[Interaction of glycogen synthase of rabbit skeletal muscles with flavin mononucleotide].
The effect of flavin mononucleotide (FMN) on the activity of the I- and D-forms of rabbit skeletal muscle glycogen synthase has been studied for the first time. FMN has been shown to inhibit in a noncompetitive fashion the both forms of the enzyme, the D-form being more sensitive to the effect of the inhibitor. It has been shown also that glycogen synthase has three different sites involved in the interaction with inhibitors, namely, and active site, an adenyl nucleotide binding site and a FMN binding site. FMN binding has been shown to occur mostly via the isoalloxasine ring.
Sundukov
S Iu
SIu
Solov'eva
G A
GA
D000227:Adenine Nucleotides / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004789:Enzyme Activation; D005486:Flavin Mononucleotide / Q000494:pharmacology*; D006006:Glycogen Synthase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D014530:Uridine Diphosphate / Q000378:metabolism
D000227:Adenine Nucleotides; D014530:Uridine Diphosphate; D005486:Flavin Mononucleotide; D006006:Glycogen Synthase
Vzaimodeĭstvie glikogensintazy skeletnykh myshts krolika s flavinmononukleotidom.