPYam
-
delays appearance of plasmin activity
peroxynitrite
-
50% inhibition at 280 microM and an enzyme concentration of 10 microM
Phe-Lys-benzylamide
-
inhibition of fibrinolytic activity, no inhibition of amidolytic activity
plasminogen activator inhibitor I
-
inhibits plasminogen activation to plasmin by urokinase-type plasminogen activator
-
plasminogen activator inhibitor II
-
inhibits plasminogen activation to plasmin by urokinase-type plasminogen activator
-
PSI-112
-
-
R484A mutant of A2
-
subunit of factor VIII, possessing ca. 250fold reduced affinity for plasmin, weakly inhibits factor VIIIa inactivation by ca. 20%
-
recombinant aprotinin
-
-
-
RG1192
-
dextran containing carboxymethylsulfate as well as benzylamide groups. Lysine-binding site domain of plasmin is the RG1192 binding site. In addition RG1192 blocks the generation of plasmin from Glu-plasminogen and inhibits the plasmin-mediated proteolysis of fibronectin and laminin
-
RG1503
-
-
-
SB203580
-
inhibits plasmin-induced TNF-alpha release by 75% and IL-6 release by 79%
sodium 2,6-diformyl-4-(4-oxo-3,4-dihydroquinazolin-2-yl)phenyl sulfate
-
about 93% residual activity at 0.4 mM
sodium 3-(3-[[1-(4-[2-[3-(acetyloxy)phenyl]-4-oxoquinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]-4-oxo-3,4-dihydroquinazolin-2-yl)phenyl sulfate
-
about 55% residual activity at 0.4 mM
Soybean trypsin inhibitor
-
-
-
streptokinase
-
-
-
sucrose octasulfate
-
about 99% residual activity at 0.4 mM
sulfated polyvinylalcohol-acrylate copolymers
-
both the amidolytic and fibrinolytic activities are inhibited
-
tert-butyl 3-(3-[[5-[[(1S)-5-amino-1-cyanopentyl]carbamoyl]-2-(pyridin-4-ylmethoxy)phenyl]amino]-3-oxopropyl)-1H-indole-1-carboxylate
-
-
tetrasodium 2-[2,4-bis(sulfonatooxy)phenyl]-5-hydroxy-4-oxo-4H-chromene-3,7-diyl disulfate
-
about 45% residual activity at 0.4 mM
tetrasodium 2-[2-[6,7-bis(sulfonatooxy)-3,4-dihydroisoquinolin-2(1H)-yl]-2-oxoethyl]-1,4-phenylene disulfate
-
about 60% residual activity at 0.4 mM
tetrasodium 2-[3,4-bis(sulfonatooxy)phenyl]-4-oxo-4H-chromene-3,7-diyl disulfate
-
about 99% residual activity at 0.4 mM
tetrasodium 2-[4-[5,6-bis(sulfonatooxy)-3,4-dihydroisoquinolin-2(1H)-yl]-4-oxobutyl]-1,4-phenylene disulfate
-
about 48% residual activity at 0.4 mM
tetrasodium 4-[5-hydroxy-4-oxo-3,7-bis(sulfonatooxy)-4H-chromen-2-yl]benzene-1,2-diyl disulfate
-
about 93% residual activity at 0.4 mM
tetrasodium 5-methoxy-2-[3-[[1-(4-[2-[3-methoxy-4-(sulfonatooxy)phenyl]-4-oxoquinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methoxy]-4-(sulfonatooxy)phenyl]-4-oxo-4H-1-benzopyran-3,7-diyl disulfate
tetrasodium 5-methoxy-4-oxo-2-[3-[[1-(4-[4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methoxy]-4-(sulfonatooxy)phenyl]-4H-1-benzopyran-3,7-diyl disulfate
-
about 20% residual activity at 0.4 mM
textilinin-1
-
textilinin-1 is a Kunitz-type serine protease inhibitor isolated from the venom of the Australian common brown snake, Pseudonaja textilis. This molecule binds to and blocks the activity plasmin
-
Tranexamic acid
trans-4-aminomethylcyclohexanecarbonyl-L-(O-picolyl)tyrosine-N-octylamide
-
-
trans-parinaric acid
-
60% inhibition of pro-matrix metalloproteinase-3 activation at 0.05 mM
trisodium 2-[(1E)-3-[2,4-bis(sulfonatooxy)phenyl]-3-oxoprop-1-en-1-yl]phenyl sulfate
-
about 42% residual activity at 0.4 mM
trisodium 4-oxo-2-[3-(sulfonatooxy)phenyl]-4H-chromene-3,7-diyl disulfate
-
about 82% residual activity at 0.4 mM
trisodium 4-[(1E)-3-[2,4-bis(sulfonatooxy)phenyl]-3-oxoprop-1-en-1-yl]phenyl sulfate
-
about 58% residual activity at 0.4 mM
trisodium 4-[(1E)-3-[2,5-bis(sulfonatooxy)phenyl]-3-oxoprop-1-en-1-yl]-2-methoxyphenyl sulfate
-
about 90% residual activity at 0.4 mM
trisodium 4-[(1E)-3-[2,5-bis(sulfonatooxy)phenyl]-3-oxoprop-1-en-1-yl]phenyl sulfate
-
about 51% residual activity at 0.4 mM
trisodium 5-(4-oxo-3-[4-[4-([4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]butyl]-3,4-dihydroquinazolin-2-yl)-1,3-phenylene disulfate
-
about 45% residual activity at 0.4 mM
VFK-CMK
-
-
[4-[(N-[[trans-4-(aminomethyl)cyclohexyl]carbonyl]-L-phenylalanyl)amino]phenyl]acetic acid
-
binding mode
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tissue plasminogen activator
-
-
urokinase plasminogen activator1
-
-
urokinase-type plasminogen activator
converts plasminogen bound to a plasminogen receptor into plasmin
-
Aprotinin
-
augments binding of hepatocytes from mice to immobilized plasmin
Efb protein
-
plasminogen bound to Efb protein is converted to plasmin
-
Factor IXa
-
regulates plasmin-catalyzed factor VIIIa inactivation
-
fragment X
-
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
-
high molecular weight urokinase-type plasminogen activator
-
induces a significant increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes
-
low molecular weight urokinase-type plasminogen activator
-
induces a significant increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes
-
Sbi protein
-
plasminogen bound to Sbi protein is converted to plasmin
-
tissue plasminogen activator
-
-
-
urokinase plasminogen activator
-
-
-
urokinase-type plasminogen activator
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
AIYRSR
-
pH 8.0
0.0135 - 0.083
benzyloxycarbonyl-Lys-p-nitrophenyl ester
0.004
CIYRSR
-
pH 8.0
0.02
D-Ile-Phe-Lys
-
pH and temperature not specified in the publication
0.138 - 0.325
D-Val-L-Leu-L-Lys-4-nitroanilide
0.21 - 1.26
D-Val-Leu-Lys-p-nitroanilide
0.03
fibrinogen
-
-
-
0.012
GIVRSR
-
pH 8.0
0.002 - 0.0058
GIYRSR
0.0047
GPGRVV
-
pH 8.0
0.00076
hemofiltrate CC chemokine 1
-
-
-
5.1
KKSPGRVVGGSVAH
-
pH 8.0
0.33
L-Ile-Phe-Lys
-
pH and temperature not specified in the publication
1.6
LGGSAMSRMSSLE
-
pH 8.0
2.4
LGGSGANFRGKLE
-
pH 8.0
0.42
LGGSGAVYKAGLE
-
pH 8.0
1.85
LGGSGIGRSRSLE
-
pH 8.0
0.1
LGGSGIYRSRSLE
-
pH 8.0
3.7
LGGSGIYRSVSLE
-
pH 8.0
0.47
LGGSGIYRVRSLE
-
pH 8.0
1.7
LGGSGPYRSRSLE
-
pH 8.0
2.9
LGGSGTQRRLRLE
-
pH 8.0
0.21
LGGSGYKIGGSLE
-
pH 8.0
0.75
LGGSIRYKGKSLE
-
pH 8.0
6.8
LGGSSIYRSRSLE
-
pH 8.0
0.021
p-tosyl-Arg methyl ester
-
-
0.04 - 0.07
Spectrozyme PL
-
at pH 7.4 and 37°C
0.036
SPGRVV
-
pH 8.0
0.005
thrombin-activatable fibrinolysis inhibitor
-
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.036
AIYRSR
-
pH 8.0
2.1 - 22.3
benzyloxycarbonyl-Lys-p-nitrophenyl ester
2.7
CIYRSR
-
pH 8.0
12.6 - 12.97
D-Val-L-Leu-L-Lys-4-nitroanilide
14.5 - 25.7
D-Val-Leu-Lys-p-nitroanilide
0.039
GIVRSR
-
pH 8.0
0.6 - 1.5
GIYRSR
0.0016
GPGRVV
-
pH 8.0
6
hemofiltrate CC chemokine 1
-
-
-
0.0086
KKSPGRVVGGSVAH
-
pH 8.0
3.2
LGGSAMSRMSSLE
-
pH 8.0
68
LGGSGANFRGKLE
-
pH 8.0
40
LGGSGAVYKAGLE
-
pH 8.0
53
LGGSGIGRSRSLE
-
pH 8.0
120
LGGSGIYRSRSLE
-
pH 8.0
39
LGGSGIYRSVSLE
-
pH 8.0
16
LGGSGIYRVRSLE
-
pH 8.0
92
LGGSGPYRSRSLE
-
pH 8.0
12
LGGSGTQRRLRLE
-
pH 8.0
12
LGGSGYKIGGSLE
-
pH 8.0
44
LGGSIRYKGKSLE
-
pH 8.0
35
LGGSSIYRSRSLE
-
pH 8.0
0.039
SPGRVV
-
pH 8.0
0.00042
thrombin-activatable fibrinolysis inhibitor
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000038
Aedes aegypti trypsin inhibitor
pH and temperature not specified in the publication
-
0.000081
amyloid precursor-like protein 2
pH and temperature not specified in the publication
-
0.00000018
Aprotinin
pH and temperature not specified in the publication
0.00000156
bdellin
pH and temperature not specified in the publication
-
0.002
bikazin salivary inhibitor
pH and temperature not specified in the publication
-
0.0001
bikunin
pH and temperature not specified in the publication
-
0.000127
chicken liver trypsin inhibitor
pH and temperature not specified in the publication
-
0.0000022
CU-2010
pH and temperature not specified in the publication
-
0.00057
D-Ile-Phe-Lys-CH2Cl
pH and temperature not specified in the publication
