Ontology highlight
ABSTRACT:
SUBMITTER: Del Rizzo PA
PROVIDER: S-EPMC2951256 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Del Rizzo Paul A PA Couture Jean-François JF Dirk Lynnette M A LM Strunk Bethany S BS Roiko Marijo S MS Brunzelle Joseph S JS Houtz Robert L RL Trievel Raymond C RC
The Journal of biological chemistry 20100801 41
SET domain lysine methyltransferases (KMTs) methylate specific lysine residues in histone and non-histone substrates. These enzymes also display product specificity by catalyzing distinct degrees of methylation of the lysine ε-amino group. To elucidate the molecular mechanism underlying this specificity, we have characterized the Y245A and Y305F mutants of the human KMT SET7/9 (also known as KMT7) that alter its product specificity from a monomethyltransferase to a di- and a trimethyltransferase ...[more]