Department of Biology, Southern University of Science and Technology , Shenzhen , Guangdong , China.
RNA Biol. 2019 Oct;16(10):1504-1512. doi: 10.1080/15476286.2019.1642712. Epub 2019 Jul 18.
aminohydrolase (ADAL) has been shown to be involved in the metabolism of N-methyl-AMP, a proposed intermediate during mA-modified RNA metabolism, which can be subsequently incorporated into newly synthesized RNA by Pol II. It has been proposed that ADAL will prevent N-methyl-AMP reuse and catabolize it to inosine monophosphate (IMP). Here, we have solved the crystal structures of ADAL in the apo form and in complex with GMP and IMP in the presence of Zn. We have identified the substrate-binding pocket of ADAL and compared it with that for adenosine deaminase (ADA), adenine deaminase (ADE) and AMP deaminase (AMPD) from multiple species. The comparisons reveal that plant ADAL1 may have the potential ability to catalyze different alkyl-group substituted substrates.
氨基水解酶 (ADAL) 已被证明参与 N-甲基-AMP 的代谢,N-甲基-AMP 是 mA 修饰 RNA 代谢过程中的一个提议中间体,可由 Pol II 掺入新合成的 RNA 中。有人提出 ADAL 将防止 N-甲基-AMP 再利用,并将其代谢为肌苷单磷酸 (IMP)。在这里,我们已经解决了 ADAL 在apo 形式和在 Zn 存在下与 GMP 和 IMP 复合物的晶体结构。我们已经确定了 ADAL 的底物结合口袋,并与来自多种物种的腺苷脱氨酶 (ADA)、腺嘌呤脱氨酶 (ADE) 和 AMP 脱氨酶 (AMPD) 进行了比较。这些比较表明,植物 ADAL1 可能具有催化不同烷基取代底物的潜在能力。