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

plasmin bound to pneumococci is able to cleave recombinant vascular endothelial cadherin

698248

carboxypeptidase N + H2O

plasmin cleaves the 83 kDa subunit of carboxypeptidase N between Arg457 and Ser458 and after prolonged incubation between Arg218 and Arg219. The small 55 kDa is cleaved to a 48 kDa product. The cleavage enhances the activity of carboxypeptidase N to 150% of the uncleaved enzyme

667503

casein + H2O

95552, 95553

chromogenic substrate S-2551 + H2O

650727

chromogranin A + H2O

catestatin + ?

chromogranin A-wild-type, chromogranin A-Gly364Ser and chromogranin A-Arg374Gln completely digested with plasmin at 0.0004 mM

686420

chromogranin A + H2O

hCgA-(360-373) + ?

CIYRSR + H2O

CIYR + Ser-Arg

complement component C3 + H2O

complement component C3a + ?

complement component C3a + H2O

complement component C3b + H2O

complement component C5 + H2O

cleavage by plasmin produces bands of approximately 41000 Da and 30000-28000 Da

D-Ile-Phe-Lys + H2O

D-Nle-hexa-hydrotyrosyl-Lys-4-nitroanilide + H2O

D-Nle-hexa-hydrotyrosyl-Lys + 4-nitroaniline

653974

D-Nle-hexahydrotyrosyl-Lys-4-nitroanilide + H2O

D-Nle-hexahydrotyrosyl-Lys + 4-nitroaniline

649912

D-Val-L-Leu-L-Lys-4-nitroanilide + H2O

D-Val-L-Leu-L-Lys + 4-nitroaniline

D-Val-Leu-Lys-4-nitroanilide + H2O

D-Val-Leu-Lys + 4-nitroaniline

D-Val-Leu-Lys-p-nitroanilide + H2O

685071

D-Val-Leu-Lys-p-nitroanilide + H2O

D-Val-Leu-Lys + p-nitroaniline

D-valyl-L-leucyl-L-lysine-4-nitroanilide + H2O

epithelial sodium channel + H2O

epithelial sodium channel gamma subunit + ?

ERK1/2

triggers activation

factor VIII + H2O

Fibrin + H2O

fibrin + H2O

soluble fibrin fragments

Fibrinogen + H2O

fibrinogen + H2O

fragment X

fragment X generated by limited plasmin digestion of fibrinogen

GIVRSR + H2O

GIVR + Ser-Arg

GIYRSR + H2O

GIYR + Ser-Arg

Glu-plasminogen + H2O

angiostatin 4.5 (AS4.5)

AS4.5 is prepared from Glu-plasminogen by plasmin digestion

GPGRVV + H2O

GPGR + Val-Val

H-D-norleucyl-hexahydrotyrosol-lysine-para nitroanilide diacetate + H2O

H-D-Val-Leu-Lys-p-nitroaniline dihydrochloride + H2O

hemofiltrate CC chemokine 1 + H2O

[9-74] processed variant of hemofiltrate CC chemokine 1 + ?

IkappaBalpha

plasmin induces phosphorylation of IkappaBalpha, targeting the inhibitor to proteosomal degradation, consequently allowing nuclear translocation of NF-kappaB

inactive complement component C3b + H2O

plasmin degrades inactive complement component C3b through cleavage at R945 generating C3dg- and C3c-like species

732405

insulin + H2O

cleavage of the Arg25-Gly and Lys29-Ala peptide bonds of the beta-chain of oxidized bovine insulin

