MODIFICATION OF ARGININE RESIDUES OF L-LYSINE-ALPHA-OXIDASE FROM A TRICHODERMA SPECIES

To investigate the nature of the active site of L-lysine-alpha-oxidase from Trichoderma sp., arginine residues of the enzyme were modified In contrast to L-amino acid oxidase from snake venom, which is completely inactivated, the L-lysine-alpha-oxidase from Trichoderma sp. is irreversibly inactivated by only 18% (the reversible inactivation was 65%) under similar conditions. The data suggest that arginine residues do not play a significant role in the enzymatic activity of the L-lysine-alpha-oxidase.