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Literature summary for 2.1.1.72 extracted from

  • Marzabal, S.; DuBois, S.; Thielking, V.; Cano, A.; Eritja, R.; Guschlbauer, W.
    Dam methylase from Escherichia coli: kinetic studies using modified DNA oligomers: hemimethylated substrates (1995), Nucleic Acids Res., 23, 3648-3655.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information Km-values fpr 14-mers and various substituted duplexes Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + DNA adenine canonical 14mers and various substituted duplexes. Non-selfcomplementary tetradecamer duplex d[GCCGGATCTAGACG]*d[CGTCTAGATCCGGC] containing the hemimethylated GATC target sequence on one or the other strand and modifications in the GATC target sequence of the complementary strands. Large differences in DNA methylation of duplexes containing single dI or dG substitutions of the Dam recognition site are observed compared with the canonical substrate, if the substitution involves the top strand, on the G-C rich side. Substitution in either strand by uracil or 5-ethyluracil result in small perturbation of the methylation patterns. When 2,6-diamino-purine replaces the adenine to be methylated, small but significant methylation is observed Escherichia coli S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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