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.
Highlights
L-amino acid oxidases are enzymes found in several organisms, including venoms of snakes, where they contribute to the toxicity of ophidian envenomation
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
Snake venoms consist of a mixture of protein with or without catalytic activity such as phospholipases A2 (PLA2), proteases, hyaluronidases, L-amino acid oxidases (LAAOs), acetylcholinesterases, growth factors, protein C activators, lectins, and von Willebrand factor-binding proteins; peptides mainly comprising bradykinin potentiators and disintegrins; low molecular weight organic compounds such as carbohydrates, serotonin, histamine, citrate, and nucleosides; and inorganic ions such as calcium, cobalt, magnesium, copper, iron, and potassium, as well as enzymatic inhibitors [3]
Summary
During the continuing evolution of snakes, according to Kardong [1], the development of more specialized glandular venom was essential in the emergence of biologically active substances capable of weakening prey to facilitate their capture. At first the discharge’s main function was to lubricate the snake’s food, but with the passage of time, some enzymes mixed with secretions allowing for the emergence of more elaborate and potentially toxic proteins, used in the immobilization of prey. A quantitative increase in the production of these secretions as well as a qualitative improvement of toxic proteins promoted a gain in absolute discretion in defense against predators [2]. Snake venoms consist of a mixture of protein with or without catalytic activity such as phospholipases A2 (PLA2), proteases, hyaluronidases, L-amino acid oxidases (LAAOs), acetylcholinesterases, growth factors, protein C activators, lectins, and von Willebrand factor-binding proteins; peptides mainly comprising bradykinin potentiators and disintegrins; low molecular weight organic compounds such as carbohydrates, serotonin, histamine, citrate, and nucleosides; and inorganic ions such as calcium, cobalt, magnesium, copper, iron, and potassium, as well as enzymatic inhibitors [3]
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