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These carbonyl and hydroxyl oxygens have been proposed to facilitate the switch of the methyl group throughout catalysis 16 , 21 , 24 In addition, tyrosine residues within the lysine-binding clefts of SET7/9 (Tyr245 and Tyr305) and DIM-5 (Tyr178) hydrogen-bond to the lysine ε-amino group, aligning it for a methyltransfer with AdoMet (Determine 4b,c ).
Methylation been found on a spread of lysine residues in numerous histones: K4 (utilizing the only-letter amino-acid code for lysine), K9, K27, K36 and K79 in histone H3, K20 in histone H4, K59 within the globular area of histone H4 2 and K26 of histone H1B three A number of proteins accountable for the methylation of particular residues have been characterised, and all however one of these incorporates a SET area