Binding capacities of various analogues of S-adenosyl-L-homocysteine to protein methyltransferase II from human erythrocytes.
A series of analogues of S-adenosyl-L-homocysteine, modified mainly in the amino acid portion of the molecule, have been synthesized. All were found to be competitive inhibitors of protein methyltransferase II from human erythrocytes. S-adenosyl-L-homocysteine remains however by far the most effective inhibitor of the methylase.
D004912:Erythrocytes / Q000201:enzymology*; D006710:Homocysteine / Q000031:analogs & derivatives*; D006801:Humans; D011485:Protein Binding; D011496:Protein Methyltransferases / Q000097:blood*; D011497:Protein O-Methyltransferase / Q000097:blood*; D012435:S-Adenosylhomocysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D013329:Structure-Activity Relationship
D006710:Homocysteine; D012435:S-Adenosylhomocysteine; D011496:Protein Methyltransferases; D011497:Protein O-Methyltransferase