Specificity of inhibition of muscle glycogen phosphorylase b by flavins.
The inhibition of glycogen phosphorylase b from rabbit skeletal muscles by the derivatives of riboflavin, FMN, FAD, and 2', 3', 4', 5'-tetraacetylriboflavin substituted in positions 6 and 8 of the isoalloxazine part of the flavin molecule is found to be cooperative (the Hill coefficient, h, exceeds 1.0). The modification of the flavin molecule slightly changes the value of the Hill coefficient, but results in the increase of the "half-saturation" concentration [I]0.5.
Klinov
S V
SV
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow.
Kurganov
B I
BI
D000818:Animals; D001665:Binding Sites; D005486:Flavin Mononucleotide / Q000494:pharmacology; D005182:Flavin-Adenine Dinucleotide / Q000494:pharmacology; D005415:Flavins / Q000494:pharmacology*; D007700:Kinetics; D018482:Muscle, Skeletal / Q000201:enzymology*; D006005:Phosphorylases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D011817:Rabbits; D012256:Riboflavin / Q000031:analogs & derivatives / Q000494:pharmacology; D013552:Swine
D005415:Flavins; D005182:Flavin-Adenine Dinucleotide; C058357:2',3',4',5'-tetraacetylriboflavin; D005486:Flavin Mononucleotide; D006005:Phosphorylases; D012256:Riboflavin