0.000000087
DX-1000
pH and temperature not specified in the publication
-
0.0000011
infestin
pH and temperature not specified in the publication
-
0.0000009
KD1-L17R
pH and temperature not specified in the publication
-
0.0000031
KM(O2)YR-H
pH and temperature not specified in the publication
0.00000104
Kunitz-type inhibitor 2
pH and temperature not specified in the publication
-
0.00000032
Leucaena-type trypsin inhibitor
pH and temperature not specified in the publication
-
0.000042
nexin 2
pH and temperature not specified in the publication
-
0.00033
ONO-3307
pH and temperature not specified in the publication
0.00000049
plasminostreptin
pH and temperature not specified in the publication
-
0.000055
TdPI tryptase inhibitor
pH and temperature not specified in the publication
-
0.0000035
textilinin-1
pH and temperature not specified in the publication
-
0.000026
tissue factor pathway inhibitor-1
pH and temperature not specified in the publication
-
0.00001
tissue factor pathway inhibitor-2
pH and temperature not specified in the publication
-
0.051 - 0.061
4-aminobenzamidine
1.074 - 1.408
4-aminomethylbenzamidine
0.292 - 0.301
4-carboxybenzamidine
0.0057
479-504 peptide of factor VIII
-
-
-
0.0103
484-509 peptide of factor VIII
-
-
-
0.0628
489-514 peptide of factor VIII
-
-
-
0.0068 - 0.0113
6-aminohexanoic acid
0.032 - 0.161
benzamidine
0.0038
fibrinogen
-
-
-
0.0095
fragment X
-
-
-
0.0000227
human aprotinin analogue
-
compared with recombinant-aprotinin, the Ki of the human aprotinin analogue is found to increase by about 2.6fold, suggesting that the substitution of Arg17-Ile18 with Lys17-Met18 in aprotinin somehow impair its interaction with plasmin
-
0.000027
LEKTI
-
-
0.0000031
Lys-Met(sulfone)-Tyr-Arg
-
pH 8.0, 22°C
0.0000075
natural aprotinin
-
-
-
0.0022 - 0.004
Pentamidine
0.0000086
recombinant aprotinin
-
-
-
0.000028
RG1192
-
pH 7.4, 37°C
-
0.00011
RG1503
-
pH 7.4, 37°C
-
0.0000035
textilinin-1
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
D-Ile-Phe-Lys
Homo sapiens
pH and temperature not specified in the publication
0.33
L-Ile-Phe-Lys
Homo sapiens
pH and temperature not specified in the publication
0.63
PKSI-527
Homo sapiens
pH and temperature not specified in the publication
0.00054
Tra-Tyr(O-Pic)-CONH-(C6H6)-(CH2)4-CH3
Homo sapiens
pH and temperature not specified in the publication
0.0017
Tra-Tyr(O-Pic)-CONH-(C6H6)-CH2-CH3
Homo sapiens
pH and temperature not specified in the publication
0.0019
Tra-Tyr(O-Pic)-CONH-(CH2)2-CH(CH3)-CH3
Homo sapiens
pH and temperature not specified in the publication
0.0055
Tra-Tyr(O-Pic)-CONH-(CH2)7-COOH
Homo sapiens
pH and temperature not specified in the publication
0.0038
Tra-Tyr(O-Pic)-CONH-(CH2)7-NH2
Homo sapiens
pH and temperature not specified in the publication
0.00053
YO-2
Homo sapiens
pH and temperature not specified in the publication
0.63
(4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-phenyl-propionylamino]-phenyl)-acetic acid
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.63 mM
0.075
(E)-5,5'-(but-2-ene-1,4-diylbis(oxy))bis(2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4Hchromen-4-one
Homo sapiens
-
at pH 7.4 and 37°C
0.024
2-(3-[3-[(6-amino-hexyl)-(2-benzyloxycarbonylamino-3-phenyl-propionyl)-amino]-2-oxo-cyclohexyl]-propionylamino)-3-(1H-indol-3-yl)-propionic acid methyl ester
Homo sapiens
-
IC50: 0.024 mM
0.0042
2-[(4-Aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionic acid pyridin-2-ylmethyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0042 mM
0.02
2-[3-(3-[(6-amino-hexyl)-[2-benzyloxycarbonylamino-3-(1H-indol-3-yl)-propionyl]-amino]-2-oxo-cyclohexyl)-propionylamino]-3-(1H-indol-3-yl)-propionic acid methyl ester
Homo sapiens
-
IC50: 0.02 mM
0.056
3-(8-(4-((2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4-oxo-4H-chromen-5-yloxy)methyl)-1H-1,2,3-triazol-1-yl)heptyl)-2-(4-O-sulfonato-phenyl)quinazolin-4(3H)-one
Homo sapiens
-
at pH 7.4 and 37°C
0.045
3-(8-(4-((2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4-oxo-4H-chromen-5-yloxy)methyl)-1H-1,2,3-triazol-1-yl)octyl)-2-(4-O-sulfonato-phenyl)quinazolin-4(3H)-one
Homo sapiens
-
at pH 7.4 and 37°C
0.0039
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid heptyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.024 mM, IC50 in reaction with fibrin is 0.0039 mM
0.0043
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid hexyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.018 mM, IC50 in reaction with fibrin is 0.0043 mM
0.0061
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid methyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0009 mM, IC50 in reaction with fibrin is 0.0061 mM
0.005
4-({2-(6-amino-hexanoylamino)-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid octyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is above 0.1 mM, IC50 in reaction with fibrin is 0.005 mM
0.00042
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid heptyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0014 mM, IC50 in reaction with fibrin is 0.00042 mM
0.0004
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid hexyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0015 mM, IC50 in reaction with fibrin is 0.0004 mM
0.00078
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid methyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.001 mM, IC50 in reaction with fibrin is 0.00078 mM
0.00056
4-({2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-3-[4-(2-bromo-benzyloxycarbonyloxy)-phenyl]-propionylamino}-methyl)-cyclohexanecarboxylic acid octyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0025 mM, IC50 in reaction with fibrin is 0.00056 mM
0.076
5,5'-(butane-1,4-diylbis(oxy))bis(2-(3,4-O,O-disulfonato-phenyl)-3,7-O,O-disulfonato-4H-chromen-4-one
Homo sapiens
-
at pH 7.4 and 37°C
0.000151
Ah-plasmin
Homo sapiens
-
-
-
0.0012
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-(1,1-dimethyl-propylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0062 mM, IC50 in reaction with fibrin is 0.0012 mM
0.0033
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-heptylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.011 mM, IC50 in reaction with fibrin is 0.0033 mM
0.0027
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-hexylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.013 mM, IC50 in reaction with fibrin is 0.0027 mM
0.0013
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-nonylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0083 mM, IC50 in reaction with fibrin is 0.0013 mM
0.0018
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-octylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.007 mM, IC50 in reaction with fibrin is 0.0018 mM
0.0013
Carbonic acid 4-[(S)-2-(6-amino-hexanoylamino)-2-pentylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.01 mM, IC50 in reaction with fibrin is 0.0013 mM
0.019
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(1,1-dimethyl-propylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.085 mM, IC50 in reaction with fibrin is 0.019 mM
0.0023
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(4-butyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.009 mM, IC50 in reaction with fibrin is 0.0023 mM
0.0035
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(4-hexyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.006 mM, IC50 in reaction with fibrin is 0.0035 mM
0.0047
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-(4-pentyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.009 mM, IC50 in reaction with fibrin is 0.0047 mM
0.002
carbonic acid 4-[2-(6-amino-hexanoylamino)-2-propylcarbamoyl-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0092 mM, IC50 in reaction with fibrin is 0.002 mM