JAK1

triggers tyrosine phosphorylation

KKSPGRVVGGSVAH + H2O

KKSPGR + VVGGSVAH

KQWK-4-nitroanilide + H2O

KQWK + 4-nitroaniline

peptide substrate

KTFK-4-nitroanilide + H2O

KTFK + 4-nitroaniline

peptide substrate

L-Ile-Phe-Lys + H2O

LGGSAMSRMSSLE + H2O

LGGSAMSR + MSSLE

LGGSGANFRGKLE + H2O

LGGSGANFR + GKLE

LGGSGAVYKAGLE + H2O

LGGSGAVYK + AGLE

LGGSGIGRSRSLE + H2O

LGGSGIGR + SRSLE

LGGSGIYRSRSLE + H2O

LGGSGIYR + SRSLE

LGGSGIYRSVSLE + H2O

LGGSGIYR + SVSLE

LGGSGIYRVRSLE + H2O

LGGSGIYR + VRSLE

LGGSGPYRSRSLE + H2O

LGGSGPYR + SRSLE

LGGSGTQRRLRLE + H2O

LGGSGTQR + RLRLE

LGGSGYKIGGSLE + H2O

LGGSGYK + IGGSLE

LGGSIRYKGKSLE + H2O

LGGSIRYK + GKSLE

LGGSSIYRSRSLE + H2O

LGGSSIYR + SRSLE

MT1-matrix metalloproteinase + H2O

N-methyl-D-aspartate receptor NR2A subunit

plasmin cleaves the native NR2A amino-terminal domain, removing the functional high affinity Zn2+ binding site. Plasmin also cleaves recombinant NR2A amino-terminal domain at lysine 317, thereby producing a 40 kDa fragment, consistent with plasmin-induced NR2A cleavage fragmentsobserved in rat brain preparations. Zn2+ inhibition of agonist-evoked N-methyl-D-aspartate receptor currents of NR1/NR2A-transfected HEK 293 cells and cultured cortical neurons is significantly reduced by plasmin treatment. Mutating the plasmin cleavage site Lys317 on NR2A to alanine blocks plasmins effect on Zn2+ inhibition

698888

osteopontin + H2O

p38 MAPK

triggers phosphorylation

p65

triggeres nuclear translocation

plasminogen + H2O

platelet-derived growth factor-C + H2O

plasmin is the major protease responsible for processing platelet-derived growth factor-C in patients undergoing retinal surgery. Plasmin is vastly more potent (192times faster) than tissue plasminogen activator in processing the substrate

687206

pro-brain-derived neurotrophic factor + H2O

plasmin is a specific and efficient activator of pro-brain-derived neurotrophic factor. The pro-form is rapidly processed to an 18 kDa fragment at a low concentration of plasmin. This C-terminal fragment is equivalent in size to the furin-processed, mature form of wild-type brain-derived neurotrophic factor. The proteolytic cleavage site is Arg125-Val126, within the consensus furin-cleavage motif

686775

pro-matrix metalloproteinase-1 + H2O

active matrix metalloproteinase-1

matrix metalloproteinase-1 activation by the UP A/plasmin system

688780

pro-matrix metalloproteinase-1 + H2O

matrix metalloproteinase-1 + ?

pro-matrix metalloproteinase-10 + H2O

matrix metalloproteinase-10 + ?

pro-matrix metalloproteinase-13 + H2O

matrix metalloproteinase-13 + ?

pro-matrix metalloproteinase-3 + H2O

matrix metalloproteinase-3 + ?

pro-matrix metalloproteinase-9 + H2O

matrix metalloproteinase-9 + ?

protamin-heparin complex + H2O

RQFR-4-nitroanilide + H2O

RQFR + 4-nitroaniline

peptide substrate

RQWK-4-nitroanilide + H2O

RQWK + 4-nitroaniline

peptide substrate

S-2251 + H2O

S-sulfo-fibrinogen + H2O

cleaves only Lys and Arg peptide bonds

Spectrozyme PL + H2O

L-norleucyl-L-hexahydrotyrosyl-L-lysine + 4-nitroaniline

i.e. L-norleucyl-L-hexahydrotyrosyl-L-lysine-4-nitroanilide

SPGRVV + H2O

SPGR + Val-Val

STAT3

phosphorylates on Tyr705 and Ser727. Triggeres activation and nuclear translocation of STAT3

thrombin-activatable fibrinolysis inhibitor + H2O

mutant variants with variants in the amino acids surrounding the scissile R92-A93 bond such as P91S, R92K, and S90P exhibit specific impairment of activation by plasmin

tissue factor pathway inhibitor + H2O

plasmin increases tissue factor activity by inactivating the cell-associated tissue factor pathway inhibitor by a limited proteolysis

699867

Tosyl-Arg methyl ester + H2O

p-tosyl-Arg methyl ester

tosyl-Gly-Pro-Lys-4-nitroanilide + H2O

tosyl-Gly-Pro-Lys + 4-nitroaniline

transforming growth factor beta 2 + H2O

685923

TYK2

triggers tyrosine phosphorylation

vascular endothelial growth factor + H2O

von Willebrand factor + H2O

the enzyme cleaves von Willebrand factor at K1491-R149. Globular von Willebrand factor is resistant to plasmin cleavage under static conditions, but is readily cleaved by plasmin under shear

