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We therefore initiated a comprehensive phylogenetic screen for enzymes that may be capable of deaminating 5-methylcytosine to thymine.
Activation-induced cytidine deaminase has also been shown to be capable of deaminating 5mC and is expressed in pluripotent tissues, including mouse oocytes [ 28].
AID has been shown to be capable of deaminating methyl C to T. Therefore, we propose that AID is likely responsible for the mutation of meC to T at CpG sites in early B cells.
In our search to identify candidate enzymes that would be capable of deaminating 5-methylcytosine to thymine, we assumed that these enzymes would be quite similar in structure and sequence to the cytosine deaminase from E. coli.
So far, AID and A3A, both of which are single-domain deaminases, are the only APOBECs reported to be capable of deaminating methylcytosine (mC), with A3A being much more active than other APOBECs in catalysing this reaction in vitro [ 35– 40].
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