0.0017
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(1,1-dimethyl-propylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.013 mM, IC50 in reaction with fibrin is 0.0017 mM
0.000056
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(3-methyl-butylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00046 mM, IC50 in reaction with fibrin is 0.000056 mM
0.00009
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-butyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00079 mM, IC50 in reaction with fibrin is 0.00009 mM
0.000098
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-ethyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00063 mM, IC50 in reaction with fibrin is 0.000098 mM
0.00024
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-hexyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00049 mM, IC50 in reaction with fibrin is 0.00024 mM
0.00007
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(4-pentyl-phenylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00057 mM, IC50 in reaction with fibrin is 0.00007 mM
0.00017
carbonic acid 4-[2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-(pyridin-4-ylcarbamoyl)-ethyl]-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00098 mM, IC50 in reaction with fibrin is 0.00017 mM
0.00043
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-heptylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0011 mM, IC50 in reaction with fibrin is 0.00043 mM
0.00038
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-hexylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0012 mM, IC50 in reaction with fibrin is 0.00038 mM
0.0001
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-nonylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
potent and selective inhibitor for plasmin, IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0005 mM, IC50 in reaction with fibrin is 0.0001 mM
0.0001
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-pentylcarbamoyl-ethyl}-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.011 mM, IC50 in reaction with fibrin is 0.0001 mM
0.00052
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-[(pyridin-2-ylmethyl)-carbamoyl]-ethyl}-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0015 mM, IC50 in reaction with fibrin is 0.00052 mM
0.0014
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-[(pyridin-4-ylmethyl)-carbamoyl]-ethyl}-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is0.0053 mM, IC50 in reaction with fibrin is 0.0014 mM
0.0003
carbonic acid 4-{2-[(4-aminomethyl-cyclohexanecarbonyl)-amino]-2-[benzyl-carbamoyl]-ethyl}-phenyl ester 2-bromo-benzyl ester
Homo sapiens
-
IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.0011 mM, IC50 in reaction with fibrin is 0.0003 mM
0.078
D-Ile-Phe-Lys-CN
Homo sapiens
-
pH and temperature not specified in the publication
0.29
D-Ile-Phe-Lys-NH2
Homo sapiens
-
pH and temperature not specified in the publication
0.4
disodium 3-(4-oxo-3-[[1-(4-[4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
1
disodium 3-(acetyloxy)-5-(4-oxo-3-[4-[4-([4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]butyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.4
disodium 3-[4-oxo-3-[3-[4-([4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]propyl]quinazolin-2(4H)-yl]phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.125 - 0.239
disodium 4-(4-oxo-3-[5-[5-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]pentyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
0.098
disodium 4-(4-oxo-3-[[1-(10-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]decyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.089 - 0.621
disodium 4-(4-oxo-3-[[1-(12-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]dodecyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
0.161
disodium 4-(4-oxo-3-[[1-(7-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]heptyl)-1H-1,2,3-triazol-4-yl]methyl]-3,4-dihydroquinazolin-2-yl)phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.111
disodium 4-[4-oxo-3-[11-[4-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]undecyl]quinazolin-2(4H)-yl]phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.183
disodium 4-[4-oxo-3-[8-[4-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]octyl]quinazolin-2(4H)-yl]phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.137
disodium 4-[4-oxo-3-[9-[4-([4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]nonyl]quinazolin-2(4H)-yl]phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.0008
N-(trans-4-aminomethylcyclohexanecarbonyl)-Tyr(O-2-bromobenzyloxycarbonyl)-octylamide
Homo sapiens
-
potent and selective inhibitor for plasmin, IC50 in reaction with D-Val-Leu-Lys-4-nitroanilide is 0.00023 mM, IC50 in reaction with fibrin is 0.0008 mM
0.000016
N-oleoyl heparin
Homo sapiens
-
at pH 7.4 and 37°C
-
0.14
N-[(1S)-5-amino-1-cyanopentyl]-3-([3-[1-(4-fluorobenzyl)-1H-indol-3-yl]propanoyl]amino)-4-(pyridin-4-ylmethoxy)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.57
N-[(1S)-5-amino-1-cyanopentyl]-3-[(naphthalen-1-ylacetyl)amino]-4-(pyridin-4-ylmethoxy)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.22
N-[(1S)-5-amino-1-cyanopentyl]-3-[(naphthalen-2-ylacetyl)amino]-4-(pyridin-4-ylmethoxy)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.59
N-[(1S)-5-amino-1-cyanopentyl]-3-[[(4-fluorophenyl)acetyl]amino]-4-(pyridin-4-ylmethoxy)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.37
N-[(1S)-5-amino-1-cyanopentyl]-3-[[3-(1H-indol-3-yl)propanoyl]amino]-4-(pyridin-4-ylmethoxy)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.24
N-[(1S)-5-amino-1-cyanopentyl]-4-(pyridin-4-ylmethoxy)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00053
Nalpha-[[trans-4-(aminomethyl)cyclohexyl]carbonyl]-N-hexyl-O-(pyridin-4-ylmethyl)-L-tyrosinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.185 - 2.83
octasodium [(ethane-1,2-diyl)bis(oxy)[4-oxo-3,7-bis(sulfonatooxy)-4H-1-benzopyran-5,2-diyl]benzene-4,1,2-triyl] tetrasulfate
0.4
octasodium [(propane-1,3-diyl)bis(oxy)[4-oxo-3,7-bis(sulfonatooxy)-4H-1-benzopyran-5,2-diyl]benzene-1,2,4-triyl] tetrasulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.13
pentasodium 2-[3,4-bis(sulfonatooxy)phenyl]-4-oxo-5-[[1-(10-[4-oxo-2-[4-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]decyl)-1H-1,2,3-triazol-4-yl]methoxy]-4H-1-benzopyran-3,7-diyl disulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.00037 - 0.00175
PSI-112
0.642
sodium 3-(3-[[1-(4-[2-[3-(acetyloxy)phenyl]-4-oxoquinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]-4-oxo-3,4-dihydroquinazolin-2-yl)phenyl sulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.22
tert-butyl 3-(3-[[5-[[(1S)-5-amino-1-cyanopentyl]carbamoyl]-2-(pyridin-4-ylmethoxy)phenyl]amino]-3-oxopropyl)-1H-indole-1-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.128 - 0.22
tetrasodium 5-methoxy-2-[3-[[1-(4-[2-[3-methoxy-4-(sulfonatooxy)phenyl]-4-oxoquinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methoxy]-4-(sulfonatooxy)phenyl]-4-oxo-4H-1-benzopyran-3,7-diyl disulfate
0.149
tetrasodium 5-methoxy-4-oxo-2-[3-[[1-(4-[4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]butyl)-1H-1,2,3-triazol-4-yl]methoxy]-4-(sulfonatooxy)phenyl]-4H-1-benzopyran-3,7-diyl disulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.08679
Tranexamic acid
Homo sapiens
-
wild type enzyme, pH and temperature not specified in the publication
0.00017 - 0.00115
trans-4-aminomethylcyclohexanecarbonyl-L-(O-picolyl)tyrosine-N-octylamide
0.084
trisodium 5-(4-oxo-3-[4-[4-([4-oxo-2-[3-(sulfonatooxy)phenyl]quinazolin-3(4H)-yl]methyl)-1H-1,2,3-triazol-1-yl]butyl]-3,4-dihydroquinazolin-2-yl)-1,3-phenylene disulfate
Homo sapiens
-
