Inhibition of Nicotinoprotein (NAD+-Containing) Alcohol Dehydrogenase by trans-4-(N,N-Dimethylamino)-Cinnamaldehyde Binding to the Active Site
作者:Sander R. Piersma、Annika Norin、Simon de Vries、Hans Jörnvall、Johannis A. Duine
DOI:10.1023/b:jopc.0000005461.53788.ee
日期:2003.7
Ethanol oxidation by nicotinoprotein alcohol dehydrogenase (np-ADH) from the bacterium Amycolatopsis methanolica is inhibited by trans-4-(N,N-dimethylamino)-cinnamaldehyde through direct binding to the catalytic zinc ion in a substrate-like geometry. This binding is accompanied by a characteristic red shift of the aldehyde absorbance from 398 nm to 467 nm. Np-ADH is structurally related to mammalian ADH class I, and a model of np-ADH shows how the cinnamaldehyde derivative can be accommodated in the active site of the nicotinoprotein, correlating the structural and enzymological data.
反式-4-(N,N-二甲基氨基)-肉桂醛以类似底物的几何形状直接与催化锌离子结合,从而抑制了甲醇嗜酸性杆菌(Amycolatopsis methanolica)的烟碱蛋白乙醇脱氢酶(np-ADH)的乙醇氧化作用。这种结合伴随着醛吸光度从 398 纳米到 467 纳米的特征性红移。Np-ADH 在结构上与哺乳动物的 I 类 ADH 有关,Np-ADH 的模型显示了肉桂醛衍生物如何能被容纳在烟碱蛋白的活性位点中,并将结构和酶学数据联系起来。