Target Information

General Information of This Target
Target ID
BTDT10288
Target Name
Trypsin
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    Cyclotide trypsin inhibitor TopI1 Dissociation constant
˜0.5 nM
 [1]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1c Dissociation constant
124 nM
 [2]
 Toxin Info    KappaPI-actitoxin-Ael3a Dissociation constant
124 nM
 [3], [4]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-1 Dissociation constant
136 nM
 [2]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-2 Dissociation constant
420 nM
 [2], [5]
 Toxin Info    Kunitz-type serine protease inhibitor BmKTT-3 Dissociation constant
760 nM
 [2]
 Toxin Info    Actinia tenebrosa protease inhibitors Inhibition constant
0.05 nM
 [6], [7]
 Toxin Info    Actinia tenebrosa protease inhibitors Inhibition constant
0.08 nM
 [6], [7]
 Toxin Info    Kunitz-type kappaPI-theraphotoxin-Hs1c Inhibition constant
0.281 nM
 [8], [9]
 Toxin Info    Kunitz-type serine protease inhibitor 1 Inhibition constant
0.34 nM
 [10], [11], [12]
 Toxin Info    Kunitz-type serine protease inhibitor textilinin-1 Inhibition constant
0.42 nM
 [13- 22]
 Toxin Info    PI-stichotoxin-Hcr2k Inhibition constant
2.4 nM
 [23]
 Toxin Info    PI-stichotoxin-Hcr2l Inhibition constant
2.5 nM
 [23]
 Toxin Info    Kunitz-type serine protease inhibitor Inhibition constant
3.5 nM
 [24]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 2 Inhibition constant
5 nM
 [25]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 3 Inhibition constant
5 nM
 [25]
 Toxin Info    Kunitz-type U15-theraphotoxin-Hs1e Inhibition constant
9.61 nM
 [8], [9]
 Toxin Info    PI-stichotoxin-Hcr2o Inhibition constant
21 nM
 [26], [27], [28]
 Toxin Info    PI-stichotoxin-Hcr2f Inhibition constant
28 nM
 [29], [30], [28]
 Toxin Info    PI-stichotoxin-Hcr2n Inhibition constant
30 nM
 [26], [27], [28]
 Toxin Info    PI-stichotoxin-Hmg3d Inhibition constant
50 nM
 [31]
 Toxin Info    PI-stichotoxin-Hcr2g Inhibition constant
50 nM
 [29], [30], [28]
 Toxin Info    PI-stichotoxin-Hcr2i Inhibition constant
52 nM
 [32], [31]
 Toxin Info    Kunitz-type serine protease inhibitor PILP-1 Inhibition constant
55.62 nM
 [33]
 Toxin Info    PI-stichotoxin-Hcr2p Inhibition constant
100 nM
 [26], [27], [28]
 Toxin Info    Secapin Inhibition constant
127.25 nM
 [34]
 Toxin Info    Kunitz-type serine protease inhibitor LmKTT-1a Inhibition constant
140 nM
 [2- 36]
 Toxin Info    PI-stichotoxin-Hcr2j Inhibition constant
190 nM
 [32], [31]
 Toxin Info    PI-stichotoxin-Hcr2m Inhibition constant
210 nM
 [26], [27], [28]
 Toxin Info    Kunitz-type serine protease inhibitor TCI Inhibition constant
391 nM
 [37], [38]
 Toxin Info    Kunitz-type serine protease inhibitor bicolin Inhibition constant
550 nM
 [39]
 Toxin Info    PI-stichotoxin-Hcr2h Inhibition constant
0.2 μM
 [28- 40]
 Toxin Info    Kunitz-type serine protease inhibitor PPTI Inhibition constant
0.2 μM
 [41], [42]
 Toxin Info    TauPI-stichotoxin-Hcr2d Inhibition constant
0.5 μM
 [43], [44], [45], [46]
 Toxin Info    TauPI-stichotoxin-Hcr2c Inhibition constant
0.9 μM
 [43]
 Toxin Info    TauPI-stichotoxin-Hcr2b Inhibition constant
1 μM
 [4- 48]
 Toxin Info    Kunitz-type serine protease inhibitor 3 Inhibition constant
5.1 μM
 [10], [12]
 Toxin Info    Kunitz-type serine protease inhibitor DrKIn-I Inhibition rate
45 %
 [49]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 2 Effective concentration 50
10 nM
 [25]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 3 Effective concentration 50
10 nM
 [25]
 Toxin Info    Kunitz-type serine protease inhibitor taicotoxin IC50
0.31 nM
 [17- 54]
 Toxin Info    Secapin IC50
80.02 nM
 [34]
 Toxin Info    Mambaquaretin-1 IC50
14.8 μM
 [55], [56], [57]
References
Ref 1 Head-to-Tail Cyclization after Interaction with Trypsin: A Scorpion Venom Peptide that Resembles Plant Cyclotides. J Med Chem. 2020 Sep 10;63(17):9500-9511. doi: 10.1021/acs.jmedchem.0c00686. Epub 2020 Aug 12.
