Peptide name : L-amino-acid oxidase Bfon20 (LAAO; LAO)

Source/Organism : Fonseca's lancehead

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 15

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1791.8926 Dalton

Aliphatic index : 0.326

Instability index : 55.98

Hydrophobicity (GRAVY) : -1.533

Isoelectric point : 4.3354

Charge (pH 7) : -3.2002

Aromaticity : 0.066

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 0.66666666

hydrophobic moment : -0.815

Missing amino acid : W,H,Q,M,I,K,S,Y,V,G

Most occurring amino acid : E

Most occurring amino acid frequency : 3

Least occurring amino acid : A

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.2)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)O)[C@@H](C)O

1 : Tashima AK, et al. Snake venomics of the Brazilian pitvipers Bothrops cotiara and Bothrops fonsecai. Identification of taxonomy markers. J Proteomics. 2008; 71:473-85. doi: 10.1016/j.jprot.2008.07.007

Paper title : Snake venomics of the Brazilian pitvipers Bothrops cotiara and Bothrops fonsecai. Identification of taxonomy markers.

Doi : https://doi.org/10.1016/j.jprot.2008.07.007

Abstract : We report the proteomic characterization of venom of the pitvipers Bothrops cotiara and Bothrops fonsecai. Crude venoms were fractionated by reverse-phase HPLC, followed by SDS-PAGE, N-terminal sequencing, MALDI-TOF mass fingerprinting, and CID-MS/MS. Each venom contained around 30 proteins in the range of 7-110 kDa belonging to only 8 (B. cotiara) and 9 (B. fonsecai) families which may target the hemostatic system, albeit distinctly distributed among the two species. B. cotiara and B. fonsecai share medium-sized disintegrins, disintegrin-like/cysteine-rich (DC) fragments, snake venom vascular endothelial growth factor, cysteine-rich secretory proteins, serine proteinases, C-type lectins, l-amino acid oxidase, and Zn(2+)-dependent metalloproteinases. In addition, B. fonsecai expresses a high abundance PLA(2) molecule (13,890 Da), whereas PLA(2) molecules were not detected in B. cotiara's venom. This striking finding is in line with previous biochemical analyses showing the absence of phospholipasic activity in the venom of B. cotiara. The potential adaptive significance of the lack of PLA(2) molecules is enigmatic, and alternative explanations are discussed. B. fonsecai is morphologically extremely similar to B. cotiara. Our comparative proteomic analysis shows that compositional differences between their venoms can be employed as a taxonomy signature for unambiguous species identification independently of geographic origin and morphological characteristics.