at pH 7.4 and 37°C
0.65
[4-[(N-[[trans-4-(aminomethyl)cyclohexyl]carbonyl]-L-phenylalanyl)amino]phenyl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
electrochemical assay and properties of plasmin adsorbed onto a carbon paste electrode
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.4 - 8
-
assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
-
pH 7.5: about 40% of maximal activity, pH 9.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 37
-
assay at 37°C or at room temperature
37
-
assay at
37 - 45
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
in blood as zymogen plasminogen
Manually annotated by BRENDA team
-
plasmin is generated by the plasmin/u-PA system on surfaces of A-549 alveolar lining cells
Manually annotated by BRENDA team
-
vessel wall
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
originally isolated from a cirrhotic liver
Manually annotated by BRENDA team
-
plasmin induces scattering of HT-29-M6 cells in the presence of 12-myristate 13-acetate
Manually annotated by BRENDA team
-
plasmin induces a concentration-dependent transient elevation in the cytosolic Ca2+ concentrations
Manually annotated by BRENDA team
-
plasmin triggers expression and release of proinflammatory cytokines such as TNF-alpha and IL-6 in human monocyte-derived macrophages with a somewhat lower potency than the standard stimulus lipopolysaccharide. Plasmin-induced activation of JAK1, p38, ERK1/2, and NF-kappaB is indispensable for the cytokine expression
Manually annotated by BRENDA team
-
plasmin is the principal protease in milk
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
vitreous from patients with proliferative vitreoretinopathy have readily detectable levels of plasmin. Presence of plasmin is not unique to patients with proliferative vitreoretinopathy, but also present in a patient undergoing retinal surgery unrelated to proliferative vitreoretinopathy
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
plasminogen is a major surface-bound protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
Defects or mutations in the PLG gene are the cause of thrombophilia, a form of recurrent thrombosis, and type I plasminogen deficiency. Ligneous conjunctivitis is usually the most common and initial form of type I plasminogen deficiency and is a rare form of chronic conjunctivitis characterized by chronic tearing and redness of the conjunctivae
metabolism
besides the main physiological inhibitor alpha2-antiplasmin, the plasmin-antiplasmin system is also regulated by the general protease inhibitor alpha2-macroglobulin, a member of the protease inhibitor I39 family. The activity of the plasminogen activators is primarily regulated by the plasminogen activator inhibitors 1 and 2, members of the serine protease inhibitor superfamily
physiological function
primary function of plasmin is the cleavage of insoluble fibrin polymers at specific sites resulting in soluble fragments. In addition, plasmin acts as a proteolytic factor in many other physiological processes such as mediation of cell migration by degrading the extracellular matrix, wound healing, tissue remodelling, angiogenesis, embryogenesis, and pathogen and tumour cell invasion. The plasmin-antiplasmin system plays a key role in blood coagulation and fibrinolysis. Plasmin and alpha2-antiplasmin are primarily responsible for a controlled and regulated dissolution of the fibrin polymers into soluble fragments
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLMN_HUMAN
810
0
90569
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
88432
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
90000
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
25700
-
x * 48800, A-chain, + x * 25700, B-chain, equilibrium sedimentation after cleavage of a single disulfide bond in Lys-plasminogen
48800
-
x * 48800, A-chain, + x * 25700, B-chain, equilibrium sedimentation after cleavage of a single disulfide bond in Lys-plasminogen
75400
-
equilibrium sedimentation
83000
-
x * 83000, SDS-PAGE
85000
-
-
91000
-
x * 91000, plasminogen, SDS-PAGE
92000
-
x * 92000, plasminogen, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination
monomer
additional information
plasminogen is a single-chain, multidomain glycoprotein, and is composed of an N-terminal peptide, five triple-loop structures stabilized by three intrachain disulfide bridges called kringles, and the trypsin-like serine protease part carrying the catalytic triad His603, Asp646, and Ser741. Primary structure of human plasminogen, overview. The three-dimensional structural model of human plasminogen based on known and overlapping 3-D structures of plasminogen fragments exhibits a spiral shape
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the human plasminogen is partially N-glycosylated at Asn289 and O-glycosylated at Ser249 and Thr346 giving rise to plasminogen variants I (Asn289, Thr346) and II (only Thr346)
phosphoprotein
plasminogen is partially phosphorylated at Ser578
proteolytic modification
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. Pgn is activated by the two main physiological plasminogen activators to the active, two-chain plasmin molecule held together by two interchain disulfide bridges, Cys548-Cys666, Cys558-Cys566, by cleavage of the Arg561-Val562 peptide bond and the release of the 77-residue N-terminal peptide. Two N-terminally different forms of plasminogen exist, Glu-Pgn and Lys-Pgn. Lys-Pgn is formed by cleavage of the Lys77-Lys78 peptide bond in Glu-Pgn, releasing the N-terminal peptide
proteolytic modification
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of plasmin complexed with streptokinase
-
in complex with trans-4-aminomethylcyclohexanecarbonyl-L-tyrosine-n-octylamide, using 10% (w/v) polyethylene glycol 6000, 4% (v/v) 2-methyl-2,4-pentanediol, and 0.1 M MES (pH 5.0) at 20°C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F587A
-
binding site mutant
F587A/K607A
-
binding site mutant
K607A
-
binding site mutant
P611I
-
mutant enzyme has no amidolytic activity with D-Val-Leu-Lys-p-nitroanilide
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
very stable below
95552
7
-
unstable in absence of glycerol
95552
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
-
rapid destruction or inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing results in loss of activity
-
plasmin-staphylokinase complex is more stable than plasmin(ogen)-streptokinase complex
-
reduction with 2-mercaptoethanol in 8 M urea at pH 9.0, complete loss of activity by cleavage of a single disulfide bond
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C to -30°C, pH 9.0, Tris-Lys-NaCl-EDTA buffer containing 25% glycerol, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
mutant enzyme P611I expressed in recombinant baculovirus-infected Spodoptera frugiperda cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
plasminogen levels ae significantly higher in Cardiac neonatal lupus compared with non-cardiac neonatal lupus children
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
electrochemical assay of plasmin activity based on a ferrocenyl peptide substrate having a plasmin-specific substrate sequence, Lys-thr-Phe-Lys, and immobilized on a gold electrode. Detection limit for plasmin is around 50 ng/ml or 0.15 mU/ml. Ratio of kcat/Km values is 0.063 microM/s
degradation
-
cleavage at Arg336 is a central mechanism of plasmin-catalyzed factor VIII inactivation. Cleavages at Arg336 and Lys36 are selectively regulated by the A2 and A3-C1-C2 domains, respectively, interacting with plasmin
medicine
pharmacology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robbins, K.; Summaria, L.; Wohl, R.C.