752616

VQYK-4-nitroanilide + H2O

VQYK + 4-nitroaniline

peptide substrate

VQYR-4-nitroanilide + H2O

VQYR + 4-nitroaniline

peptide substrate

additional information

17 entries

Go to Natural Substrate Search

ADAMTS13 + H2O

inactivation

718043

amyloid-beta + H2O

the plasmin pathway is induced by aggregated amyloid-beta, which can lead to amyloid-beta degradation and inhibition of amyloid-beta actions

652978

beta2-glycoprotein I + H2O

in human plasma beta2-glycoprotein I is proteolytically cleaved by plasmin in its domain V (nicked beta2GPI), resulting in binding to plasminogen

chromogranin A + H2O

hCgA-(360-373) + ?

the product hCgA-(360-373) is a bioactive fragment that inhibits nicotinic-mediated catecholamine release. The plasminogen/plasmin system through its interaction with chromogranin A may play a major role in catecholaminergic function

652141

complement component C3 + H2O

complement component C3a + ?

complement component C3a + H2O

complement component C3b + H2O

complement component C5 + H2O

cleavage by plasmin produces bands of approximately 41000 Da and 30000-28000 Da

epithelial sodium channel + H2O

epithelial sodium channel gamma subunit + ?

731900

Fibrin + H2O

fibrin + H2O

soluble fibrin fragments

Fibrinogen + H2O

the fibrinogen alpha-chain is degraded in low-molecular-mass fragments of approximately 63000-60000 Da

Glu-plasminogen + H2O

angiostatin 4.5 (AS4.5)

AS4.5 is prepared from Glu-plasminogen by plasmin digestion

hemofiltrate CC chemokine 1 + H2O

[9-74] processed variant of hemofiltrate CC chemokine 1 + ?

urokinase plasminogen activator and plasmin efficiently convert hemofiltrate CC chemokine 1 into its active [9-74] processed variant

inactive complement component C3b + H2O

plasmin degrades inactive complement component C3b through cleavage at R945 generating C3dg- and C3c-like species

732405

MT1-matrix metalloproteinase + H2O

N-methyl-D-aspartate receptor NR2A subunit

698888

osteopontin + H2O

osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a substrate for plasmin and cathepsin D

712488

pro-matrix metalloproteinase-1 + H2O

matrix metalloproteinase-1 + ?

pro-matrix metalloproteinase-10 + H2O

matrix metalloproteinase-10 + ?

pro-matrix metalloproteinase-13 + H2O

matrix metalloproteinase-13 + ?

pro-matrix metalloproteinase-3 + H2O

matrix metalloproteinase-3 + ?

pro-matrix metalloproteinase-9 + H2O

matrix metalloproteinase-9 + ?

tissue factor pathway inhibitor + H2O

plasmin increases tissue factor activity by inactivating the cell-associated tissue factor pathway inhibitor by a limited proteolysis

699867

vascular endothelial growth factor + H2O

in non-healing wounds plasmin cleaves and inactivates vascular endothelial growth factor VEGF165

651314

von Willebrand factor + H2O

the enzyme cleaves von Willebrand factor at K1491-R149. Globular von Willebrand factor is resistant to plasmin cleavage under static conditions, but is readily cleaved by plasmin under shear

752616

additional information

7 entries

Go to Inhibitor Search

(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

about 2% residual activity at 0.4 mM

4-(2-aminoethyl)benzenesulfonyl fluoride

695548

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

684784

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-aminohexanoate

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

753021

Aedes aegypti trypsin inhibitor

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-antiplasmin

potent inhibitor

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

708063

aminomethyl cyclohexane carboxylic acid

amyloid precursor-like protein 2

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

649912

antiplasmin

the inhibition of plasmin by antiplasmin can be reduced by high molecular weight fibrin degradation products with carboxy-terminal lysine residues

