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Ligand Aprotinin

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.14.5

aprotinin + H2O = ?

697489

-

Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Substrate (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.14.5

aprotinin + H2O = ?

679710, 697489

-

Activator in Enzyme-catalyzed Reactions (4 results)

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Show Activating Compound (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.1.21.1

activates DNase1/3-like activity

697891

-

3.4.21.7

augments binding of hepatocytes from mice to immobilized plasmin

685347

-

3.4.21.83

0.3 microM, 103% activity

663686

-

3.4.21.89

-

651885

-

Inhibitor in Enzyme-catalyzed Reactions (134 results)

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Show Inhibitors (134 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.8.4.2

-

394810

-

2.4.3.9

serine protease inhibitor, 0.0003 mM, 74% inhibition of purified sialyltransferase-1

638781

-

3.1.1.75

10 mM, 26% inhibition

678879

-

3.1.21.1

inhibits DNase1 as a result of plasmin inhibition

697891

-

3.2.1.2

-

694842

-

3.4.11.10

the recombinant enzyme shows 58.9% relative activity in the presence of 0.001 mM aprotinin on hydrolysis of L-Leu-7-amido-4-methylcoumarin

700078

-

3.4.11.14

82% residual activity at 0.1 mM

678175

-

3.4.11.6

34% residual activity at 0.25 mg/ml

682114

-

3.4.11.9

-

36057

-

3.4.11.9

slight

36061

-

3.4.14.4

1.0 mM inhibitor, 59% inhibition, 5.0 mM inhibitor, 99% inhibition

684026

-

3.4.14.4

competitive inhibitor

754208, 774468

-

3.4.11.9

2 entries

3.4.14.4

2 entries

3.4.14.9

0.08 mM, 60% loss of activity

647182

-

3.4.17.22

-

28969

-

3.4.18.1

0.1 mM, proPoCtX: 31.9% inhibition, native PoCtX: 51.3% inhibition

691910

-

3.4.19.2

-

95276

-

3.4.21.1

-

171873, 653202

-

3.4.21.1

partial inhibition at 0.1 mg/ml

680927

-

3.4.21.1

2 entries

3.4.21.10

-

36466, 36479, 36487

-

3.4.21.106

90% inhibition at 0.008 mM

651852

-

3.4.21.106

residual hepsin activity: 1%

697904

-

3.4.21.109

-

697904, 707795, 717966

-

3.4.21.109

inhibition of IGFBP-rP1 processing

673572

-

3.4.21.117

-

647342

-

3.4.21.117

90.3% inhibition at 0.0027 mM

647346

-

3.4.21.118

-

717863

-

3.4.21.118

0.01 mg/ml, 98% inhibition

668625

-

3.4.21.118

65% inhibition at 0.1 mM

647323

-

3.4.21.106

2 entries

3.4.21.109

2 entries

3.4.21.117

2 entries

3.4.21.118

3 entries

3.4.21.120

0.05 mM, 97% inhibition

667563

-

3.4.21.26

-

755073

-

3.4.21.26

1.4% inhibition at 0.05 mM

755073

-

3.4.21.26

89% residual activity at 1 mM

732281

-

3.4.21.26

inhibition of extracellular isozyme

683926

-

3.4.21.26

4 entries

3.4.21.27

-

667583, 669347

-

3.4.21.34

-

651518, 717295, 717809, 732931, 771627, 95360

-

3.4.21.34

besides PKal, aprotinin inhibits glandular kallikrein, plasmin, trypsin and tissue kallikrein

770942

-

3.4.21.34

besides PKal, aprotinin inhibits glandular kallikrein, plasmin, trypsin and tissue kallikrein. No inhibition by N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide, 1-benzyl-N-[(4-carbamimidoylphenyl)methyl]-1H-pyrazole-4-carboxamide, 3-amino-N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(3,5-dimethyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide, N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(trifluoromethyl)-1H-pyrazole-4-carboxamide, N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(methoxymethyl)-1H-pyrazole-4-carboxamide, 3-amino-1-methyl-15-[(1H-pyrazol-1-yl)methyl]-7,10,11,12,24,25-hexahydro-6H,18H,23H-19,22-(metheno)pyrido[4,3-j][1,9,13,17,18]benzodioxatriazacyclohenicosin-23-one, and 3-amino-1-methyl-15-[(1H-pyrazol-1-yl)methyl]-7,10,11,12,24,25-hexahydro-6H,18H,23H-19,22-(metheno)pyrido[4,3-j][1,9,13,17,18]benzodioxatriazacyclohenicosin-23-one

