Grafstrom R H, Shaper N L, Grossman L
J Biol Chem. 1982 Nov 25;257(22):13459-64.
The mechanism of action of the homogeneous preparation of human placental apurinic/apyrimidinic (AP) endonuclease, described in the previous paper (Shaper, N. L., Grafstrom, R. H., and Grossman, L. (1982) J. Biol. Chem. 257, 13455-13458), has been investigated in detail. This enzyme cleaves apyrimidinic DNA both 5' and 3' to the site of damage in a ratio of 60:40, respectively. Even though this enzyme can cleave on both sides of an internal AP site, it does not release deoxyribose 5-phosphate from terminal AP sites. However, a compound, tentatively identified as alpha, beta unsaturated deoxyribose 5-phosphate, is nonenzymatically released only from 5'-terminal AP sites, presumably by a beta-elimination mechanism.
前一篇论文(Shaper, N. L., Grafstrom, R. H., and Grossman, L. (1982) J. Biol. Chem. 257, 13455 - 13458)中描述的人胎盘无嘌呤/无嘧啶(AP)内切核酸酶的均一制剂的作用机制已得到详细研究。该酶在损伤位点的5'和3'端切割无嘧啶DNA,其比例分别为60:40。尽管这种酶可以在内部AP位点的两侧进行切割,但它不会从末端AP位点释放5'-磷酸脱氧核糖。然而,一种暂定为α,β-不饱和5'-磷酸脱氧核糖的化合物仅从5'-末端AP位点非酶促释放,推测是通过β-消除机制。