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Literature summary extracted from

  • Thielking, V.; Du Bois, S.; Eritja, R.; Guschlbauer, W.
    Dam methyltransferase from Escherichia coli. Kinetic studies using modified DNA oligomers. Nonmethylated substrates (1997), Biol. Chem., 378, 407-415.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.72 additional information
-
 additional information turnover numbers for the canonical 14-mer duplex and various substituted duplexes Escherichia coli

Organism

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

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.72 S-adenosyl-L-methionine + DNA adenine non-self-complementary tetradecanucleotide duplexes that contain the GATC target sequence. The enzyme is rather tolerant to base modification, binding of the enzyme is inversely proportional to the thermodynamic stability of the duplex in the ternary complex Escherichia coli S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.72 additional information
-
 additional information turnover numbers for the canonical 14-mer duplex and various substituted duplexes Escherichia coli