Human plasmin
Methods Enzymol.
80
379-387
1981
Homo sapiens
Manually annotated by BRENDA team
Robbins, K.C.; Summaria, L.
Plasminogen and plasmin
Methods Enzymol.
45
257-273
1976
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Castellino, F.J.
A unique enzyme - protein substrate modifier reaction: plasmin/streptokinase interaction
Trends Biochem. Sci.
4
1-5
1979
Homo sapiens
-
Manually annotated by BRENDA team
Robbins, K.C.; Summaria, L.
Human plasminogen and plasmin
Methods Enzymol.
19
184-199
1970
Homo sapiens
-
Manually annotated by BRENDA team
Greig, H.B.W.; Cornelius, E.M.
Protamine-heparin complex as substrate for plasmin
Biochim. Biophys. Acta
67
658-668
1963
Homo sapiens
Manually annotated by BRENDA team
Kolev, K.; Lerant, I.; Tenekejiev, K.; Machovich, R.
Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors
J. Biol. Chem.
269
17030-17034
1994
Homo sapiens
Manually annotated by BRENDA team
Wang, X.; Lin, X.; Loy, J.A.; Tang, J.; Zhang, X.C.
Crystal structure of the catalytic structure of the catalytic domain of human plasmin complexed with streptokinase
Science
281
1662-1665
1998
Homo sapiens
Manually annotated by BRENDA team
Higazi, A.A.R.; Mayer, M.
Inhibition of plasmin by fibrinogen
Biochem. J.
269
299-302
1990
Homo sapiens
Manually annotated by BRENDA team
Mhashilkar, A.M.; Viswanatha, T.; Chibber, B.A.K.; Castellino, F.J.
Breaching the conformational integrity of the catalytic triad of the serine protease plasmin: localized disruption of a side chain of His-603 strongly inhibits the amidolytic activity of human plasmin
Proc. Natl. Acad. Sci. USA
90
5374-5377
1993
Homo sapiens
Manually annotated by BRENDA team
Sazonova, I.Y.; Aisina, R.B.; Muhametova, L.I.; Varfolomeyev, S.D.
Kinetic properties of the activator complexes plasmin-staphylokinase and plasmin(ogen)-streptokinase in vitro
Biochemistry
64
66-74
1999
Homo sapiens
Manually annotated by BRENDA team
Rickli, E.E.; Otavsky, W.I.
A new method of isolation and some properties of the heavy chain of human plasmin
Eur. J. Biochem.
59
441-447
1975
Homo sapiens
Manually annotated by BRENDA team
Lijnen, H.R.; van Hoef, B.; Smith, R.A.G.; Collen, D.
Functional properties of p-anisoylated plasmin-staphylokinase complex
Thromb. Haemost.
70
326-331
1993
Homo sapiens
Manually annotated by BRENDA team
Longchamp, S.; Randriamahazaka, H.N.; Nigretto, J.M.
Electrochemical assay and properties of plasmin adsorbed onto a carbon paste electrode
J. Electroanal. Chem.
412
31-37
1996
Homo sapiens
-
Manually annotated by BRENDA team
Fitzpatrick, S.L.; Kassam, G.; Choi, K.S.; Kang, H.M.; Fogg, D.K.; Waisman, D.M.
Regulation of plasmin activity by annexin II tetramer
Biochemistry
39
1021-1028
2000
Homo sapiens
Manually annotated by BRENDA team
Mitsudo, K.; Jayakumar, A.; Henderson, Y.; Frederick, M.J.; Kang, Y.; Wang, M.; El-Naggar, A.K.; Clayman, G.L.
Inhibition of serine proteinases plasmin, trypsin, subtilisin A, cathepsin G, and elastase by LEKTI: a kinetic analysis
Biochemistry
42
3874-3881
2003
Homo sapiens
Manually annotated by BRENDA team
Brown, E.W.; Ravindran, S.; Patston, P.A.
The reaction between plasmin and C1-inhibitor results in plasmin inhibition by the serpin mechanism
Blood Coagul. Fibrinolysis
13
711-714
2002
Homo sapiens
Manually annotated by BRENDA team
Ries, M.; Zenker, M.
Influence of soluble fibrin on reaction kinetics of plasmin type 1 and type 2 with alpha2-antiplasmin
Blood Coagul. Fibrinolysis
14
203-209
2003
Homo sapiens
Manually annotated by BRENDA team
Syrovets, T.; Simmet, T.
Novel aspects and new roles for the serine protease plasmin
Cell. Mol. Life Sci.
61
873-885
2004
Homo sapiens
Manually annotated by BRENDA team
Hervio, L.S.; Coombs, G.S.; Bergstrom, R.C.; Trivedi, K.; Corey, D.R.; Madison, E.L.
Negative selectivity and the evolution of protease cascades: the specificity of plasmin for peptide and protein substrates
Chem. Biol.
7
443-453
2000
Homo sapiens
Manually annotated by BRENDA team
Okada, Y.; Matsumoto, Y.; Tsuda, Y.; Tada, M.; Wanaka, K.; Hijikata-Okunomiya, A.; Okamoto, S.
Development of plasmin-selective inhibitors and studies of their structure-activity relationship
Chem. Pharm. Bull.
48
184-193
2000
Homo sapiens
Manually annotated by BRENDA team
Lauer, G.; Sollberg, S.; Cole, M.; Krieg, T.; Eming, S.A.
Generation of a novel proteolysis resistant vascular endothelial growth factor165 variant by a site-directed mutation at the plasmin sensitive cleavage site
FEBS Lett.
531
309-313
2002
Homo sapiens
Manually annotated by BRENDA team
Zhang, W.Y.; Ishii, I.; Kruth, H.S.
Plasmin-mediated macrophage reversal of low density lipoprotein aggregation
J. Biol. Chem.
275
33176-33183
2000
Homo sapiens
Manually annotated by BRENDA team
Jiang, Q.; Taupenot, L.; Mahata, S.K.; Mahata, M.; O'Connor, D.T.; Miles, L.A.; Parmer, R.J.
Proteolytic cleavage of chromogranin A (CgA) by plasmin. Selective liberation of a specific bioactive CgA fragment that regulates catecholamine release
J. Biol. Chem.
276
25022-25029
2001
Homo sapiens
Manually annotated by BRENDA team
Vakili, J.; Standker, L.; Detheux, M.; Vassart, G.; Forssmann, W.G.; Parmentier, M.
Urokinase plasminogen activator and plasmin efficiently convert hemofiltrate CC chemokine 1 into its active [9-74] processed variant
J. Immunol.
167
3406-3413
2001
Homo sapiens
Manually annotated by BRENDA team
Tucker, H.M.; Kihiko, M.; Caldwell, J.N.; Wright, S.; Kawarabayashi, T.; Price, D.; Walker, D.; Scheff, S.; McGillis, J.P.; Rydel, R.E.; Estus, S.
The plasmin system is induced by and degrades amyloid-beta aggregates
J. Neurosci.
20
3937-3946
2000
Homo sapiens
Manually annotated by BRENDA team
Abato, P.; Yuen, C.M.; Cubanski, J.Y.; Seto, C.T.
Inhibitors of plasmin that extend into both the S and S' binding sites: cooperative interactions between S1 and S2
J. Org. Chem.
67
1184-1191
2002
Homo sapiens
Manually annotated by BRENDA team
Exley, C.; Korchazhkina, O.V.
Plasmin cleaves Abeta42 in vitro and prevents its aggregation into beta-pleated sheet structures
Neuroreport
12
2967-2970
2001
Homo sapiens
Manually annotated by BRENDA team
Midura-Nowaczek, K.; Roszkowska-Jakimiec, W.; Lepietuszko, I.; Bruzgo, I.
Synthesis of benzylamides of dipeptides as potential inhibitors of plasmin
Pharmazie
58
687-689
2003
Homo sapiens
Manually annotated by BRENDA team
Hseu, Y.C.; Chang, W.C.; Yang, H.L.