669210

Aprotinin

5 entries

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

bdellin

benzamidine

competitive inhibition

bikazin salivary inhibitor

bikunin

C1 inhibitor

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

chicken liver trypsin inhibitor

Cholesterol sulfate

reduces plasmin activity in a dose-dependent manner

708672

cis-parinaric acid

more than 60% inhibition of pro-matrix metalloproteinase-3 activation at 0.05 mM

CO elicits hypofibrinolysis by enhancing alpha2-antiplasmin activity and decreasing plasmin activity

CU-2010

potent inhibitpr

D-Ile-Phe-Lys

D-Ile-Phe-Lys-CH2Cl

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

695935

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

about 25% residual activity at 0.4 mM; about 35% residual activity at 0.4 mM

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

about 2% residual activity at 0.4 mM; about 30% residual activity at 0.4 mM; about 40% residual activity at 0.4 mM

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

DX-1000

elaidic acid

60% inhibition of pro-matrix metalloproteinase-3 activation at 0.05 mM

epsilon-aminocaproic acid

inhibits plasmin-induced phosphorylation of ERK1/2; lysine binding sites inhibitor, partially blocks binding of hepatocytes from mice to immobilized plasmin at 10 mM, but not at 0.01 mM

Fibrin

inhibits hydrolysis of D-Val-Leu-Lys-p-nitroanilide

95559

fibrinogen

fragment X

competitive inhibitor of plasmin chromogenic activity

histidine-rich glycoprotein

binds at sites of tissue injury and seems to act as a high-affinity receptor to immobilize plasminogen on cell surfaces

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

653880

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

infestin

KD1-L17R

KM(O2)YR-H

Kunitz-type inhibitor 2

L-Ile-Phe-Lys

L-lysine

LEKTI

potent noncompetitive inhibitor, recombinant LEKTI is purified using a baculovirus/insect cell expression system

650209

Leu-Lys-benzylamide

inhibition of fibrinolytic activity, no inhibition of amidolytic activity

Leucaena-type trypsin inhibitor

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

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

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

about 16% residual activity at 0.4 mM; about 18% residual activity at 0.4 mM; about 65% residual activity at 0.4 mM

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

ONO-3307

i.e. 4-sulfamoyl phenyl-4-guanidinobenzoate methanesulfonate

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

685071

peroxynitrite

50% inhibition at 280 microM and an enzyme concentration of 10 microM

670233

Phe-Lys-benzylamide

inhibition of fibrinolytic activity, no inhibition of amidolytic activity

PKSI-527

plasminogen activator inhibitor I

inhibits plasminogen activation to plasmin by urokinase-type plasminogen activator

717845

plasminogen activator inhibitor II

inhibits plasminogen activation to plasmin by urokinase-type plasminogen activator

717845

plasminogen activator inhibitors 1

plasminogen activator inhibitors 2

plasminostreptin

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

653974

TdPI tryptase inhibitor

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

about 3% residual activity at 0.4 mM; about 7% residual activity at 0.4 mM; about 8% residual activity at 0.4 mM

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

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

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

YO-2

i.e. Tra-Tyr(O-Pic)-CONH-(CH2)7-CH3

[4-[(N-[[trans-4-(aminomethyl)cyclohexyl]carbonyl]-L-phenylalanyl)amino]phenyl]acetic acid

