title: [Substrate specificity of glycogen synthase from rabbit skeletal muscles].
abstract: Nitrous bases were shown to play an essential role in the specificity of active and adenyl nucleotide binding sites. Pyrimidine base determines the substrate specificity of rabbit skeletal muscle glycogen synthase; a crucial role in this process is ascribed to the lactam fragment of the pyrimidine cycle. The 2-oxo group was also shown to be involved in substrate binding. The adenyl nucleotide binding site interacts only with 6-aminopurine derivatives. A negative interaction was found between the enzyme active center and the adenyl nucleotide binding site.
authors.forename: S Iu
authors.initials: SIu
authors.lastname: Sundukov
authors.forename: G A
authors.initials: GA
authors.lastname: Solov'eva
mesh_terms: D000227:Adenine Nucleotides / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D006006:Glycogen Synthase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007290:Inosine Diphosphate / Q000378:metabolism; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D013379:Substrate Specificity; D014530:Uridine Diphosphate / Q000378:metabolism
chemical_list: D000227:Adenine Nucleotides; D014530:Uridine Diphosphate; D007290:Inosine Diphosphate; D006006:Glycogen Synthase
vernacular_title: O substratnoĭ spetsifichnosti glikogensintazy skeletnykh myshts krolika.