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Peptidic Partial Bisubstrates as Inhibitors of the Protein Arginine N ‐Methyltransferases
Author(s) -
't Hart Peter,
Lakowski Ted M.,
Thomas Dylan,
Frankel Adam,
Martin Nathaniel I.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100074
Subject(s) - methyltransferase , sn2 reaction , arginine , methionine , biochemistry , chemistry , cofactor , stereochemistry , enzyme , methylation , computational biology , biology , amino acid , dna
Double player: Protein arginine N ‐methyltransferases (PRMTs) employ a general S N 2‐like bisubstrate reaction mechanism with the cofactor S ‐adenosyl‐ L ‐methionine (AdoMet) to methylate L ‐arginine residues in target proteins. In this study, new peptidic partial bisubstrate analogues, bearing a minimal AdoMet fragment (highlighted in yellow) were prepared and evaluated as PRMT inhibitors.