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Literature summary for 2.1.1.37 extracted from

  • Hermann, A.; Goyal, R.; Jeltsch, A.
    The Dnmt1 DNA-(cytosine-C5)-methyltransferase methylates DNA processively with high preference for hemimethylated target sites (2004), J. Biol. Chem., 279, 48350-48359.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + DNA Mus musculus major enzyme in maintenance of the pattern of DNA methylation after DNA replication S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
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Organism

Organism UniProt Comment Textmining
Mus musculus P13864
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + DNA major enzyme in maintenance of the pattern of DNA methylation after DNA replication Mus musculus S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
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S-adenosyl-L-methionine + DNA methylates DNA processively with high preference for hemimethylated target sites. Dnmt1 methylates a hemimethylated 958-mer substrate in a highly processive reaction. Fully methylated and unmethylated CG sites do not inhibit processive methylation of the DNA. Unmethylated sites embedded in a hemimethylated context are modified at an approximately 24fold reduced rate. Completely unmodified DNA is methylated even more slowly. Dnmt1 is not able to methylate hemimethylated CG sites on different strands of the DNA in a processive manner, indicating that Dnmt1 keeps its orientation with respect to the DNA while methylating the CG sites on one strand of the DNA Mus musculus S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
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Synonyms

Synonyms Comment Organism
Dnmt1 DNA-(cytosine-C5)-methyltransferase
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Mus musculus