Snake venom L-amino acid oxidases: trends in pharmacology and biochemistry.

Biomed Res Int

Centro de Estudos de Biomoléculas Aplicadas à Saúde, (CEBio), Fundação Oswaldo Cruz, Fiocruz Rondônia e Departamento de Medicina, Universidade Federal de Rondônia (UNIR), Porto Velho, RO, Brazil.

Published: January 2015

AI Article Synopsis

  • - L-amino acid oxidases are enzymes found in snake venoms that contribute to their toxicity mainly through their enzymatic activity, but other potential mechanisms are still being researched.
  • - These enzymes have significant biological effects, such as influencing platelet aggregation, triggering cell death (apoptosis), causing hemorrhage, and exhibiting cytotoxic properties.
  • - The review discusses the biochemical characteristics of snake venom L-amino acid oxidases, their relationships between structure and activity, and the different mechanisms of action that have been proposed.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3971498PMC
http://dx.doi.org/10.1155/2014/196754DOI Listing

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