Effects of carnosine and anserine on muscle and non-muscle phosphorylases.
Rabbit muscle phosphorylases a and b are activated by carnosine, whereas potato and yeast phosphorylases are inhibited at the same concentration of dipeptide. Rabbit muscle phosphorylase a is activated by anserine whereas the b form enzyme and the potato and yeast enzymes are inhibited by the dipeptide. The dipeptides affect the Vmax values for the enzymes rather than the substrate Km values. Kinetic analysis suggested that, for rabbit muscle phosphorylase, both dipeptides compete for occupancy of the same binding site(s) on the enzyme.
D000818:Animals; D000861:Anserine / Q000494:pharmacology*; D002336:Carnosine / Q000494:pharmacology*; D004151:Dipeptides / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D006005:Phosphorylases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010944:Plants / Q000201:enzymology; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D004151:Dipeptides; D002336:Carnosine; D006005:Phosphorylases; D000861:Anserine