Dunkerton J, James S P
Biochem J. 1976 Feb 1;153(2):503-4. doi: 10.1042/bj1530503.
In the oxidation of methylglyoxal by 2-oxoaldehyde dehydrogenase, the apparent Km value for NADP+ was about 2.5 times lower than the corresponding Km for NAD+; the apparent Km values for methylglyoxal and for the amine activator L-2-aminopropan-1-ol, with NADP+ as cofactor, were also different from those obtained with NAD+. In the presence of NADP+, the enzyme was not activated by P1, in contrast with the activation of the enzyme when NAD+ was used. The significance of the results is discussed.
在2-氧代醛脱氢酶催化甲基乙二醛氧化的过程中,NADP⁺的表观Km值比相应的NAD⁺的Km值低约2.5倍;以NADP⁺作为辅因子时,甲基乙二醛和胺激活剂L-2-氨基丙醇-1的表观Km值也与以NAD⁺作为辅因子时得到的值不同。与使用NAD⁺时酶的激活情况相反,在NADP⁺存在时,该酶未被P1激活。文中讨论了这些结果的意义。