Lee H J, Chang G G
Department of Biochemistry, National Defense Medical Center, Taipei, Taiwan, Republic of China.
FEBS Lett. 1990 Dec 17;277(1-2):175-9. doi: 10.1016/0014-5793(90)80837-9.
Pigeon liver malic enzyme (EC 1.1.1.40) has a double dimer quaternary structure. The NADP+ analogs, aminopyridine adenine dinucleotide phosphate and nicotinamide-1,N6-ethenoadenosine dinucleotide phosphate, bind to the enzyme anti-cooperatively. In the presence of non-cooperative competing ligand NADP+, the binding parameter Hill coefficients of these analogues changed very little. Binding of L-malate with enzyme-AADP+ complex first enhanced then reduced the nucleotide fluorescence. Two L-malate binding sites, with Kd values of 23-30 and 270-400 microM, respectively. for the tight and weak binding sites were postulated. A hybrid model between the sequential and pre-existing asymmetrical models was proposed for the pigeon liver malic enzyme.
鸽肝苹果酸酶(EC 1.1.1.40)具有双二聚体四级结构。NADP⁺类似物,氨基吡啶腺嘌呤二核苷酸磷酸和烟酰胺-1,N⁶-乙烯腺苷二核苷酸磷酸,与该酶的结合呈反协同效应。在非协同竞争性配体NADP⁺存在的情况下,这些类似物的结合参数希尔系数变化很小。L-苹果酸与酶-AADP⁺复合物的结合首先增强然后降低了核苷酸荧光。推测有两个L-苹果酸结合位点,紧密结合位点和弱结合位点的解离常数(Kd)值分别为23 - 30和270 - 400微摩尔。针对鸽肝苹果酸酶提出了顺序模型和预先存在的不对称模型之间的混合模型。