Ref 2 Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family. J Biol Chem. 2012 Apr 20;287(17):13813-21. doi: 10.1074/jbc.M112.343996. Epub 2012 Feb 21.
Ref 3 A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties. Biochem Pharmacol. 2011 Jul 1;82(1):81-90. doi: 10.1016/j.bcp.2011.03.023. Epub 2011 Apr 6.
Ref 4 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 5 Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins. PLoS One. 2013;8(4):e60201. doi: 10.1371/journal.pone.0060201. Epub 2013 Apr 3.
Ref 6 The draft genome of Actinia tenebrosa reveals insights into toxin evolution. Ecol Evol. 2019 Sep 18;9(19):11314-11328. doi: 10.1002/ece3.5633. eCollection 2019 Oct.
Ref 7 A Versatile and Robust Serine Protease Inhibitor Scaffold from Actinia tenebrosa. Mar Drugs. 2019 Dec 12;17(12):701. doi: 10.3390/md17120701.
Ref 8 Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from tarantulas. PLoS One. 2008;3(10):e3414. doi: 10.1371/journal.pone.0003414. Epub 2008 Oct 15.
Ref 9 Molecular cloning, bioinformatics analysis and functional characterization of HWTX-XI toxin superfamily from the spider Ornithoctonus huwena. Peptides. 2014 Apr;54:9-18. doi: 10.1016/j.peptides.2014.01.001. Epub 2014 Jan 10.
Ref 10 Adaptive evolution in the snake venom Kunitz/BPTI protein family. FEBS Lett. 2003 Jul 17;547(1-3):131-6. doi: 10.1016/s0014-5793(03)00693-8.
Ref 11 The primary structure of Vipera ammodytes venom trypsin inhibitor I. Biochim Biophys Acta. 1983 Nov 14;748(3):429-35. doi: 10.1016/0167-4838(83)90189-9.
Ref 12 Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and kinetic studies. Eur J Biochem. 1983 Jun 15;133(2):427-32. doi: 10.1111/j.1432-1033.1983.tb07481.x.
Ref 13 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 14 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 15 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 16 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 17 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 18 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 19 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 20 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 21 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 22 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 23 Proteinase inhibitors from the tropical sea anemone Radianthus macrodactylus: isolation and characteristic. Biochemistry (Mosc). 2007 Mar;72(3):301-6. doi: 10.1134/s0006297907030078.
Ref 24 Primary structure and functional properties of cobra (Naja naja naja) venom Kunitz-type trypsin inhibitor. Eur J Biochem. 1990 Dec 12;194(2):337-41. doi: 10.1111/j.1432-1033.1990.tb15622.x.
Ref 25 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 26 A new multigene superfamily of Kunitz-type protease inhibitors from sea anemone Heteractis crispa. Peptides. 2012 Mar;34(1):88-97. doi: 10.1016/j.peptides.2011.09.022. Epub 2011 Oct 5.
Ref 27 Analgesic effect of novel Kunitz-type polypeptides of the sea anemone Heteractis crispa. Dokl Biochem Biophys. 2015;461:80-3. doi: 10.1134/S1607672915020052. Epub 2015 May 5.
Ref 28 Sea Anemone Kunitz-Type Peptides Demonstrate Neuroprotective Activity in the 6-Hydroxydopamine Induced Neurotoxicity Model. Biomedicines. 2021 Mar 10;9(3):283. doi: 10.3390/biomedicines9030283.
Ref 29 New Kunitz-Type HCRG Polypeptides from the Sea Anemone Heteractis crispa. Mar Drugs. 2015 Sep 24;13(10):6038-63. doi: 10.3390/md13106038.
Ref 30 Kunitz-Type Peptides from the Sea Anemone Heteractis crispa Demonstrate Potassium Channel Blocking and Anti-Inflammatory Activities. Biomedicines. 2020 Nov 4;8(11):473. doi: 10.3390/biomedicines8110473.
Ref 31 Kunitz-Type Peptides from Sea Anemones Protect Neuronal Cells against Parkinson's Disease Inductors via Inhibition of ROS Production and ATP-Induced P2X7 Receptor Activation. Int J Mol Sci. 2022 May 4;23(9):5115. doi: 10.3390/ijms23095115.