770942

-

3.4.21.35

-

647480, 647482, 647483, 647486, 647495, 647496, 647497, 647498, 647505, 647537

-

3.4.21.35

0.1 mM, 55% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide

668967

-

3.4.21.35

attenuates high-glucose stimulated expression of KLK1

710059

-

3.4.21.35

blocks increase of DU145 cell migration and invasion by tissue kallikrein

707627

-

3.4.21.35

delays skin wound healing

708418

-

3.4.21.35

strong

647488

-

3.4.21.35

tissue kallikrein is inactivated by incubation with 5fold molar excess of aprotinin at 37°C for 1 h

698208

-

3.4.21.35

up to 40% inhibition

668284

-

3.4.21.35

wild-type and recombinant enzyme

647494

-

3.4.21.35

-

647485

-

3.4.21.37

-

647555

-

3.4.21.37

no inhibition of proteinase 2A and 2B

647555

-

3.4.21.39

-

29374, 655425

-

3.4.21.39

partial

81365

-

3.4.21.4

-

699494, 701304, 708221

-

3.4.21.4

immobilized enzyme

95455

-

3.4.21.4

very efficient inhibition of trypsin-1 and trypsin-2, but not of trypsin-4

700478

-

3.4.21.45

0.0005 mM, 23% inhibition of proteolytic activity. 0.0005 mM, 37% inhibition of amidolytic activity

652686

-

3.4.21.45

0.005 mM, inhibits SP domain form and fI

667666

-

3.4.21.34

3 entries

3.4.21.35

10 entries

3.4.21.37

2 entries

3.4.21.39

2 entries

3.4.21.4

3 entries

3.4.21.45

2 entries

3.4.21.48

i.e. trasylol, weak

95499

-

3.4.21.59

-

29374, 29378, 29393, 29395, 29396, 651070

-

3.4.21.59

not

29407, 29408

-

3.4.21.59

weak inhibitor

653718

-

3.4.21.59

3 entries

3.4.21.6

95% inhibition of factor Xa and 2% inhibition of prothrombinase complex activity at 10 U/ml

652682

-

3.4.21.62

-

669614, 769821

-

3.4.21.62

inhibits the enzymatic activity by 15%

707232

-

3.4.21.68

-

664747, 666406

-

3.4.21.68

mitigates tPA-induced neuronal injury. Pre-treatment of N27 cells with aprotinin for 30 min before tPA exposure is protective against cell death, increasing the cell viability to 91.8% at a tPA concentration of 20 microg/ml. When aprotinin treatment follows tPA exposure, cell death is proportional to the length of tPA exposure

695293

-

3.4.21.62

2 entries

3.4.21.68

2 entries

3.4.21.69

-

29625

-

3.4.21.7

-

709033, 717259, 718070, 731653, 754794

-

3.4.21.7

complete inhibition of pro-matrix metalloproteinase-3 activation at 0.05 mM

667544

-

3.4.21.7

in a mouse tail-vein bleeding model, intravenous textilinin-1 and aprotinin cause similar decreases in blood loss while time to hemostasis in the textilinin-treated animals is significantly shorter

697026

-

3.4.21.7

inhibits plasmin-induced phosphorylation of ERK1/2

685347

-

3.4.21.7

plasmin inhibitor, completely blocks ability of noninhibitory plasminogen activator inhibitor-type 1 to normalize ECM degradation

688737

-

3.4.21.7

5 entries

3.4.21.73

-

29674

-

3.4.21.74

from bovine

29680

-

3.4.21.77

-

647583

-

3.4.21.77

efficient inhibition

680680

-

3.4.21.77

2 entries

3.4.21.78

-

29734, 29736, 29737

-

3.4.21.9

-

95584

-

3.4.21.9

40-90% loss of activtity

683172

-

3.4.21.91

-

665644, 681172, 681174, 681687, 707440, 769661

-

3.4.21.91

a 60-amino acid bovine pancreatic trypsin inhibitor and an efficient inhibitor of ZIKV NS2B-NS3pro

