On the Enzymatic Properties of Dnmt1 Specificity, Processivity, Mechanism of Linear Diffusion and Allosteric Regulation of the Enzyme
On the Enzymatic Properties of Dnmt1 Specificity, Processivity, Mechanism of Linear Diffusion and Allosteric Regulation of the Enzyme
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DOI：
10.4161/epi.1.2.2767
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发表时间：
2006-04-01
期刊：
影响因子：
3.7
通讯作者：
Jeltsch, Albert
中科院分区：
文献类型：
--
作者：
Jeltsch, Albert
本文对DNMT1的酶学性质进行了综述。对DNMT1特异性的研究表明，它对半甲基化的靶点有30-40倍的偏好。它在一个过程中使半甲基化的DNA甲基化，在DNA上以随机行走的方式移动。根据底物和效应物的性质，脱氧核糖核酸与酶N端的变构位点(S)的结合可以导致对其催化活性的刺激和抑制。
In this short review the enzymatic properties of Dnmt1 are summarized. Studies on the specificity of Dnmt1 have shown that it has 30-40 fold preference for hemimethylated target sites. It methylates hemimethylated DNA in a processive reaction, moving on the DNA in a random walk. Binding of DNA to allosteric site(s) in the N-terminal part of the enzyme can lead to stimulation and inhibition of its catalytic activity depending on the nature of the substrate and effector.