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| Collectively, the crystallographic studies of SET7/9 and DIM-5 bound to histone H3 peptides have offered a framework for understanding the histone lysine specificity of various SET-domain enzymes. | |||
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| With accumulating proof that these modifications are usually not histone particular, a new nomenclature has been advocated for extra generic names for these enzymes 1 The enzymes that add or remove the methylation mark on lysine residues at the moment are named lysine methyltransferases (KMTs) and lysine demethylases (KDMs), respectively, for their broad or doubtlessly broad spectra of protein substrates. | |||
| High-throughput strategies are needed to determine proteome-large lysine methylation. | |||
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| In particular, as in DIM-5, these two enzymes depend on residues carboxy-terminal to the SET area for the formation of lysine channel, however they accomplish that by packing of an α helix, relatively than a metallic center, onto the lively site. | |||
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