752516

-

3.4.21.91

bovine pancreatic trypsin inhibitor, BPTI

752513

-

3.4.21.91

completely inhibits autolysis of the NS2B-NS3pro construct

682663

-

3.4.21.91

non-specific inhibitor of NS2B-NS3pro, full inhibition at 0.001 mM

677891

-

3.4.21.9

2 entries

3.4.21.91

5 entries

3.4.21.98

-

667522, 681172

-

3.4.21.99

weak

665085

-

3.4.21.B1

-

650458, 668344, 685438, 717169

-

3.4.21.B1

at high concentrations

652018

-

3.4.21.B1

most efficient inhibition

651257

-

3.4.21.B1

potent serine protease inhibitor, inhibits autoactivation at physiological concentrations

650444

-

3.4.21.B10

-

665086

-

3.4.21.B10

pan-serine protease inhibitor

731396

-

3.4.21.B12

complex formation with the self-activated recombinant, chimeric enzyme

647338

-

3.4.21.B12

markedly decreases migratory potential of K4 clones

689848

-

3.4.21.B1

4 entries

3.4.21.B10

2 entries

3.4.21.B12

2 entries

3.4.21.B39

34% inhibition at 0.1 g/ml

683017

-

3.4.21.B4

0.015 mM

679100

-

3.4.21.B4

89% inactivation at 0.005 mM

651259

-

3.4.21.B4

93% inactivation at 0.015 mM

651948

-

3.4.21.B4

94% inactivation at 0.005 mM

651259

-

3.4.21.B4

complete inhibition at 0.015 mM

668782

-

3.4.21.B4

5 entries

3.4.21.B40

16% inhibition at 0.001 mM

752721

-

3.4.21.B42

30% inhibition at 2.5 mM

668284

-

3.4.21.B43

weak inhibition at 0.02 mM

678534

-

3.4.21.B57

-

727459, 769821

-

3.4.21.B6

-

671687, 673905

-

3.4.21.B6

0.02 mg/ml, 41% inhibition within 60 min

651463

-

3.4.21.B6

50% inhibition at 0.0000018 mM

651845

-

3.4.21.B6

completely inhibits

671251

-

3.4.21.B6

reversible binding to prostasin

652134

-

3.4.21.B61

0.01 mM, 0.2% residual activity

752448

-

3.4.21.B61

ratio of inhibitor to protease concentration achieving 50% inhibition is 147

755105

-

3.4.21.B61

spread of viral infection in MDCK cells expressing HAT is completely inhibited

755631

-

3.4.21.B6

5 entries

3.4.21.B61

3 entries

3.4.22.15

55.22% inhibition at 0.1 mM

710915

-

3.4.22.28

0.1 mM, 64% inhibition

648030

-

3.4.22.29

0.015 mM, 23% inhibition

648056

-

3.4.22.38

25.08% inhibition at 0.1 mM

708216

-

3.4.22.41

36.94% inhibition at 0.1 mM

708220

-

3.4.22.8

-

81593

-

3.4.22.B49

-

754348

-

3.4.23.23

72.6% residual activity at 1 mM

754970

-

3.4.23.24

-

709986

-

3.4.23.48

inhibits the recombinant enzyme expressed in Escherichia coli strain BL21 or DELTAcroP mutant strain of Citrobacter rodentium, in vivo. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptins

753795

-

3.4.23.49

ability of EHEC EDL933 cells to cleave the FRET substrate in the presence of increasing concentrations of aprotinin, about 90% inhibition at 0.2 mM. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptin

753795

-

3.4.23.49

classical protease inhibitors are ineffective against CroP activity, but the serine protease inhibitor aprotinin displays inhibitory potency in the micromolar range. Aprotinin acts as a competitive inhibitor of CroP activity and interferes with the cleavage of the murine cathelicidin-related antimicrobial peptide. Structural model of the aprotinin-omptin complex in which Lys15 of aprotinin forms salt bridges with conserved negatively charged residues of the omptin active site, molecular docking, overview. Aprotinin inhibits CRAMP proteolytic degradation by CroP. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptins

753795

-

3.4.23.49

inhibits CroP in a competitive manner

754014

-

3.4.23.49

inhibits OmpT in a competitive manner

754014

-

3.4.23.49

4 entries

3.4.24.26

markedly decreases enzymatic activity

754211

-

3.4.24.38

-

31235

-

3.4.24.56

22.4% inhibition

652058

-

3.4.24.72

82.3% residual activity at 5 mM

754441

-

3.4.24.72

strong inhibition

733596

-

3.4.24.72

2 entries

3.4.24.B10

0.1 mg/ml

677883

-

3.4.24.B9

11% inhibition at 0.025 mM

651308

-

3.4.25.1

0.0133 mg/ml, 53.62% inhibition

669016

-

3.4.99.B2

0.1 mM, 14% inhibition

667380, 695517

-

Enzyme Kinetic Parameters

K_i Value (24 results)

