Snake venom L-amino acid oxidases: trends in pharmacology and biochemistry
Luiz Fernando M Izidoro1, Juliana C Sobrinho2, Mirian M Mendes1
1Faculdade de Ciências Integradas do Pontal e Departamento de Genética e Bioquímica, Universidade Federal de Uberlândia (UFU), Uberlândia, MG, Brazil.
Abstract:
L-amino acid oxidases are enzymes found in several organisms, including venoms of snakes, where they contribute to the toxicity of ophidian envenomation. Their toxicity is primarily due to enzymatic activity, but other mechanisms have been proposed recently which require further investigation. L-amino acid oxidases exert biological and pharmacological effects, including actions on platelet aggregation and the induction of apoptosis, hemorrhage, and cytotoxicity. These proteins present a high biotechnological potential for the development of antimicrobial, antitumor, and antiprotozoan agents. This review provides an overview of the biochemical properties and pharmacological effects of snake venom L-amino acid oxidases, their structure/activity relationship, and supposed mechanisms of action described so far.
More Related Videos
10:25Extraction of Venom and Venom Gland Microdissections from Spiders for Proteomic and Transcriptomic Analyses
Published on: November 3, 2014
12:12Identification of Hemolytic and Phospholipase Activity in Crude Extracts from Sea Anemones by Straightforward Bioassays
Published on: March 29, 2022
Related Concept Videos
Physical Properties of Amines
Amino Acid Biosynthetic Pathways
Antidotes
Specific antidotes operate by inhibiting the enzymes that control biochemical pathways, reducing the production of harmful metabolites.
An example of an antidote is atropine, which counteracts the detrimental effects of cholinesterase inhibitors. It achieves this by deactivating muscarinic receptors,...
Amines: Introduction
Local Anesthetics: Chemistry and Structure-Activity Relationship
Anticholinesterase Agents: Poisoning and Treatment
Irreversible agents form a strong bond with the cholinesterase enzyme, making it inactive. The breakdown of the phosphorylated enzyme is...