binding mode

additional information

9 entries

Go to Activating Compound Search

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 plasminogen activator1

urokinase-type plasminogen activator

additional information

5 entries

Go to KM Value Search

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

Go to Turnover Number Search

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

hemofiltrate CC chemokine 1

0.0086

KKSPGRVVGGSVAH

pH 8.0

3.2

LGGSAMSRMSSLE

pH 8.0

LGGSGANFRGKLE

pH 8.0

LGGSGAVYKAGLE

pH 8.0

LGGSGIGRSRSLE

pH 8.0

120

LGGSGIYRSRSLE

pH 8.0

LGGSGIYRSVSLE

pH 8.0

LGGSGIYRVRSLE

pH 8.0

LGGSGPYRSRSLE

pH 8.0

LGGSGTQRRLRLE

pH 8.0

LGGSGYKIGGSLE

pH 8.0

LGGSIRYKGKSLE

pH 8.0

LGGSSIYRSRSLE

pH 8.0

0.039

SPGRVV

pH 8.0

0.00042

thrombin-activatable fibrinolysis inhibitor

Go to Ki Value Search

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

0.0000038

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

0.032 - 0.161

benzamidine

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

0.0038

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

0.0000011

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

0.000027

LEKTI

650209

0.00000032

Leucaena-type trypsin inhibitor

pH and temperature not specified in the publication

0.0000031

Lys-Met(sulfone)-Tyr-Arg

pH 8.0, 22°C

0.0000075

natural aprotinin

0.000042

nexin 2

pH and temperature not specified in the publication

0.00033

ONO-3307

pH and temperature not specified in the publication

0.0022 - 0.004

Pentamidine

0.00000049

plasminostreptin

pH and temperature not specified in the publication

0.0000086

recombinant aprotinin

0.000028

RG1192

pH 7.4, 37°C

652048

0.00011

RG1503

pH 7.4, 37°C

652048

0.000055

TdPI tryptase inhibitor

pH and temperature not specified in the publication

0.0000035

textilinin-1

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

Go to IC50 Value Search

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

0.02

D-Ile-Phe-Lys

Homo sapiens

pH and temperature not specified in the publication

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

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

0.33

L-Ile-Phe-Lys

Homo sapiens

pH and temperature not specified in the publication

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

0.63

PKSI-527

Homo sapiens

pH and temperature not specified in the publication

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

0.00054

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

0.08679

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

0.00053

YO-2

Homo sapiens

pH and temperature not specified in the publication

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

Go to Specific Activity Search

additional information

electrochemical assay and properties of plasmin adsorbed onto a carbon paste electrode

95564

Go to pH Optimum Search

7.4

assay at

7.4 - 8

assay at

7.5

assay at

8.5

Go to pH Range Search

7.5 - 9.5

pH 7.5: about 40% of maximal activity, pH 9.5: about 50% of maximal activity

Go to Temperature Optimum Search

22 - 37

assay at 37°C or at room temperature

assay at

37 - 45

Go to Organism Search

11 entries

Go to Source Tissue Search

A-549 cell

plasmin is generated by the plasmin/u-PA system on surfaces of A-549 alveolar lining cells

vessel wall

commercial preparation

endometrial stromal cell

eye

hepatic stellate cell

originally isolated from a cirrhotic liver

718070

HT-29 cell

plasmin induces scattering of HT-29-M6 cells in the presence of 12-myristate 13-acetate

668502

HUVEC cell

plasmin induces a concentration-dependent transient elevation in the cytosolic Ca2+ concentrations

684784

macrophage

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

milk

plasmin is the principal protease in milk

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

687206

additional information

Go to General Information Search

Go to Localization Search

plasminogen is a major surface-bound protein

malfunction

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

12 entries

additional information

5 entries

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

P00747 pBLAST

PLMN_HUMAN

810

90569

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 1)

B2R7F8 pBLAST

B2R7F8_HUMAN

810

90539

TrEMBL

Show Sequence

Secretory Pathway (Reliability: 1)

A0A0F7G8J1 pBLAST

A0A0F7G8J1_HUMAN

809

90628

TrEMBL

Show Sequence

Secretory Pathway (Reliability: 1)

Go to PDB and Structure Links Search

36 entries

Go to Molecular Weight Search

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

88432

x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination

90000

x * 90000, plasminogen, SDS-PAGE, x * 88432, plasminogen, sequence determination

91000

x * 91000, plasminogen, SDS-PAGE

92000

x * 92000, plasminogen, SDS-PAGE

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

Go to Posttranslational Modification Search

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

8 entries

side-chain modification

Go to Crystallization (commentary) Search

crystal structure of plasmin complexed with streptokinase

95558

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

Go to Protein Variants Search

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

95560

additional information

Go to pH Stability Search

very stable below

95552

unstable in absence of glycerol

95552

Go to Temperature Stability Search

rapid destruction or inactivation

Go to General Stability Search

freezing and thawing results in loss of activity

plasmin-staphylokinase complex is more stable than plasmin(ogen)-streptokinase complex

95561

reduction with 2-mercaptoethanol in 8 M urea at pH 9.0, complete loss of activity by cleavage of a single disulfide bond

Go to Storage Stability Search

-20°C to -30°C, pH 9.0, Tris-Lys-NaCl-EDTA buffer containing 25% glycerol, stable

Go to Purification (commentary) Search

affinity chromatography

670233

Go to Cloned (commentary) Search

expression in Escherichia coli

701279

mutant enzyme P611I expressed in recombinant baculovirus-infected Spodoptera frugiperda cells

95560

Go to Expression Search

plasminogen levels ae significantly higher in Cardiac neonatal lupus compared with non-cardiac neonatal lupus children

732904

Go to Application Search

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

695548

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

687666

medicine

17 entries

pharmacology

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95547

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Homo sapiens

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Oryctolagus cuniculus, Homo sapiens

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A unique enzyme - protein substrate modifier reaction: plasmin/streptokinase interaction

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Homo sapiens

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Human plasminogen and plasmin

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Homo sapiens

Greig, H.B.W.; Cornelius, E.M.

