title: Neisseria gonorrhoeae M.Ngo AI DNA methyltransferase: physical and catalytic properties of the homogeneous enzyme.
abstract: A DNA methyltransferase, M.NgoAI, was purified to homogeneity from Neisseria gonorrhoeae strain WR220 by successive column chromatography. Its Mr is 25,000, as determined by both gel filtration and denaturing polyacrylamide gel electrophoresis. Maximal enzymatic activity was obtained in 50 mM Tris.HCl (pH 7.4), 10 mM EDTA, with incubation at 37 degrees C. An apparent Km value for S-adenosylmethionine and 5' -GGCC sites was determined to be 1.25 microM and 89.6 nM, respectively.
authors.affiliation: Medical Biotechnology Center, University of Maryland, Baltimore.
authors.forename: A
authors.initials: A
authors.lastname: Piekarowicz
authors.forename: R
authors.initials: R
authors.lastname: Yuan
authors.forename: D C
authors.initials: DC
authors.lastname: Stein
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism; D007700:Kinetics; D008745:Methylation; D008970:Molecular Weight; D009344:Neisseria gonorrhoeae / Q000201:enzymology*; D012436:S-Adenosylmethionine / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D012436:S-Adenosylmethionine