Dam Methyltransferase from Escherichia coli: Kinetic Studies Using Modified DNA Oligomers: Nonmethylated Substrates
Author:
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm.1997.378.5.407/pdf
Reference40 articles.
1. Base-base mismatches. Thermodynamics of double helix formation for dCA3XA3G + dCT3YT3G (X, Y = A,C,G,D
2. Preferential Site-specific Hemimethylation of GATC Sites in pBR322 DNA by Dam Methyltransferase from Escherichia coli
3. The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli
4. Allosteric and catalytic binding of S-adenosylmethionine to Escherichia coli DNA adenine methyltransferase monitored by 3H NMR.
5. The effects of base analogue substitutions on the methylation by the EcoRI modification methylase of octadeoxyribonucleotides containing modified EcoRI recognition sequences.
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