Target Information

General Information of This Target
Target ID
BTDT30004
Target Name
Plasmin
Target Bioclass
Enzyme
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N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Kunitz-type serine protease inhibitor DrKIn-II Inhibition constant
0.19 nM
 [1], [2]
 Toxin Info    Kunitz-type serine protease inhibitor textilinin-1 Inhibition constant
0.44 nM
 [3- 12]
 Toxin Info    Kunitz-type serine protease inhibitor Bt-KTI Inhibition constant
2.01 nM
 [13]
 Toxin Info    Kunitz-type serine protease inhibitor textilinin-2 Inhibition constant
2.2 nM
 [3- 14]
 Toxin Info    Kunitz-type serine protease inhibitor Bi-KTI Inhibition constant
3.6 nM
 [15]
 Toxin Info    Kunitz-type serine protease inhibitor OMI Inhibition constant
33 nM
 [7]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 2 Inhibition constant
40 nM
 [16]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 3 Inhibition constant
100 nM
 [16]
 Toxin Info    Secapin Inhibition constant
502.91 nM
 [17]
 Toxin Info    Kunitz-type serine protease inhibitor DrKIn-I Inhibition rate
70 %
 [1]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 2 Effective concentration 50
100 nM
 [16]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 3 Effective concentration 50
200 nM
 [16]
 Toxin Info    Kunitz-type serine protease inhibitor taicotoxin IC50
6.1 nM
 [7- 21]
 Toxin Info    Kunitz-type serine protease inhibitor Bi-KTI IC50
43.53 nM
 [15]
 Toxin Info    Secapin IC50
457.98 nM
 [17]
References
Ref 1 A novel heparin-dependent inhibitor of activated protein C that potentiates consumptive coagulopathy in Russell's viper envenomation. J Biol Chem. 2012 May 4;287(19):15739-48. doi: 10.1074/jbc.M111.323063. Epub 2012 Mar 13.
Ref 2 Functional characterization of a slow and tight-binding inhibitor of plasmin isolated from Russell's viper venom. Biochim Biophys Acta. 2014 Jan;1840(1):153-9. doi: 10.1016/j.bbagen.2013.08.019. Epub 2013 Aug 30.
Ref 3 A family of textilinin genes, two of which encode proteins with antihaemorrhagic properties. Br J Haematol. 2002 Nov;119(2):376-84. doi: 10.1046/j.1365-2141.2002.03878.x.
Ref 4 Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model. Blood Coagul Fibrinolysis. 2000 Jun;11(4):385-93. doi: 10.1097/00001721-200006000-00011.
Ref 5 Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents. Pathophysiol Haemost Thromb. 2005;34(4-5):188-93. doi: 10.1159/000092421.
Ref 6 Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss. Br J Haematol. 2009 Apr;145(2):207-11. doi: 10.1111/j.1365-2141.2009.07605.x. Epub 2009 Feb 22.
Ref 7 Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms. Biochimie. 2012 Feb;94(2):365-73. doi: 10.1016/j.biochi.2011.08.003. Epub 2011 Aug 11.
Ref 8 Drug development from Australian elapid snake venoms and the Venomics pipeline of candidates for haemostasis: Textilinin-1 (Q8008), Haempatch? (Q8009) and CoVase? (V0801). Toxicon. 2012 Mar 15;59(4):456-63. doi: 10.1016/j.toxicon.2010.12.010. Epub 2010 Dec 22.
Ref 9 Molecular diversity in venom from the Australian Brown snake, Pseudonaja textilis. Mol Cell Proteomics. 2006 Feb;5(2):379-89. doi: 10.1074/mcp.M500270-MCP200. Epub 2005 Nov 10.
Ref 10 Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 from Pseudonaja textilis textilis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt 7):642-5. doi: 10.1107/S1744309106019099. Epub 2006 Jun 10.
Ref 11 Crystal structure of textilinin-1, a Kunitz-type serine protease inhibitor from the venom of the Australian common brown snake (Pseudonaja textilis). FEBS J. 2009 Jun;276(11):3163-75. doi: 10.1111/j.1742-4658.2009.07034.x. Epub 2009 Apr 28.
Ref 12 The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake. PLoS One. 2013;8(1):e54104. doi: 10.1371/journal.pone.0054104. Epub 2013 Jan 15.
Ref 13 Molecular cloning and antifibrinolytic activity of a serine protease inhibitor from bumblebee (Bombus terrestris) venom. Toxicon. 2013 Mar 1;63:1-6. doi: 10.1016/j.toxicon.2012.11.004. Epub 2012 Nov 16.
Ref 14 Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes. Cell Mol Life Sci. 2008 Dec;65(24):4039-54. doi: 10.1007/s00018-008-8573-5.
Ref 15 Antifibrinolytic role of a bee venom serine protease inhibitor that acts as a plasmin inhibitor. PLoS One. 2012;7(2):e32269. doi: 10.1371/journal.pone.0032269. Epub 2012 Feb 16.
Ref 16 Functional characterization of Kunitz-type protease inhibitor Pr-mulgins identified from New Guinean Pseudechis australis. Toxicon. 2012 Jan;59(1):74-80. doi: 10.1016/j.toxicon.2011.10.005. Epub 2011 Oct 19.
Ref 17 Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Dev Comp Immunol. 2016 Oct;63:27-35. doi: 10.1016/j.dci.2016.05.011. Epub 2016 May 18.
Ref 18 Isolation and physiological characterization of taicatoxin, a complex toxin with specific effects on calcium channels. Toxicon. 1992 Nov;30(11):1343-64. doi: 10.1016/0041-0101(92)90511-3.
Ref 19 Effect of TaiCatoxin (TCX) on the electrophysiological, mechanical and biochemical characteristics of spontaneously beating ventricular cardiomyocytes. Mol Cell Biochem. 1996 Jul-Aug;160-161:61-6. doi: 10.1007/BF00240032.
Ref 20 A novel small conductance Ca2+-activated K+ channel blocker from Oxyuranus scutellatus taipan venom. Re-evaluation of taicatoxin as a selective Ca2+ channel probe. J Biol Chem. 1997 Aug 8;272(32):19925-30. doi: 10.1074/jbc.272.32.19925.
Ref 21 Taicatoxin inhibits the calcium-dependent slow motility of mammalian outer hair cells. Hear Res. 2005 May;203(1-2):172-9. doi: 10.1016/j.heares.2004.12.003.
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