Properties of D(+)-lysopine dehydrogenase from crown gall tumour tissue.
D(+)-Lysopine dehydrogenase of an octopine-type Crown Gall tumour has been partially purified and a number of kinetic parameters have been determined. D(+)-Lysopine dehydrogenase catalyzes the reductive condensation of pyruvate and one of at least six different L-amino acids, as well as the reverse reactions, with preferential use of NADP(H) as a cofactor. The optimal pH for both reductive and oxidative reactions has been determined. At pH 6.8, L-lysine has of all the amino acids the lowest Km value, while at the same pH the highest V was found with L-arginine and L-histidine. The isoelectric point of D(+)-lysopine dehydrogenase is about 4.5.
D000596:Amino Acids / Q000032:analysis; D003605:D-Amino-Acid Oxidase / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives; D010941:Plant Tumors; D013379:Substrate Specificity
D000596:Amino Acids; D003605:D-Amino-Acid Oxidase; D008239:Lysine