Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases.
Journal
Chemical communications (Cambridge, England)
ISSN: 1364-548X
Titre abrégé: Chem Commun (Camb)
Pays: England
ID NLM: 9610838
Informations de publication
Date de publication:
10 Mar 2020
10 Mar 2020
Historique:
pubmed:
13
2
2020
medline:
25
3
2020
entrez:
13
2
2020
Statut:
ppublish
Résumé
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.
Substances chimiques
Alkenes
0
Alkynes
0
Histone-Lysine N-Methyltransferase
EC 2.1.1.43
Lysine
K3Z4F929H6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM