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BioMed Research International
Volume 2014 (2014), Article ID 196754, 19 pages
http://dx.doi.org/10.1155/2014/196754
Review Article

Snake Venom L-Amino Acid Oxidases: Trends in Pharmacology and Biochemistry

1Faculdade de Ciências Integradas do Pontal e Departamento de Genética e Bioquímica, Universidade Federal de Uberlândia (UFU), Uberlândia, MG, Brazil
2Centro 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
3Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP), Universidade de São Paulo (USP), Ribeirão Preto, SP, Brazil
4Departamento de Química, Biotecnologia e Engenharia de Bioprocessos, Universidade Federal de São João del Rei (UFSJ), Campus Altoparaopeba, Ouro Branco, MG, Brazil

Received 20 October 2013; Revised 13 December 2013; Accepted 16 December 2013; Published 12 March 2014

Academic Editor: Fernando Albericio

Copyright © 2014 Luiz Fernando M. Izidoro et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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.