Inhibition of human plasmin activity using humic acids with arsenic
Sci. Total Environ.
273
93-99
2001
Homo sapiens
Manually annotated by BRENDA team
Yuasa, H.; Tanaka, H.; Hayashi, T.; Wakita, T.; Nakamura, H.; Nishioka, J.; Kawarada, Y.; Suzuki, K.
Bovine protein C inhibitor has a unique reactive site and can transiently inhibit plasmin
Thromb. Haemost.
83
262-267
2000
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Vrs, G.; Kolev, K.; Csomor, K.; Machovich, R.
Inhibition of plasmin activity by sulfated polyvinylalcohol-acrylate copolymers
Thromb. Res.
100
353-361
2000
Homo sapiens
Manually annotated by BRENDA team
Quagraine, M.O.; Tan, F.; Tamei, H.; Erdoes, E.G.; Skidgel, R.A.
Plasmin alters the activity and quaternary structure of human plasma carboxypeptidase N
Biochem. J.
388
81-91
2005
Homo sapiens
Manually annotated by BRENDA team
Huet, E.; Cauchard, J.H.; Berton, A.; Robinet, A.; Decarme, M.; Hornebeck, W.; Bellon, G.
Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5
Biochem. Pharmacol.
67
643-654
2004
Homo sapiens
Manually annotated by BRENDA team
Crawley, J.T.; Lam, J.K.; Rance, J.B.; Mollica, L.R.; ODonnell, J.S.; Lane, D.A.
Proteolytic inactivation of ADAMTS13 by thrombin and plasmin
Blood
105
1085-1093
2005
Homo sapiens
Manually annotated by BRENDA team
Diaz, V.M.; Hurtado, M.; Kort, E.J.; Resnati, M.; Blasi, F.; Thomson, T.; Paciucci, R.
Requirement of the enzymatic and signaling activities of plasmin for phorbol-ester-induced scattering of colon cancer cells
Exp. Cell Res.
312
2203-2213
2006
Homo sapiens
Manually annotated by BRENDA team
Bergmann, S.; Rohde, M.; Chhatwal, G.S.; Hammerschmidt, S.
Characterization of plasmin(ogen) binding to Streptococcus pneumoniae
Indian J. Med. Res.
119 Suppl
29-32
2004
Homo sapiens
Manually annotated by BRENDA team
Schneider, M.; Brufatto, N.; Neill, E.; Nesheim, M.
Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin
J. Biol. Chem.
279
13340-13345
2004
Homo sapiens
Manually annotated by BRENDA team
Drinane, M.C.; Sherman, J.A.; Hall, A.E.; Simons, M.; Mulligan-Kehoe, M.J.
Plasminogen and plasmin activity in patients with coronary artery disease
J. Thromb. Haemost.
4
1288-1295
2006
Homo sapiens
Manually annotated by BRENDA team
Nowak, P.; Kolodziejczyk, J.; Wachowicz, B.
Peroxynitrite and fibrinolytic system: the effect of peroxynitrite on plasmin activity
Mol. Cell. Biochem.
267
141-146
2004
Homo sapiens
Manually annotated by BRENDA team
Li, Q.; Laumonnier, Y.; Syrovets, T.; Simmet, T.
Plasmin triggers cytokine induction in human monocyte-derived macrophages
Arterioscler. Thromb. Vasc. Biol.
27
1383-1389
2007
Homo sapiens
Manually annotated by BRENDA team
Fujiyoshi, T.; Hirano, K.; Hirano, M.; Nishimura, J.; Takahashi, S.; Kanaide, H.
Plasmin Induces Endothelium-Dependent Nitric Oxide-Mediated Relaxation in the Porcine Coronary Artery
Arterioscler. Thromb. Vasc. Biol.
27
949-954
2007
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Doolittle, R.F.; Pandi, L.
Binding of synthetic B knobs to fibrinogen changes the character of fibrin and inhibits its ability to activate tissue plasminogen activator and its destruction by plasmin
Biochemistry
45
2657-2667
2006
Homo sapiens
Manually annotated by BRENDA team
Schaefer, A.V.; Leslie, B.A.; Rischke, J.A.; Stafford, A.R.; Fredenburgh, J.C.; Weitz, J.I.
Incorporation of fragment X into fibrin clots renders them more susceptible to lysis by plasmin
Biochemistry
45
4257-4265
2006
Homo sapiens
Manually annotated by BRENDA team
Kawao, N.; Okada, K.; Kawata, S.; Okamoto, C.; Tsuritani, M.; Ueshima, S.; Matsuo, O.
Plasmin decreases the BH3-only protein BimEL via the ERK1/2 signaling pathway in hepatocytes
Biochim. Biophys. Acta
1773
718-727
2007
Homo sapiens
Manually annotated by BRENDA team
Nogami, K.; Nishiya, K.; Saenko, E.L.; Takeyama, M.; Tanaka, I.; Yoshioka, A.; Shima, M.
Identification of a plasmin-interactive site within the A2 domain of the factor VIII heavy chain
Biochim. Biophys. Acta
1784
753-763
2008
Homo sapiens
Manually annotated by BRENDA team
Nielsen, V.G.
Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions
Blood Coagul. Fibrinolysis
18
647-656
2007
Homo sapiens
Manually annotated by BRENDA team
Erbas, H.; Erten, O.; Irfanoglu, M.E.
Breast cyst fluid plasmin activity and its effect on TGF-beta2 activation
Cancer Invest.
26
22-27
2008
Homo sapiens
Manually annotated by BRENDA team
Biswas, N.; Vaingankar, S.M.; Mahata, M.; Das, M.; Gayen, J.R.; Taupenot, L.; Torpey, J.W.; OConnor, D.T.; Mahata, S.K.
Proteolytic cleavage of human chromogranin a containing naturally occurring catestatin variants: differential processing at catestatin region by plasmin
Endocrinology
149
749-757
2008
Homo sapiens
Manually annotated by BRENDA team
Gray, K.; Ellis, V.
Activation of pro-BDNF by the pericellular serine protease plasmin
FEBS Lett.
582
907-910
2008
Homo sapiens
Manually annotated by BRENDA team
Lei, H.; Velez, G.; Hovland, P.; Hirose, T.; Kazlauskas, A.
Plasmin is the major protease responsible for processing PDGF-C in the vitreous of patients with proliferative vitreoretinopathy
Invest. Ophthalmol. Vis. Sci.
49
42-48
2008
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Nogami, K.; Shima, M.; Matsumoto, T.; Nishiya, K.; Tanaka, I.; Yoshioka, A.
Mechanisms of plasmin-catalyzed inactivation of factor VIII: a crucial role for proteolytic cleavage at Arg336 responsible for plasmin-catalyzed factor VIII inactivation
J. Biol. Chem.
282
5287-5295
2007
Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Zhou, Z.H.; Bugge, T.H.; Wahl, L.M.
Urokinase-type plasminogen activator stimulation of monocyte matrix metalloproteinase-1 production is mediated by plasmin-dependent signaling through annexin A2 and inhibited by inactive plasmin
J. Immunol.
179
3297-3304
2007
Homo sapiens
Manually annotated by BRENDA team
Ishida, T.; Tsukada, H.; Hasegawa, T.; Yoshizawa, H.; Gejyo, F.
Matrix metalloproteinase-1 activation via plasmin generated on alveolar epithelial cell surfaces
Lung
184
15-19
2006
Homo sapiens
Manually annotated by BRENDA team
Paczek, L.; Michalska, W.; Bartlomiejczyk, I.
Trypsin, elastase, plasmin and MMP-9 activity in the serum during the human ageing process
Age Ageing
37
318-323
2008
Homo sapiens
Manually annotated by BRENDA team
Ohtsuka, K.; Maekawa, I.; Waki, M.; Takenaka, S.
Electrochemical assay of plasmin activity and its kinetic analysis
Anal. Biochem.
385
293-299
2009
Homo sapiens
Manually annotated by BRENDA team
Brazon, J.; DSuze, G.; DErrico, M.L.; Arocha-Pinango, C.L.; Guerrero, B.
