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Literature summary for 2.1.1.37 extracted from

  • Zhou, H.; Purdy, M.M.; Dahlquist, F.W.; Reich, N.O.
    The recognition pathway for the DNA cytosine methyltransferase M.HhaI (2009), Biochemistry, 48, 7807-7816.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DNA + S-adenosyl-L-methionine Haemophilus haemolyticus
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DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
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?

Organism

Organism UniProt Comment Textmining
Haemophilus haemolyticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + S-adenosyl-L-methionine
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Haemophilus haemolyticus DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
-
?
DNA + S-adenosyl-L-methionine cytosine DNA methyltransferase M.HhaI modifies the internal cytosine within its cognate recognition site 5'-GCGC-3'. Binding of either unmethylated or hemimethylated cognate DNA to the cofactor-bound binary complex leads to dramatic changes in the 1H-15N correlation spectrum, analysis of hemimethylated and methylated, cognate and noncognate substrate binding , detailed overview Haemophilus haemolyticus DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
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?
additional information reorganization of an essential catalytic loop, residues 80-100, is regulated by sequence-specific protein-DNA interactions, DNA-dependent positioning of the catalytic loop Haemophilus haemolyticus ?
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?

Synonyms

Synonyms Comment Organism
DNA cytosine methyltransferase
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Haemophilus haemolyticus
M.HhaI
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Haemophilus haemolyticus

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine binding of either unmethylated or hemimethylated cognate DNA to the cofactor-bound binary complex leads to dramatic changes in the 1H-15N correlation spectrum Haemophilus haemolyticus