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. 1994 Jan 11;22(1):1–10. doi: 10.1093/nar/22.1.1

The DNA (cytosine-5) methyltransferases.

S Kumar 1, X Cheng 1, S Klimasauskas 1, S Mi 1, J Posfai 1, R J Roberts 1, G G Wilson 1
PMCID: PMC307737  PMID: 8127644

Abstract

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.

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Selected References

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