Binding of vitamin B2 and its coenzyme forms by muscle glycogen phosphorylase b.
Binding of vitamin B2 and its coenzyme forms by glycogen phosphorylase b was studied by sedimentation velocity and sedimentation equilibrium methods. Microscopic dissociation constants for complexes of the enzyme with riboflavin, FMN and FAD were found to be 12.5, 6.8 and 18.1 microM, respectively (0.1 M KCl, pH 6.8, 20 degrees C). We revealed also that glucose 1-phosphate, glycogen and AMP decreased the affinity of the enzyme for FMN.
D000249:Adenosine Monophosphate / Q000378:metabolism; D000818:Animals; D003067:Coenzymes / Q000378:metabolism*; D005486:Flavin Mononucleotide / Q000378:metabolism; D005958:Glucosephosphates / Q000378:metabolism; D006003:Glycogen / Q000378:metabolism; D007700:Kinetics; D009132:Muscles / Q000378:metabolism*; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011817:Rabbits; D012256:Riboflavin / Q000378:metabolism*; D014461:Ultracentrifugation
D003067:Coenzymes; D005958:Glucosephosphates; D000249:Adenosine Monophosphate; D005486:Flavin Mononucleotide; D006003:Glycogen; D010763:Phosphorylase b; D006005:Phosphorylases; D012256:Riboflavin