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Show KI Value (24 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.14.4

0.0117

-

pH and temperature not specified in the publication

774468

3.4.21.1

0.0000075

-

25°C, pH 7.5

653202

3.4.21.1

0.000018

-

25°C, pH 7.5

653202

3.4.21.109

0.000005

-

matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

717966

3.4.21.109

0.0000098

-

recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

717966

3.4.21.109

0.000013

-

purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

717966

3.4.21.1

2 entries

3.4.21.109

3 entries

3.4.21.117

0.000027

-

pH 8.0, 37°C

647346

3.4.21.27

0.52

-

L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroanilide substrate, free FXIa

667583

3.4.21.27

0.96

-

FIX substrate, free FXIa

667583

3.4.21.27

10.42

-

FIX substrate, FXIa-FIX complex

667583

3.4.21.27

3 entries

3.4.21.34

0.0000164

-

in 0.1 M Tris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25°C

717295

3.4.21.59

0.25

-

pH 8.2, 22°C

653718

3.4.21.59

0.369

-

pH 8.2, 22°C, recombinant tryptase

653718

3.4.21.59

2 entries

3.4.21.7

0.00000018

-

pH and temperature not specified in the publication

731653

3.4.21.91

0.000000079

-

enzyme from Dengue virus serotype 1

665644

3.4.21.91

0.00001761

-

-

681172

3.4.21.91

0.00002

-

wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C

707440

3.4.21.91

0.000025

-

-

682663

3.4.21.91

0.000026

-

pH and temperature not specified in the publication

769661

3.4.21.91

0.00007

-

pH 8.0, 20°C

752516

3.4.21.98

0.00001761

-

-

681172

3.4.21.98

0.000026

-

pH 8.0, 18°C

667522

3.4.21.91

6 entries

3.4.21.98

2 entries

3.4.21.B1

0.00000088

-

pH 8.2, 37°C

651257

3.4.21.B6

0.0000014

-

-

671687

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

3.4.21.91

0.0001024

-

-

677891

References & Links

Literature References (188)

top print hide

Show Reference (188 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

28969

7559630

Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme from bovine pituitary

1995

Song, L.; Fricker, L.D.

J. Biol. Chem.

270

25007-25013

29374

3890754

Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and functions

1985

Kido, H.; Fukusen, N.; Katunuma, N.

Arch. Biochem. Biophys.

239

436-443

29378

7845247

Tryptase: a mast cell serine protease

1994

Schwartz, L.B.

Methods Enzymol.

244

88-100

29393

1515079

Bovine tryptase: purification and characterization

1992

Fiorucci, L.; Erba, F.; Ascoli, F.

Biol. Chem. Hoppe-Seyler

373

483-490

29395

2036367

Tryptase from rat skin: purification and properties

1991

Braganza, V.J.; Simmons, W.H.

Biochemistry

30

4997-5007

29396

2205244

A new, highly sensitive enzymic assay for human tryptase and its use for identification of tryptase inhibitors

1990

Dietze, S.C.; Auerswald, E.A.; Fritz, H.

Biol. Chem. Hoppe-Seyler

371

65-73

29407

1469068

Pericellular substrates of human mast cell tryptase: 72,000 dalton gelatinase and fibronectin

1992

Lohi, J.; Harvima, I.; Keski-Oja, J.

J. Cell. Biochem.

50

337-349

29408

2110591

Purification of tryptase from a human mast cell line

1990

Butterfield, J.H.; Weiler, D.A.; Hunt, L.W.; Wynn, S.R.; Roche, P.C.

J. Leukocyte Biol.

47

409-419

29625

1697990

Inhibition of activated protein C by aprotinin and the use of the insolubilized inhibitor for its purification

1990

Taby, O.; Chabbat, J.; Steinbuch, M.

Thromb. Res.

59

27-35

29674

6682102

Purification and characterization of rat urinary esterase A, a plasminogen activator

1983

Chao, J.

