On the enzymatic properties of Dnmt1: specificity, processivity, mechanism of linear diffusion and allosteric regulation of the enzyme.
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.
Jeltsch
Albert
A
International University Bremen, School of Engineering and Science, Campus Ring 1, 28759 Bremen, Germany. a.jeltsch@iu-bremen.de
D000494:Allosteric Regulation; D001665:Binding Sites; D002384:Catalysis; D019175:DNA Methylation; D004058:Diffusion; D004789:Enzyme Activation; D006801:Humans; D008954:Models, Biological; D012097:Repressor Proteins / Q000378:metabolism*; D013379:Substrate Specificity
C411744:DMAP1 protein, human; D012097:Repressor Proteins