Determination of sites in rabbit muscle glycogen phosphorylase b modified by an adenosine 5'-monophosphate analog, N6-p-bromoacetaminobenzyladenosine-5'-phosphate.
To identify the residues modified by radioactive N6-p-bromoacetaminobenzyladenosine-5'-phosphate in phosphorylase b, the peptic peptides of the modified enzyme were purified. Two radioactive peptides were isolated, each of which had a cysteine residue modified. The cysteine residue involved in the AMP site was determined to be cystein-317 and the other eactive cysteine residue was cysteine-171.
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives*; D000494:Allosteric Regulation; D000495:Allosteric Site; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003545:Cysteine / Q000032:analysis; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification; D010763:Phosphorylase b; D006005:Phosphorylases; D011485:Protein Binding; D011817:Rabbits
D000596:Amino Acids; D010446:Peptide Fragments; D000249:Adenosine Monophosphate; D010763:Phosphorylase b; D006005:Phosphorylases; D003545:Cysteine