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On the Enzymatic Properties of Dnmt1: Specificity, Processivity, Mechanism of Linear Diffusion and Allosteric Regulation of the Enzyme
Albert Jeltsch
volume 1 | issue 2
april/may/june 2006Pages: 63 - 66
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In this short review the enzymatic properties of Dnmt1 are summarized. Studies on the specificity of Dnmt1 have shown that the enzymes 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.

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.