Ref 32 A new multigene HCIQ subfamily from the sea anemone Heteractis crispa encodes Kunitz-peptides exhibiting neuroprotective activity against 6-hydroxydopamine. Sci Rep. 2020 Mar 6;10(1):4205. doi: 10.1038/s41598-020-61034-x.
Ref 33 Genetic organization of Bungarus multicinctus protease inhibitor-like proteins. Toxicon. 2008 Jun 15;51(8):1490-5. doi: 10.1016/j.toxicon.2008.03.025. Epub 2008 Mar 27.
Ref 34 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 35 Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components. BMC Genomics. 2010 Jul 28;11:452. doi: 10.1186/1471-2164-11-452.
Ref 36 SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. PLoS One. 2011;6(11):e27548. doi: 10.1371/journal.pone.0027548. Epub 2011 Nov 8.
Ref 37 Isolation, expression and characterization of a novel dual serine protease inhibitor, OH-TCI, from king cobra venom. Peptides. 2008 Oct;29(10):1692-9. doi: 10.1016/j.peptides.2008.05.025. Epub 2008 Jun 5.
Ref 38 The king cobra genome reveals dynamic gene evolution and adaptation in the snake venom system. Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):20651-6. doi: 10.1073/pnas.1314702110. Epub 2013 Dec 2.
Ref 39 A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius. Comp Biochem Physiol B Biochem Mol Biol. 2009 May;153(1):116-20. doi: 10.1016/j.cbpb.2009.02.010. Epub 2009 Mar 1.
Ref 40 Kunitz-Type Peptide HCRG21 from the Sea Anemone Heteractis crispa Is a Full Antagonist of the TRPV1 Receptor. Mar Drugs. 2016 Dec 15;14(12):229. doi: 10.3390/md14120229.
Ref 41 Characterization of a new member of kunitz-type protein family from the venom of Persian false-horned viper, Pseudocerastes persicus. Arch Biochem Biophys. 2019 Feb 15;662:1-6. doi: 10.1016/j.abb.2018.11.017. Epub 2018 Nov 16.
Ref 42 Structural characterization of PPTI, a kunitz-type protein from the venom of Pseudocerastes persicus. PLoS One. 2019 Apr 11;14(4):e0214657. doi: 10.1371/journal.pone.0214657. eCollection 2019.
Ref 43 [New polypeptide components from the Heteractis crispa sea anemone with analgesic activity]. Bioorg Khim. 2009 Nov-Dec;35(6):789-98. doi: 10.1134/s1068162009060065.
Ref 44 Modulation of TRPV1-dependent contractility of normal and diabetic bladder smooth muscle by analgesic toxins from sea anemone Heteractis crispa. Life Sci. 2012 Nov 2;91(19-20):912-20. doi: 10.1016/j.lfs.2012.09.001. Epub 2012 Sep 12.
Ref 45 Polypeptide modulators of TRPV1 produce analgesia without hyperthermia. Mar Drugs. 2013 Dec 16;11(12):5100-15. doi: 10.3390/md11125100.
Ref 46 Anti-Inflammatory and Analgesic Effects of TRPV1 Polypeptide Modulator APHC3 in Models of Osteo- and Rheumatoid Arthritis. Mar Drugs. 2021 Jan 17;19(1):39. doi: 10.3390/md19010039.
Ref 47 Analgesic compound from sea anemone Heteractis crispa is the first polypeptide inhibitor of vanilloid receptor 1 (TRPV1). J Biol Chem. 2008 Aug 29;283(35):23914-21. doi: 10.1074/jbc.M800776200. Epub 2008 Jun 25.
Ref 48 [Interaction of sea amemone Heteractis crispa Kunitz type polypeptides with pain vanilloid receptor TRPV1: in silico investigation]. Bioorg Khim. 2012 Mar-Apr;38(2):185-98. doi: 10.1134/s106816201202015x.
Ref 49 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 50 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 51 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 52 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 53 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 54 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.
Ref 55 Green mamba peptide targets type-2 vasopressin receptor against polycystic kidney disease. Proc Natl Acad Sci U S A. 2017 Jul 3;114(27):7154-7159. doi: 10.1073/pnas.1620454114. Epub 2017 Jun 19.
Ref 56 A snake toxin as a theranostic agent for the type 2 vasopressin receptor. Theranostics. 2020 Sep 18;10(25):11580-11594. doi: 10.7150/thno.47485. eCollection 2020.
Ref 57 A new Kunitz-type snake toxin family associated with an original mode of interaction with the vasopressin 2 receptor. Br J Pharmacol. 2022 Jul;179(13):3470-3481. doi: 10.1111/bph.15814. Epub 2022 Feb 28.
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