Discreplasminin, a plasmin inhibitor isolated from Tityus discrepans scorpion venom
Arch. Toxicol.
83
669-678
2008
Homo sapiens
Manually annotated by BRENDA team
Guo, Y.; Li, J.; Hagstroem, E.; Ny, T.
Protective effects of plasmin(ogen) in a mouse model of Staphylococcus aureus-induced arthritis
Arthritis Rheum.
58
764-772
2008
Homo sapiens
Manually annotated by BRENDA team
Kamio, N.; Hashizume, H.; Nakao, S.; Matsushima, K.; Sugiya, H.
Plasmin is involved in inflammation via protease-activated receptor-1 activation in human dental pulp
Biochem. Pharmacol.
75
1974-1980
2008
Homo sapiens
Manually annotated by BRENDA team
Potier, A.; Lavigne, C.; Chappard, D.; Verret, J.L.; Chevailler, A.; Nicolie, B.; Drouet, M.
Cutaneous manifestations in Hymenoptera and Diptera anaphylaxis: relationship with basal serum tryptase
Clin. Exp. Allergy
39
717-725
2009
Homo sapiens
Manually annotated by BRENDA team
Heide, R.; van Doorn, K.; Mulder, P.G.; van Toorenenbergen, A.W.; Beishuizen, A.; de Groot, H.; Tank, B.; Oranje, A.P.
Serum tryptase and SCORMA (SCORing MAstocytosis) Index as disease severity parameters in childhood and adult cutaneous mastocytosis
Clin. Exp. Dermatol.
34
462-468
2008
Homo sapiens
Manually annotated by BRENDA team
Hermel, M.; Prenner, J.; Alabdulrazzak, M.; Dailey, W.; Hartzer, M.
Effect of intravitreal plasmin on vitreous removal through a 25-gauge cutting system in the rabbit in vivo
Graefes Arch. Clin. Exp. Ophthalmol.
247
331-334
2009
Homo sapiens
Manually annotated by BRENDA team
Marcinkiewicz, M.; Gordon, P.V.
A role for plasmin in platelet aggregation: differential regulation of IGF release from IGF-IGFBP complexes?
Growth Horm. IGF Res.
18
325-334
2008
Homo sapiens
Manually annotated by BRENDA team
Attali, C.; Durmort, C.; Vernet, T.; Di Guilmi, A.M.
The interaction of Streptococcus pneumoniae with plasmin mediates transmigration across endothelial and epithelial monolayers by intercellular junction cleavage
Infect. Immun.
76
5350-5356
2008
Homo sapiens
Manually annotated by BRENDA team
Bonadonna, P.; Perbellini, O.; Passalacqua, G.; Caruso, B.; Colarossi, S.; Dal Fior, D.; Castellani, L.; Bonetto, C.; Frattini, F.; Dama, A.; Martinelli, G.; Chilosi, M.; Senna, G.; Pizzolo, G.; Zanotti, R.
Clonal mast cell disorders in patients with systemic reactions to Hymenoptera stings and increased serum tryptase levels
J. Allergy Clin. Immunol.
123
680-686
2009
Homo sapiens
Manually annotated by BRENDA team
Yuan, H.; Vance, K.M.; Junge, C.E.; Geballe, M.T.; Snyder, J.P.; Hepler, J.R.; Yepes, M.; Low, C.M.; Traynelis, S.F.
The serine protease plasmin cleaves the amino-terminal domain of the NR2A subunit to relieve zinc inhibition of the N-methyl-D-aspartate receptors
J. Biol. Chem.
284
12862-12873
2009
Homo sapiens
Manually annotated by BRENDA team
Kothari, H.; Kaur, G.; Sahoo, S.; Idell, S.; Rao, L.V.; Pendurthi, U.
Plasmin enhances cell surface tissue factor activity in mesothelial and endothelial cells
J. Thromb. Haemost.
7
121-131
2009
Homo sapiens
Manually annotated by BRENDA team
Miah, M.F.; Boffa, M.B.
Functional analysis of mutant variants of thrombin-activatable fibrinolysis inhibitor resistant to activation by thrombin or plasmin
J. Thromb. Haemost.
7
665-672
2009
Homo sapiens
Manually annotated by BRENDA team
Hunt, J.A.; Petteway, S.R.; Scuderi, P.; Novokhatny, V.
Simplified recombinant plasmin: production and functional comparison of a novel thrombolytic molecule with plasma-derived plasmin
Thromb. Haemost.
100
413-419
2008
Homo sapiens
Manually annotated by BRENDA team
Novokhatny, V.
Structure and activity of plasmin and other direct thrombolytic agents
Thromb. Res.
122
S3-S8
2008
Homo sapiens
Manually annotated by BRENDA team
Nakagawa, H.; Yasuda, S.; Matsuura, E.; Kobayashi, K.; Ieko, M.; Kataoka, H.; Horita, T.; Atsumi, T.; Koike, T.
Nicked beta2-glycoprotein I binds angiostatin 4.5 (plasminogen kringle 1-5) and attenuates its antiangiogenic property
Blood
114
2553-2559
2009
Homo sapiens
Manually annotated by BRENDA team
Gerber, S.S.; Lejon, S.; Locher, M.; Schaller, J.
The human alpha(2)-plasmin inhibitor: functional characterization of the unique plasmin(ogen)-binding region
Cell. Mol. Life Sci.
67
1505-1518
2010
Homo sapiens
Manually annotated by BRENDA team
Millers, E.K.; Trabi, M.; Masci, P.P.; Lavin, M.F.; de Jersey, J.; Guddat, L.W.
Crystal structure of textilinin-1, a Kunitz-type serine protease inhibitor from the venom of the Australian common brown snake (Pseudonaja textilis)
FEBS J.
276
3163-3175
2009
Homo sapiens
Manually annotated by BRENDA team
Koizumi, M.; Momoeda, M.; Hiroi, H.; Nakazawa, F.; Nakae, H.; Ohno, T.; Yano, T.; Taketani, Y.
Inhibition of proteases involved in embryo implantation by cholesterol sulfate
Hum. Reprod.
25
192-197
2010
Homo sapiens
Manually annotated by BRENDA team
Sun, Z.; Lu, W.; Jiang, A.; Chen, J.; Tang, F.; Liu, J.N.
Expression, purification and characterization of aprotinin and a human analogue of aprotinin
Protein Expr. Purif.
65
238-243
2009
Homo sapiens
Manually annotated by BRENDA team
Christensen, B.; Schack, L.; Klaening, E.; Sorensen, E.S.
Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D
J. Biol. Chem.
285
7929-7937
2010
Homo sapiens
Manually annotated by BRENDA team
Li, X.; Syrovets, T.; Genze, F.; Pitterle, K.; Oberhuber, A.; Orend, K.H.; Simmet, T.
Plasmin triggers chemotaxis of monocyte-derived dendritic cells through an Akt2-dependent pathway and promotes a T-helper type-1 response
Arterioscler. Thromb. Vasc. Biol.
30
582-590
2010
Homo sapiens
Manually annotated by BRENDA team
Doeuvre, L.; Plawinski, L.; Goux, D.; Vivien, D.; Angles-Cano, E.
Plasmin on adherent cells: from microvesiculation to apoptosis
Biochem. J.
432
365-373
2010
Homo sapiens
Manually annotated by BRENDA team
Swedberg, J.E.; Harris, J.M.
Plasmin substrate binding site cooperativity guides the design of potent peptide aldehyde inhibitors
Biochemistry
50
8454-8462
2011
Homo sapiens
Manually annotated by BRENDA team
Teno, N.; Gohda, K.; Wanaka, K.; Sueda, T.; Tsuda, Y.
Identification of novel plasmin inhibitors possessing nitrile moiety as warhead
Bioorg. Med. Chem. Lett.
21
6305-6309
2011
Homo sapiens
Manually annotated by BRENDA team
Venkatraman, L.; Li, H.; Dewey Jr., C.; White, J.; Bhowmick, S.; Yu, H.; Tucker-Kellogg, L.
