AI Article Synopsis
- The study investigates how human histone lysine methyltransferases catalyze the methylation of histones with lysine and its structurally modified analogues (E)-alkene, (Z)-alkene, and alkyne.
- Both G9a and GLP methyltransferases exhibit a higher efficiency for regular lysine, with a decreasing ability for the rigid analogues in the order of K > KE > KZ ∼ Kyne.
- In contrast, the monomethyltransferase SETD8 only supports the methylation of lysine and its (E)-alkene analogue, showing limited activity with the others.
Article Abstract
We report synthesis and enzymatic assays on human histone lysine methyltransferase catalysed methylation of histones that possess lysine and its geometrically constrained analogues containing rigid (E)-alkene (KE), (Z)-alkene (KZ) and alkyne (Kyne) moieties. Methyltransferases G9a and GLP do have a capacity to catalyse methylation in the order K ≫ KE > KZ ∼ Kyne, whereas monomethyltransferase SETD8 catalyses only methylation of K and KE.
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| http://dx.doi.org/10.1039/c9cc09098c | DOI Listing |
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