Model studies of enzymatic NH2-terminal acetylation of porteins with des-Nalpha1-acetyl-alpha-melanotropin as a substrate.
The present study describes the acetylation by an enzyme present in calf lens of a synthetic tridecapeptide [analogous to alpha-melanotropin (alpha-melanocyte stimulating hormone) but lacking the naturally occurring NH2-terminal acetyl group: des-Nalpha1-Ac-alpha-melanotropin]. The reaction is specific for the alpha-amino group of the NH2-terminal amino acid. The minimum length required for the substrate to become acetylated appears to be a sequence of five to eight amino acid residues. Modification of the internal lysine decreases the incorporation of acetate, irrespective of the size of the blocking group.
D000085:Acetates / Q000378:metabolism*; D000107:Acetylation; D000595:Amino Acid Sequence; D002474:Cell-Free System; D007908:Lens, Crystalline / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D009074:Melanocyte-Stimulating Hormones / Q000032:analysis / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D012694:Serine / Q000378:metabolism; D013329:Structure-Activity Relationship
D000085:Acetates; D010455:Peptides; D012694:Serine; D009074:Melanocyte-Stimulating Hormones; D008239:Lysine