title: On the enzymatic properties of Dnmt1: specificity, processivity, mechanism of linear diffusion and allosteric regulation of the enzyme.
abstract: 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.
authors.affiliation: International University Bremen, School of Engineering and Science, Campus Ring 1, 28759 Bremen, Germany. a.jeltsch@iu-bremen.de
authors.forename: Albert
authors.initials: A
authors.lastname: Jeltsch
mesh_terms: 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
chemical_list: C411744:DMAP1 protein, human; D012097:Repressor Proteins