title: Exploring the origin of the catalytic power and product specificity of SET domain protein methyltransferase.
abstract: Herein, we used computer simulation to evaluate the free energy activation barriers of the first and second methyl transfer for native SET8 PKMT and its Y334F mutant. The results suggest that the origin of SET8 catalytic power is mainly due to electrostatic preorganization.
authors.affiliation: Faculdade de Biotecnologia e Laboratório de Planejamento e Desenvolvimento de Fármacos, Universidade Federal do Pará, 66075-110, Belém, PA, Brazil. lameira@ufpa.br.
authors.forename: A H
authors.initials: AH
authors.lastname: Lima
authors.forename: C N
authors.initials: CN
authors.lastname: Alves
authors.forename: R
authors.initials: R
authors.lastname: Prasad
authors.forename: J
authors.initials: J
authors.lastname: Lameira
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D003062:Codon; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D055672:Static Electricity; D013379:Substrate Specificity
chemical_list: D003062:Codon; D011495:Histone-Lysine N-Methyltransferase; C470730:KMT5A protein, human