Protamine-heparin complex as substrate for plasmin

Biochim. Biophys. Acta

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1963

Homo sapiens

13950275

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Kolev, K.; Lerant, I.; Tenekejiev, K.; Machovich, R.

Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors

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Homo sapiens

7516329

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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

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1998

Homo sapiens

9733510

95559

Higazi, A.A.R.; Mayer, M.

Inhibition of plasmin by fibrinogen

Biochem. J.

269

299-302

1990

Homo sapiens

2143650

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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

5374-5377

1993

Homo sapiens

8506386

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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

66-74

1999

Homo sapiens

9986915

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Rickli, E.E.; Otavsky, W.I.

A new method of isolation and some properties of the heavy chain of human plasmin

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1975

Homo sapiens

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Lijnen, H.R.; van Hoef, B.; Smith, R.A.G.; Collen, D.

Functional properties of p-anisoylated plasmin-staphylokinase complex

Thromb. Haemost.

326-331

1993

Homo sapiens

8236143

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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

649912

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

1021-1028

2000

Homo sapiens

10653646

650209

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

3874-3881

2003

Homo sapiens

12667078

650727

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

711-714

2002

Homo sapiens

12441910

650728

Ries, M.; Zenker, M.

Influence of soluble fibrin on reaction kinetics of plasmin type 1 and type 2 with alpha2-antiplasmin

Blood Coagul. Fibrinolysis

203-209

2003

Homo sapiens

12632033

650808

Syrovets, T.; Simmet, T.

Novel aspects and new roles for the serine protease plasmin

Cell. Mol. Life Sci.

873-885

2004

Homo sapiens

15095009

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.

443-453

2000

Homo sapiens

10873836

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.

184-193

2000

Homo sapiens

10705502

651314

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

12417332

652048

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

10942782

652141

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

11342539

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

11544332

652978

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.

3937-3946

2000

Homo sapiens

10818128

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.

1184-1191

2002

Homo sapiens

11846661

653359

Exley, C.; Korchazhkina, O.V.

Plasmin cleaves Abeta42 in vitro and prevents its aggregation into beta-pleated sheet structures

Neuroreport

2967-2970

2001

Homo sapiens

11588612

Midura-Nowaczek, K.; Roszkowska-Jakimiec, W.; Lepietuszko, I.; Bruzgo, I.

Synthesis of benzylamides of dipeptides as potential inhibitors of plasmin

Pharmazie

687-689

2003

Homo sapiens

14609277

653880

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

11419606

653967

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.

262-267

2000

Bos taurus, Homo sapiens

10739384

653974

V�r�s, G.; Kolev, K.; Csomor, K.; Machovich, R.

Inhibition of plasmin activity by sulfated polyvinylalcohol-acrylate copolymers

Thromb. Res.

100

353-361

2000

Homo sapiens

11113279

667503

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

15617514

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.

643-654

2004

Homo sapiens

14757164

668067

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

15388580

668502

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

16631161

668903

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

15232158

669210

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

14715654

670064

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.

1288-1295

2006

Homo sapiens

16706973

670233

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

15663195

Li, Q.; Laumonnier, Y.; Syrovets, T.; Simmet, T.

Plasmin triggers cytokine induction in human monocyte-derived macrophages

Arterioscler. Thromb. Vasc. Biol.

1383-1389

2007

Homo sapiens

17413040

684784

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.

949-954

2007

Homo sapiens, Sus scrofa

17272753

685071

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

2657-2667

2006

Homo sapiens

16489759

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

4257-4265

2006

Homo sapiens

16566600

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

17482686

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

18329389

685797

Nielsen, V.G.

Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions

Blood Coagul. Fibrinolysis

647-656

2007

Homo sapiens

17890952

685923

Erbas, H.; Erten, O.; Irfanoglu, M.E.

Breast cyst fluid plasmin activity and its effect on TGF-beta2 activation

Cancer Invest.

22-27

2008

Homo sapiens

18181041

686420

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

17991725

686775

Gray, K.; Ellis, V.

Activation of pro-BDNF by the pericellular serine protease plasmin

FEBS Lett.

582

907-910

2008

Homo sapiens

18291105

687206

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.

42-48

2008

Oryctolagus cuniculus, Homo sapiens

18172073

687666

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

17189254

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

17709546

688780

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

16598647

695428

Paczek, L.; Michalska, W.; Bartlomiejczyk, I.

Trypsin, elastase, plasmin and MMP-9 activity in the serum during the human ageing process

Age Ageing

318-323

2008

Homo sapiens

18332058

695548

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

19041631

695935

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.

669-678

2008

Homo sapiens

19015833

695957

Guo, Y.; Li, J.; Hagstroem, E.; Ny, T.

Protective effects of plasmin(ogen) in a mouse model of Staphylococcus aureus-induced arthritis

Arthritis Rheum.

764-772

2008

Homo sapiens

18311818

696130

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.

1974-1980

2008

Homo sapiens

18384756

697405

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

717-725

2009

Homo sapiens

19302252

697407

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.

462-468

2008

Homo sapiens

19077102

698137

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

19034484

698139

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.

325-334

2008

Homo sapiens

18328759

698248

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.

5350-5356

2008

Homo sapiens

18725422

698446

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

19135713

698888

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

19240037

699867

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.

121-131

2009

Homo sapiens

18983492

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.

665-672

2009

Homo sapiens

19335449

701279

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

18766256

701290

Novokhatny, V.

Structure and activity of plasmin and other direct thrombolytic agents

Thromb. Res.

122

S3-S8

2008

Homo sapiens

18718639

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

19625706

708063

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.

1505-1518

2010

Homo sapiens

20112045

708474

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

19490116

708672

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.

192-197

2010

Homo sapiens

19897854

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.

238-243

2009

Homo sapiens

19152836

712488

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

20071328

717165

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.

582-590

2010

Homo sapiens

20056908

717216

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

20846121

Swedberg, J.E.; Harris, J.M.

Plasmin substrate binding site cooperativity guides the design of potent peptide aldehyde inhibitors

Biochemistry

8454-8462

2011

Homo sapiens

21877690

Teno, N.; Gohda, K.; Wanaka, K.; Sueda, T.; Tsuda, Y.

Identification of novel plasmin inhibitors possessing nitrile moiety as warhead

Bioorg. Med. Chem. Lett.

6305-6309

2011

Homo sapiens

21944858

717386

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

22004735

717417

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

712-719

2011

Homo sapiens

22024794

Schaller, J.; Gerber, S.S.

The plasmin-antiplasmin system: structural and functional aspects

Cell. Mol. Life Sci.

785-801

2011

Homo sapiens (P00747)

21136135

717604

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

21510941

717845

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

21795691

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.

:571-577

2011

Homo sapiens

21992704

718043

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.

2053-2062

2010

Homo sapiens

20553378

718070

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.

298-310

2010

Homo sapiens

19889106

718272

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

e16483

2011

Homo sapiens, Mus musculus

21311769

718277

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

e18119

2011

Homo sapiens

21464960

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

25576865

731322

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

6348-6356

2014

Homo sapiens

25222106

Swedberg, J.E.; Harris, J.M.

Natural and engineered plasmin inhibitors: applications and design strategies

ChemBioChem

336-348

2012

Homo sapiens (P00747), Homo sapiens

22238174

731900

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

1346-1351

2012

Homo sapiens

22987920

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.

571-577

2012

Homo sapiens (P00747)

21992704

732405

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.

610-618

2015

Homo sapiens

25556624

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

e47638

2012

Homo sapiens

23071827

732904

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

1448-1453

2013

Homo sapiens

23598443

752616

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.

845-855

2017

Homo sapiens

28279966

753021

Yusova, E.

Plasmin enzymatic activity in the presence of actin

Biopolym. Cell

345-350

2015

Homo sapiens

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.

766-771

2017

Homo sapiens

29296720

753319

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

26551872

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

26822552