Kleber H P
Acta Biol Med Ger. 1975;34(11-12):1739-43.
The malic enzyme enriched from Acinetobacter calcoaceticus is inhibited by NADPH and NADH. The inhibition afforded by the reduced coenzymes is not affected by NAD+, AMP and 3'.5'-AMP. Against L-malate, NADPH inhibits the enzyme in a noncompetitive linear fashion (Ki = 1.5 x 10(-4) M), against NADP+, competitively linearly (Ki = 5.0 x 10(-5) M). While NADPH acted as a product inhibitor, NADH seems to be an allosteric effector of the malic enzyme, because with L-malate as the variable substrate in the double reciprocal plot, a nonlinear curve is obtained.
从醋酸钙不动杆菌中富集的苹果酸酶受NADPH和NADH抑制。还原型辅酶产生的抑制作用不受NAD⁺、AMP和3',5'-AMP影响。对于L-苹果酸，NADPH以非竞争性线性方式抑制该酶（Ki = 1.5×10⁻⁴ M），对于NADP⁺，则以竞争性线性方式抑制（Ki = 5.0×10⁻⁵ M）。虽然NADPH作为产物抑制剂起作用，但NADH似乎是苹果酸酶的变构效应物，因为在双倒数图中以L-苹果酸作为可变底物时，会得到一条非线性曲线。
