The DNA (cytosine-5) methyltransferases

Nucleic Acids Res. 1994 Jan 11;22(1):1-10. doi: 10.1093/nar/22.1.1.


The m5C-MTases form a closely-knit family of enzymes in which common amino acid sequence motifs almost certainly translate into common structural and functional elements. These common elements are located predominantly in a single structural domain that performs the chemistry of the reaction. Sequence-specific DNA recognition is accomplished by a separate domain that contains recognition elements not seen in other structures. This, combined with the novel and unexpected mechanistic feature of trapping a base out of the DNA helix, makes the m5C-MTases an intriguing class of enzymes for further study. The reaction pathway has suddenly become more complicated because of the base-flipping and much remains to be learned about the DNA recognition elements in the family members for which structural information is not yet available.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • DNA-Cytosine Methylases* / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • S-Adenosylmethionine / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity


  • S-Adenosylmethionine
  • DNA-Cytosine Methylases