J. Biol. Chem.

258

4434-4439

29680

8024586

Isolation of multiple isoforms of alpha-fibrinogenase from the Western diamondback rattlesnake, Crotalus atrox: N-terminal sequence homology with ancrod, an antithrombotic agent from Malayan viper

1994

Hung, C.C.; Chiou, S.H.

Biochem. Biophys. Res. Commun.

201

1414-1423

29734

1998680

Human and murine cytotoxic T lymphocyte serine proteases: subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins

1991

Odake, S.; Kam, C.M.; Narasimhan, L.; Poe, M.; Blake, J.T.; Krahenbuhl, O.; Tschopp, J.; Powers, J.C.

Biochemistry

30

2217-2227

29736

3545816

Purification and characterization of a T cell specific serine proteinase (TSP-1) from cloned cytolytic T lymphocytes

1986

Simon, M.M.; Hoschutzky, H.; Fruth, U.; Simon, H.G.; Kramer, M.D.

EMBO J.

5

3267-3274

29737

7845244

Granzyme A

1994

Simon, M.M.; Kramer, M.D.

Methods Enzymol.

244

68-79

31235

3319620

Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii are (hydroxy)proline-specific proteases

1987

Jaenicke, L.; Kuhne, W.; Spessert, R.; Wahle, U.; Waffenschmidt, S.

Eur. J. Biochem.

170

485-491

36057

1645659

Aminopeptidase P from rat brain. Purification and action on bioactive peptides

1991

Harbeck, H.T.; Mentlein, R.

Eur. J. Biochem.

198

451-458

36061

1363864

Localization and characterization of aminopeptidase P in bovine adrenal medulla

1992

Vanhoof, G.; de Block, J.; de Meester, I.; Scharpe, S.; de Potter, W.P.

Neurochem. Int.

21

203-208

36466

1191254

Studies on ram acrosin. Isolation from spermatozoa, activation by cations and organic solvents, and influence of cations on its reaction with inhibitors

1975

Brown, C.R.; Andani, Z.; Hartree, E.F.

Biochem. J.

149

133-146

36479

1772311

Human acrosin: purification and some properties

1991

Kobayashi, T.; Matsuda, Y.; Oshio, S.; Kaneko, S.; Nozawa, S; Mhori, H.; Akihama, S.; Fujimoto, Y.

Arch. Androl.

27

9-16

36487

1333593

Research note: kinetic and inhibition studies with turkey acrosin

1992

Richardson, M.E.; Korn, N.; Bodine, A.B.; Thurston, R.J.

Poult. Sci.

71

1789-1793

81365

3544704

Biological functions of serine proteases in the granules of rat mast cells

1986

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Kallikrein 4 is a potential mediator of cellular interactions between cancer cells and osteoblasts in metastatic prostate cancer

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Molecular cloning, tissue distribution and enzymatic characterization of cathepsin X from olive flounder (Paralichthys olivaceus)

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Purification and characterization of camel (Camelus dromedarius) milk amylase

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Isolation and characterization of mammalian D-aspartyl endopeptidase

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Murine serum nucleases - contrasting effects of plasmin and heparin on the activities of DNase1 and DNase1-like 3 (DNase1/3)

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Partial purification and characterization of trypsin-like proteinases from insecticide-resistant and -susceptible strains of the maize weevil, Sitophilus zeamais

2010

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A novel signaling pathway of tissue kallikrein in promoting keratinocyte migration: activation of proteinase-activated receptor 1 and epidermal growth factor receptor

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The yeast Candida albicans evades human complement attack by secretion of aspartic proteases

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2010

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Plasmin plays a key role in the regulation of profibrogenic molecules in hepatic stellate cells

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Kallikrein 6 is a novel molecular trigger of reactive astrogliosis

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Inhibition of outer membrane proteases of the omptin family by aprotinin

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Cloning and characterization of a basic cysteine-like protease (cathepsin L1) expressed in the gut of larval Diaprepes abbreviatus L. (Coleoptera Curculionidae)

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MDCK cells that express proteases TMPRSS2 and HAT provide a cell system to propagate influenza viruses in the absence of trypsin and to study cleavage of HA and its inhibition

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Discovery and development of plasma kallikrein inhibitors for multiple diseases

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Survey of dipeptidyl peptidase III inhibitors From small molecules of microbial or synthetic origin to aprotinin

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Molecules

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Links to other databases for Aprotinin

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