Foucaud B, Biellmann J F
Biochim Biophys Acta. 1983 Nov 14;748(3):362-6. doi: 10.1016/0167-4838(83)90180-2.
The reactive analogue of NAD+, CPAD+, was incorporated in the horse liver alcohol dehydrogenase (EC 1.1.1.1) linearly with its inactivation, to stoichiometry, with no apparent subunit interaction. No hydride transfer could take place in the modified enzyme, nor the interaction of trans-4-N,N-dimethylaminocinnamaldehyde with its reduced form, indicating an impairment of the accessibility to the catalytic zinc atom. The labeling in the enzyme, alkylated by [carbonyl-14C]CPAD+ was not stable, with a half-life of 32 h.
NAD+的反应类似物CPAD+与马肝醇脱氢酶（EC 1.1.1.1）的失活呈线性关系，按化学计量比掺入，且无明显的亚基相互作用。修饰后的酶中无法发生氢化物转移，反式-4-N,N-二甲基氨基肉桂醛与其还原形式也不发生相互作用，这表明催化锌原子的可及性受损。用[羰基-14C]CPAD+烷基化的酶中的标记不稳定，半衰期为32小时。
