Otten L A, Vreugdenhil D, Schilperoort R A
Biochim Biophys Acta. 1977 Dec 8;485(2):268-77. doi: 10.1016/0005-2744(77)90163-2.
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.
章鱼碱型冠瘿瘤的D(+)-溶菌碱脱氢酶已得到部分纯化，并测定了一些动力学参数。D(+)-溶菌碱脱氢酶催化丙酮酸与至少六种不同L-氨基酸之一的还原缩合反应以及逆反应，优先使用NADP(H)作为辅因子。已确定了还原反应和氧化反应的最佳pH值。在pH 6.8时，L-赖氨酸在所有氨基酸中具有最低的Km值，而在相同pH值下，L-精氨酸和L-组氨酸的V值最高。D(+)-溶菌碱脱氢酶的等电点约为4.5。
