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2. Molecular enzymology of the EcoRV DNA-(Adenine-N (6))-methyltransferase: kinetics of DNA binding and bending, kinetic mechanism and linear diffusion of the enzyme on DNA. Gowher H, Jeltsch A. J Mol Biol; 2000 Oct 13; 303(1):93-110. PubMed ID: 11021972 [Abstract] [Full Text] [Related]
3. How does a DNA interacting enzyme change its specificity during molecular evolution? A site-directed mutagenesis study at the DNA binding site of the DNA-(adenine-N6)-methyltransferase EcoRV. Beck C, Cranz S, Solmaz M, Roth M, Jeltsch A. Biochemistry; 2001 Sep 18; 40(37):10956-65. PubMed ID: 11551190 [Abstract] [Full Text] [Related]
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10. DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases. Szegedi SS, Gumport RI. Nucleic Acids Res; 2000 Oct 15; 28(20):3972-81. PubMed ID: 11024177 [Abstract] [Full Text] [Related]
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15. Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases. Scavetta RD, Thomas CB, Walsh MA, Szegedi S, Joachimiak A, Gumport RI, Churchill ME. Nucleic Acids Res; 2000 Oct 15; 28(20):3950-61. PubMed ID: 11024175 [Abstract] [Full Text] [Related]
16. On the substrate specificity of DNA methyltransferases. adenine-N6 DNA methyltransferases also modify cytosine residues at position N4. Jeltsch A, Christ F, Fatemi M, Roth M. J Biol Chem; 1999 Jul 09; 274(28):19538-44. PubMed ID: 10391886 [Abstract] [Full Text] [Related]
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