Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.74 extracted from

  • Madrigal, M.; Alape-Giron, A.; Barboza-Arguedas, E.; Aguilar-Ulloa, W.; Flores-Dixadaz, M.
    Identification of B cell recognized linear epitopes in a snake venom serine proteinase from the central American bushmaster Lachesis stenophrys (2017), Toxicon, 140, 72-82 .
    View publication on PubMed
Search for more literature for 3.4.21.74

Application

Application Comment Organism
medicine the identification and characterization of relevant epitopes recognized by B cells in snake venom toxins may provide valuable information for the preparation of immunogens that help in the production of improved therapeutic antivenoms Lachesis stenophrys
medicine the identification and characterization of relevant epitopes recognized by B cells in snake venom toxins may provide valuable information for the preparation of immunogens that help in the production of improved therapeutic antivenoms Deinagkistrodon acutus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Lachesis stenophrys
-
-
extracellular
-
 Deinagkistrodon acutus
-
-

Organism

Organism UniProt Comment Textmining
Deinagkistrodon acutus Q9I8X1 i.e. Agkistrodon acutus
-
Lachesis stenophrys Q072L7
-
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Lachesis stenophrys
-
venom
-
 Deinagkistrodon acutus
-

Synonyms

Synonyms Comment Organism
AaV-SP-II UniProt Deinagkistrodon acutus
Dav-PA
-
 Deinagkistrodon acutus
Lachesis stenophrys venom serine proteinase
-
 Lachesis stenophrys
snake venom serine protease UniProt Lachesis stenophrys
snake venom serine protease UniProt Deinagkistrodon acutus

General Information

General Information Comment Organism
evolution the enzyme belongs to the peptidase S1 family, snake venom subfamily Deinagkistrodon acutus
additional information determination of 13 surface-located B cell-recognized linear epitopes of a Lachesis stenophrys venom serine proteinase. The corresponding peptides are synthesized and their immunoreactivity is analyzed against a panel of experimental and therapeutic antivenoms. Molecular modeling of the Lachesis stenophrys enzyme using as a template the structure of the Deinagkistrodon acutus Dav-PA serine proteinase (Q9I8X1), which displays the highest degree of sequence similarity to the Lachesis stenophrys enzyme among proteins of known 3D structure, and the surface-located epitopes are identified in the protein model using iCn3D Lachesis stenophrys
additional information molecular modeling of the Lachesis stenophrys enzyme (Q072L7) using as a template the structure of the Deinagkistrodon acutus Dav-PA serine proteinase (Q9I8X1), which displays the highest degree of sequence similarity to the Lachesis stenophrys enzyme among proteins of known 3D structure, and the surface-located epitopes are identified in the protein model using iCn3D Deinagkistrodon acutus