Interaction of aliphatic amines with glycogen phosphorylase.
A number of aliphatic amines was shown to stimulate AMP-dependent activity of phosphorylase b. The extent of stimulation depends on the molecular structure of amines. For linear amines, the longer the linear chain, the greater the stimulation observed. High concentrations of amines were able to induce a small activation of phosphorylase b in the absence of AMP. Kinetic studies of phosphorylase b indicated that the presence of n-hexylamine (a) results in lowering Km values for AMP and glucose 1-phosphate, (b) increases maximal velocity of the enzyme, and (c) modifies the glucose 6-phosphate, ATP, caffeine, and glucose binding sites of the enzyme by increasing the inhibition constants for these inhibitors. In contrast, the activity of phosphorylase b' is not altered by n-hexylamine. This fact suggests the possibility that amines interact with the N-terminal tail of phosphorylase b chain.
D000249:Adenosine Monophosphate / Q000378:metabolism; D000588:Amines / Q000494:pharmacology*; D000818:Animals; D002384:Catalysis; D066298:In Vitro Techniques; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D010125:Ostreidae / Q000378:metabolism; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011817:Rabbits
D000588:Amines; D000249:Adenosine Monophosphate; D010763:Phosphorylase b; D006005:Phosphorylases