A new antitumor enzyme, L-lysine alpha-oxidase from Trichoderma viride. Purification and enzymological properties.
L-Lysine alpha-oxidase from Trichoderma viride Y244-2 has been purified to homogeneity. The enzyme shows absorption maxima at 277, 388, and 466 nm and a shoulder around 490 nm and contains 2 mol of FAD/mol of enzyme. The enzyme has a molecular weight of approximately 116,000 and consists of two subunits identical in molecular weight (about 56,000). In addition to L-lysine, L-ornithine, L-phenylalanine, L-tyrosine, L-arginine, and L-histidine are oxidized by the enzyme to a lesser extent. Several lysine analogs such as delta-hydroxylysine are oxidized efficiently. Balance studies showed that 1 mol of L-lysine is converted to an equimolar amount of alpha-keto-epsilon-aminocaproate, ammonia, and hydrogen peroxide with the consumption of 1 mol of oxygen. alpha-Keto-epsilon-aminocaproate spontaneously is dehydrated intramolecularly into delta 1-piperideine-2-carboxylate in the presence of catalase, and is oxidatively decarboxylated into delta-aminovalerate in the absence of catalase. The Michaelis constants are as follows: 0.04 mM for L-lysine, 0.44 mM for L-ornithine, 14 mM for L-phenylalanine, and 1.6 mM for oxygen with L-lysine.
D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification*; D000818:Animals; D000970:Antineoplastic Agents; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007940:Leukemia L5178 / Q000188:drug therapy; D051379:Mice; D003904:Mitosporic Fungi / Q000201:enzymology*; D010101:Oxygen Consumption; D008249:Protein-Lysine 6-Oxidase / Q000302:isolation & purification* / Q000378:metabolism / Q000627:therapeutic use; D013053:Spectrophotometry; D013379:Substrate Specificity; D014242:Trichoderma / Q000201:enzymology*
D000970:Antineoplastic Agents; D000594:Amino Acid Oxidoreductases; D008249:Protein-Lysine 6-Oxidase