Peptide Information

General Information of This Peptide
Peptide ID
BTDP005864
Peptide Name
Basic phospholipase A2 homolog 2
Symonym
Myotoxin II
Species
Bothrops asper (Terciopelo)
Uniprot Name
PA2H2_BOTAS
Alphafold ID
P24605
3D Structure
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2D Sequence
3D Structure
Source
RSCB PDB: 1CLP
Sequence
MRTLWIMAVLLVGVEGSLFELGKMILQETGKNPAKSYGAYGCNCGVLGRGKPKDATDRCC
YVHKCCYKKLTGCNPKKDRYSYSWKDKTIVCGENNSCLKELCECDKAVAICLRENLNTYN
KKYRYYLKPLCKKADAC
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Sequence Length
137
Mass (Da)
15509
Signal Sequence
MRTLWIMAVLLVGVEG
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Sequence Removed Signal Peptide
SLFELGKMILQETGKNPAKSYGAYGCNCGVLGRGKPKDATDRCCYVHKCCYKKLTGCNPK
KDRYSYSWKDKTIVCGENNSCLKELCECDKAVAICLRENLNTYNKKYRYYLKPLCKKADA
C
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Disulfide Bond
42-131;44-60;59-111;65-137;66-104;73-97;91-102
PDB ID
1CLP , 1Y4L
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Lepidosauria
Order: Squamata
Family: Viperidae
Genus: Bothrops
Species: Bothrops asper
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    factor Xa (F10) IC50
3 nM
 .
Prothrombinase activity
 [1- 17]
References
Ref 1 Cloning and cDNA sequence analysis of Lys(49) and Asp(49) basic phospholipase A(2) myotoxin isoforms from Bothrops asper. Int J Biochem Cell Biol. 2001 Feb;33(2):127-32. doi: 10.1016/s1357-2725(00)00073-x.
Ref 2 Myotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2. Arch Biochem Biophys. 1991 Feb 1;284(2):352-9. doi: 10.1016/0003-9861(91)90307-5.
Ref 3 Solving the microheterogeneity of Bothrops asper myotoxin-II by high-resolution mass spectrometry: Insights into C-terminal region variability in Lys49-phospholipase A(2) homologs. Toxicon. 2022 Apr 30;210:123-131. doi: 10.1016/j.toxicon.2022.02.024. Epub 2022 Mar 3.
Ref 4 A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo). Toxicon. 1989;27(7):725-33. doi: 10.1016/0041-0101(89)90039-1.
Ref 5 Neutralizing interaction between heparins and myotoxin II, a lysine 49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modeling. J Biol Chem. 1994 Nov 25;269(47):29867-73.
Ref 6 Broad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venom. Toxicon. 1994 Nov;32(11):1359-69. doi: 10.1016/0041-0101(94)90408-1.
Ref 7 Autocatalytic acylation of phospholipase-like myotoxins. Biochemistry. 1995 Apr 11;34(14):4670-5. doi: 10.1021/bi00014a021.
Ref 8 Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom--synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region. Eur J Biochem. 1998 Apr 15;253(2):452-61. doi: 10.1046/j.1432-1327.1998.2530452.x.
Ref 9 Pharmacological modulation of edema induced by Lys-49 and Asp-49 myotoxic phospholipases A2 isolated from the venom of the snake Bothrops asper (terciopelo). Toxicon. 1998 Dec;36(12):1861-9. doi: 10.1016/s0041-0101(98)00107-x.
Ref 10 Comparative study of the cytolytic activity of myotoxic phospholipases A2 on mouse endothelial (tEnd) and skeletal muscle (C2C12) cells in vitro. Toxicon. 1999 Jan;37(1):145-58. doi: 10.1016/s0041-0101(98)00171-8.
Ref 11 Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics. BMC Struct Biol. 2007 Dec 6;7:82. doi: 10.1186/1472-6807-7-82.
Ref 12 Bothrops snake myotoxins induce a large efflux of ATP and potassium with spreading of cell damage and pain. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14140-5. doi: 10.1073/pnas.1009128107. Epub 2010 Jul 26.
Ref 13 Membrane cholesterol modulates the cytolytic mechanism of myotoxin II, a Lys49 phospholipase A2 homologue from the venom of Bothrops asper. Cell Biochem Funct. 2011 Jul;29(5):365-70. doi: 10.1002/cbf.1758. Epub 2011 Apr 19.
Ref 14 N-terminal domain of Bothrops asper Myotoxin II Enhances the Activity of Endothelin Converting Enzyme-1 and Neprilysin. Sci Rep. 2016 Mar 2;6:22413. doi: 10.1038/srep22413.
Ref 15 Corrigendum: N-terminal domain of Bothrops asper Myotoxin II Enhances the Activity of Endothelin Converting Enzyme-1 and Neprilysin. Sci Rep. 2016 Apr 22;6:24333. doi: 10.1038/srep24333.
Ref 16 Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper venom. Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):311-7. doi: 10.1107/S0907444994011455.
Ref 17 Inhibition of myotoxic activity of Bothrops asper myotoxin II by the anti-trypanosomal drug suramin. J Mol Biol. 2005 Jul 15;350(3):416-26. doi: 10.1016/j.jmb.2005.04.072.
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