Abstract
L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H2O2, ammonia, and α-keto-ε-aminocaproate. Multiple in vitro and in vivo studies have reported cytotoxic, antitumor, antimetastatic, and antitumor activity of LO. Unlike asparaginase, LO has a dual mechanism of action: depletion of L-lysine and formation of H2O2, both targeting tumor growth. Prominent results were obtained on murine and human tumor models, including human colon cancer xenografts HCT 116, LS174T, and T47D with maximum T/C 12, 37, and 36%, respectively. The data obtained from human cancer xenografts in immunodeficient mice confirm the potential of LO as an agent for colon cancer treatment. In this review, we discuss recently discovered molecular mechanisms of biological action and the potential of LO as anticancer enzyme.
Highlights
Asparagine, arginine, and methionine were appointed as essential amino acids for cancer cells, and enzymes cleaving the aforementioned amino acids were reported to produce clinical effects against leukemia and solid cancers in animal experiments and clinical trials [1,2,3,4,5,6,7,8,9,10]
L-amino acid oxidases (LAAOs) of fungal origin, Amanita phalloides and Clitocybe geotropa, showed cytotoxic activity against Jurkat T-lymphoblastic leukemia and human breast epithelial MCF7 cells cultures and the most pronounced effect was in Jurkat cells (Table S1, Supplementary Materials) [15]
The review is devoted to a group of amino acid oxidases that are called lysine α-oxidase (LO) because they are specific towards L-lysine and, to some extent, to its structural analogs
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Therapeutic strategy aimed at reducing the serum level of certain amino acids, and for that reason, the decrease of their intake by cancer cells has been extensively investigated during the last 40 years. Asparagine, arginine, and methionine were appointed as essential amino acids for cancer cells, and enzymes cleaving the aforementioned amino acids were reported to produce clinical effects against leukemia and solid cancers in animal experiments and clinical trials [1,2,3,4,5,6,7,8,9,10]. L-lysine α-oxidases (LOs, EC 1.4.3.14) represent distinct group of LAAOs with unique substrate specificity catalyzing the oxidative deamination of. Ological action, pharmacological data, as well as evaluation of LO as anticancer agent
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