Human AP endonuclease (APE1), like most AP endonucleases, is of class II and requires an Mg 2+ in its active site in order to carry out its role in base excision repair. The yeast homolog of this enzyme is APN1.

人源脱嘌呤/脱嘧啶（AP）核酸内切酶 APE 1，也称为 HAP 1 或 Ref-1，与大肠杆菌核酸外切酶 III 蛋白具有同源性。 APE 1 水解断裂脱嘌呤/脱嘧啶位点 5´ 端的磷酸二酯键，产生单链 DNA 断 …

摘要：脱嘌呤/脱嘧啶核酸内切酶1 (Apurinic/apyrimidinic endonuclease 1，APE1)是一种广泛存在于生物体内、在碱基切除修复 (Base excision repair，BER)过程中能够在碱基缺失位点 (AP site)处识别并切割DNA的蛋白酶，其作用效率高且特异性强。 同时，APE1在一些癌症细胞中的活性较正常细胞明显偏高，因此其自身也是一种癌症生物标志物。 目前，通过在DNA上人工设计AP位点，利用APE1的切割能力生成理想的功能核酸链，并结合不同的信号输出及放大方式，研究者 …

2022年9月14日 · Here, we determine how the base excision repair (BER) endonuclease AP-endonuclease 1 (APE1) recognizes and cleaves DNA damage in the nucleosome. Kinetic assays determine that APE1 cleaves...

APE1 is the main apurinic/apyrimidinic endonuclease in eukaryotic cells, playing a central role in the DNA base excision repair pathway of all DNA lesions (uracil, alkylated and oxidized, and abasic sites), including single-strand breaks, and has also cotranscriptional activity by modulating genes expression directly regulated by either ubiquito...

2021年1月27日 · The exonuclease activity of Apurinic/apyrimidinic endonuclease 1 (APE1) is responsible for processing matched/mismatched terminus in various DNA repair pathways and for removing...

人APE (APE1)同大多数 APE一样，属于二型并需要二价镁离子于其活性位点以完成在 碱基切除修复 中的功能。 脱嘌呤嘧啶核酸内切酶（apurinic/apyrimidinic (AP) endonuclease，简称APE）是一种生物酶。

Apurinic endonuclease 1 (APE1) is one of the key enzyme in the DNA base excision repair system. APE1 hydrolyzes DNA adjacent to the 5'-end of an apurinic/apyrimidinic (AP) site to produce a nick with a 3'-hydroxyl group and a 5'-deoxyribose phosphate moiety. 无嘌呤核酸内切酶 1 (APE1) 是 DNA 碱基切除修复系统中的关键酶之一。

摘要： 脱嘌呤/脱嘧啶核酸内切酶1（Apurinic/apyrimidinic endonuclease 1,APE1）是一种广泛存在于生物体内、在碱基切除修复（Base excision repair,BER）过程中能够在碱基缺失位点（AP site）处识别并切割DNA的蛋白酶,其作用效率高且特异性强。同时,APE1在一些癌症细胞中的活性 ...

APE1 preforms AP site incision with surgical precision and skill, by sculpting the DNA to place the cleavage site in an optimal position for nucleophilic attack within its compact protein active site. APE1, however, has demonstrated broad surgical expertise, and applies its DNA cleavage activity to a wide variety of DNA and RNA substrates.