Target Information

General Information of This Target
Target ID
BTDT10033
Target Name
Chymotrypsin
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    PI-stichotoxin-Hcr2g Inhibition constant
1.6 nM
 [1], [2], [3]
 Toxin Info    PI-stichotoxin-Hcr2f Inhibition constant
1.8 nM
 [1], [2], [3]
 Toxin Info    Actinia tenebrosa protease inhibitors Inhibition constant
2.9 nM
 [4], [5]
 Toxin Info    Kunitz-type serine protease inhibitor B1 Inhibition constant
4.77 nM
 [6]
 Toxin Info    Actinia tenebrosa protease inhibitors Inhibition constant
7.4 nM
 [4], [5]
 Toxin Info    Kunitz-type serine protease inhibitor IX Inhibition constant
18 nM
 [7], [8], [9]
 Toxin Info    PI-stichotoxin-Hcr2k Inhibition constant
23 nM
 [10]
 Toxin Info    Kunitz-type serine protease inhibitor NACI Inhibition constant
25 nM
 [11], [12], [13], [14]
 Toxin Info    PI-stichotoxin-Hcr2l Inhibition constant
30 nM
 [10]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 2 Inhibition constant
40 nM
 [15]
 Toxin Info    Kunitz-type serine protease inhibitor TCI Inhibition constant
84.6 nM
 [16], [17]
 Toxin Info    Secapin Inhibition constant
432.59 nM
 [18]
 Toxin Info    PI-stichotoxin-Hcr2o Inhibition constant
500 nM
 [3- 20]
 Toxin Info    PI-stichotoxin-Hcr2h Inhibition constant
0.7 μM
 [2- 21]
 Toxin Info    Kunitz-type serine protease inhibitor Inhibition constant
3.52 μM
 [22]
 Toxin Info    TauPI-stichotoxin-Hcr2c Inhibition constant
4.5 μM
 [23]
 Toxin Info    TauPI-stichotoxin-Hcr2b Inhibition constant
5 μM
 [24- 28]
 Toxin Info    TauPI-stichotoxin-Hcr2d Inhibition constant
7 μM
 [23- 29]
 Toxin Info    Kunitz serine protease inhibitor Pr-mulgin 2 Effective concentration 50
100 nM
 [15]
 Toxin Info    Secapin IC50
393.78 nM
 [18]
References
Ref 1 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 2 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 3 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 4 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 5 A Versatile and Robust Serine Protease Inhibitor Scaffold from Actinia tenebrosa. Mar Drugs. 2019 Dec 12;17(12):701. doi: 10.3390/md17120701.
Ref 6 Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis. Peptides. 2013 May;43:126-32. doi: 10.1016/j.peptides.2013.02.009. Epub 2013 Feb 18.
Ref 7 Complete amino acid sequences of two protease inhibitors in the venom of Bungarus fasciatus. Int J Pept Protein Res. 1983 Feb;21(2):209-15. doi: 10.1111/j.1399-3011.1983.tb03095.x.
Ref 8 BF9, the first functionally characterized snake toxin peptide with Kunitz-type protease and potassium channel inhibiting properties. J Biochem Mol Toxicol. 2014 Feb;28(2):76-83. doi: 10.1002/jbt.21538. Epub 2013 Nov 14.
Ref 9 Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus. J Biol Chem. 2001 Nov 30;276(48):45079-87. doi: 10.1074/jbc.M106182200. Epub 2001 Sep 18.
Ref 10 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 11 Taiwan cobra chymotrypsin inhibitor: cloning, functional expression and gene organization. Biochim Biophys Acta. 2005 Mar 14;1747(2):213-20. doi: 10.1016/j.bbapap.2004.11.006. Epub 2004 Dec 15.
Ref 12 Purification, characterization and primary structure of a chymotrypsin inhibitor from Naja atra venom. Comp Biochem Physiol B Biochem Mol Biol. 2004 Feb;137(2):219-24. doi: 10.1016/j.cbpc.2003.11.007.
Ref 13 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.
Ref 14 NMR solution structure of a Chymotrypsin inhibitor from the Taiwan cobra Naja naja atra. Molecules. 2013 Jul 26;18(8):8906-18. doi: 10.3390/molecules18088906.
Ref 15 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 16 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 17 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 18 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 19 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 20 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 21 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 22 Purification and characterization of a chymotrypsin inhibitor from the venom of Ophiophagus hannah (King Cobra). Biochem Biophys Res Commun. 2001 May 18;283(4):862-7. doi: 10.1006/bbrc.2001.4878.
Ref 23 [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 24 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 25 [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 26 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 27 Polypeptide modulators of TRPV1 produce analgesia without hyperthermia. Mar Drugs. 2013 Dec 16;11(12):5100-15. doi: 10.3390/md11125100.
Ref 28 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 29 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.
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