Pyridoxal phosphate-dependent conformational states of glycogen phosphorylase as probed by interconverting enzymes.
The interaction between pyridoxal 5'-phosphate and the convertible serine of glycogen phosphorylase has been investigated by using: specific interconverting enzymes, phosphorylase kinase and phosphorylase phosphatase; effectors, glucose and glucose 6-phosphate; and a protein kinase and trypsin. Both phosphorylase kinase and phosphorylase phosphatase utilized the native protein while having little influence on the apoprotein. Removal of a peptide containing the critical serine residue gave phosphorylase b' from which the pyridoxal 5'-phosphate in phosphorylase has an important effect on enzymic interconversion.
D001051:Apoenzymes / Q000378:metabolism; D005947:Glucose / Q000494:pharmacology; D005958:Glucosephosphates / Q000494:pharmacology; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010764:Phosphorylase Kinase / Q000378:metabolism; D006005:Phosphorylases / Q000378:metabolism*; D011487:Protein Conformation; D011494:Protein Kinases / Q000494:pharmacology; D011732:Pyridoxal Phosphate / Q000494:pharmacology*; D012694:Serine; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000494:pharmacology
D001051:Apoenzymes; D005958:Glucosephosphates; D012694:Serine; D011732:Pyridoxal Phosphate; D006005:Phosphorylases; D011494:Protein Kinases; D010764:Phosphorylase Kinase; D010744:Phosphoric Monoester Hydrolases; D014357:Trypsin; D005947:Glucose