Steady states and dynamics of urokinase-mediated plasmin activation in silico and in vitro
Biophys. J.
101
1825-1834
2011
Homo sapiens
Manually annotated by BRENDA team
Arkebauer, M.; Kanaparthy, S.; Malayaman, S.; Vosseller, K.; Nielsen, V.
Carbon monoxide and nitric oxide modulate alpha2-antiplasmin and plasmin activity: role of heme
Blood Coagul. Fibrinolysis
22
712-719
2011
Homo sapiens
Manually annotated by BRENDA team
Schaller, J.; Gerber, S.S.
The plasmin-antiplasmin system: structural and functional aspects
Cell. Mol. Life Sci.
68
785-801
2011
Homo sapiens (P00747)
Manually annotated by BRENDA team
Dahiya, M.; Singh, S.; Rajamohan, G.; Sethi, D.; Ashish, D.; Dikshit, K.L.
Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: function of His43 and Tyr44
FEBS Lett.
585
1814-1820
2011
Homo sapiens
Manually annotated by BRENDA team
Okunishi, K.; Sisson, T.H.; Huang, S.K.; Hogaboam, C.M.; Simon, R.H.; Peters-Golden, M.
Plasmin overcomes resistance to prostaglandin E2 in fibrotic lung fibroblasts by reorganizing protein kinase A signaling
J. Biol. Chem.
286
32231-32243
2011
Homo sapiens, Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
Gohda, K.; Teno, N.; Wanaka, K.; Tsuda, Y.
Predicting subsite interactions of plasmin with substrates and inhibitors through computational docking analysis
J. Enzyme Inhib. Med. Chem.
27
:571-577
2011
Homo sapiens
Manually annotated by BRENDA team
Feys, H.B.; Vandeputte, N.; Palla, R.; Peyvandi, F.; Peerlinck, K.; Deckmyn, H.; Lijnen, H.R.; Vanhoorelbeke, K.
Inactivation of ADAMTS13 by plasmin as a potential cause of thrombotic thrombocytopenic purpura
J. Thromb. Haemost.
8
2053-2062
2010
Homo sapiens
Manually annotated by BRENDA team
Martinez-Rizo, A.; Bueno-Topete, M.; Gonzalez-Cuevas, J.; Armendariz-Borunda, J.
Plasmin plays a key role in the regulation of profibrogenic molecules in hepatic stellate cells
Liver Int.
30
298-310
2010
Homo sapiens
Manually annotated by BRENDA team
Li, Q.; Ke, F.; Zhang, W.; Shen, X.; Xu, Q.; Wang, H.; Yu, X.Z.; Leng, Q.; Wang, H.
Plasmin plays an essential role in amplification of psoriasiform skin inflammation in mice
PLoS ONE
6
e16483
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chung, M.C.; Tonry, J.H.; Narayanan, A.; Manes, N.P.; Mackie, R.S.; Gutting, B.; Mukherjee, D.V.; Popova, T.G.; Kashanchi, F.; Bailey, C.L.; Popov, S.G.
Bacillus anthracis interacts with plasmin(ogen) to evade C3b-dependent innate immunity
PLoS ONE
6
e18119
2011
Homo sapiens
Manually annotated by BRENDA team
Alves, N.J.; Kline, J.A.
Comparative study on the inhibition of plasmin and delta-plasmin viabenzamidine derivatives
Biochem. Biophys. Res. Commun.
457
358-362
2015
Homo sapiens
Manually annotated by BRENDA team
Varju, I.; Tenekedjiev, K.; Keresztes, Z.; Pap, A.E.; Szabo, L.; Thelwell, C.; Longstaff, C.; Machovich, R.; Kolev, K.
Fractal kinetic behavior of plasmin on the surface of fibrin meshwork
Biochemistry
53
6348-6356
2014
Homo sapiens
Manually annotated by BRENDA team
Swedberg, J.E.; Harris, J.M.
Natural and engineered plasmin inhibitors: applications and design strategies
ChemBioChem
13
336-348
2012
Homo sapiens (P00747), Homo sapiens
Manually annotated by BRENDA team
Buhl, K.; Friis, U.; Svenningsen, P.; Gulaveerasingam, A.; Ovesen, P.; Frederiksen-Moller, B.; Jespersen, B.; Bistrup, C.; Jensen, B.
Urinary plasmin activates collecting duct ENaC current in preeclampsia
Hypertension
60
1346-1351
2012
Homo sapiens
Manually annotated by BRENDA team
Gohda, K.; Teno, N.; Wanaka, K.; Tsuda, Y.
Predicting subsite interactions of plasmin with substrates and inhibitors through computational docking analysis
J. Enzyme Inhib. Med. Chem.
27
571-577
2012
Homo sapiens (P00747)
Manually annotated by BRENDA team
Foley, J.H.; Peterson, E.A.; Lei, V.; Wan, L.W.; Krisinger, M.J.; Conway, E.M.
Interplay between fibrinolysis and complement: plasmin cleavage of iC3b modulates immune responses
J. Thromb. Haemost.
13
610-618
2015
Homo sapiens
Manually annotated by BRENDA team
Koch, T.K.; Reuter, M.; Barthel, D.; Boehm, S.; van den Elsen, J.; Kraiczy, P.; Zipfel, P.F.; Skerka, C.
Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b
PLoS ONE
7
e47638
2012
Homo sapiens
Manually annotated by BRENDA team
Briassouli, P.; Halushka, M.K.; Reed, J.H.; Molad, Y.; Fox-Talbot, K.; Buyon, L.; Guzman, E.; Ludomirsky, A.; Clancy, R.M.; Buyon, J.P.
A central role of plasmin in cardiac injury initiated by fetal exposure to maternal anti-Ro autoantibodies
Rheumatology
52
1448-1453
2013
Homo sapiens
Manually annotated by BRENDA team
Brophy, T.M.; Ward, S.E.; McGimsey, T.R.; Schneppenheim, S.; Drakeford, C.; OSullivan, J.M.; Chion, A.; Budde, U.; ODonnell, J.S.
Plasmin cleaves von Willebrand factor at K1491-R1492 in the A1-A2 linker region in a shear- and glycan-dependent manner in vitro
Arterioscler. Thromb. Vasc. Biol.
37
845-855
2017
Homo sapiens
Manually annotated by BRENDA team
Yusova, E.
Plasmin enzymatic activity in the presence of actin
Biopolym. Cell
31
345-350
2015
Homo sapiens
-
Manually annotated by BRENDA team
Law, R.H.P.; Wu, G.; Leung, E.W.W.; Hidaka, K.; Quek, A.J.; Caradoc-Davies, T.T.; Jeevarajah, D.; Conroy, P.J.; Kirby, N.M.; Norton, R.S.; Tsuda, Y.; Whisstock, J.C.
X-ray crystal structure of plasmin with tranexamic acid-derived active site inhibitors
Blood Adv.
1
766-771
2017
Homo sapiens
Manually annotated by BRENDA team
Wise, S.G.; Michael, P.L.; Waterhouse, A.; Santos, M.; Filipe, E.; Hung, J.; Kondyurin, A.; Bilek, M.M.; Ng, M.K.
Immobilization of bioactive plasmin reduces the thrombogenicity of metal surfaces
Colloids Surf. B Biointerfaces
136
944-954
2015
Homo sapiens
Manually annotated by BRENDA team
Castiblanco-Valencia, M.M.; Fraga, T.R.; Pagotto, A.H.; Serrano, S.M.; Abreu, P.A.; Barbosa, A.S.; Isaac, L.
Plasmin cleaves fibrinogen and the human complement proteins C3b and C5 in the presence of Leptospira interrogans proteins A new role of LigA and LigB in invasion and complement immune evasion
Immunobiology
221
679-689
2016
Homo sapiens
Manually annotated by BRENDA team
Al-Horani, R.; Karuturi, R.; White, D.; Desai, U.
Plasmin regulation through allosteric, sulfated, small molecules
Molecules
20
608-624
2015
Homo sapiens
Manually annotated by BRENDA team