[Hexamere purine nucleoside phosphorylase from Escherichia coli K-12. Kinetic analysis and mechanism of reaction].
A kinetic analysis of the phosphorolytic reaction catalyzed by hexameric purine nucleoside phosphorylase II from E. coli K-12 in the presence and absence of reaction products was carried out. The results of the kinetic analysis are consistent with a rapid equilibrium random Bi-Bi mechanism, in which a dead-end ternary (enzyme.purine base.phosphate) complex is formed.
D004926:Escherichia coli / Q000201:enzymology*; D019271:Hypoxanthine; D007042:Hypoxanthines / Q000494:pharmacology; D007288:Inosine / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D010430:Pentosyltransferases / Q000302:isolation & purification*; D010766:Phosphorylation; D011487:Protein Conformation; D011683:Purine-Nucleoside Phosphorylase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D007042:Hypoxanthines; D046911:Macromolecular Substances; D019271:Hypoxanthine; D007288:Inosine; D010430:Pentosyltransferases; D011683:Purine-Nucleoside Phosphorylase
Geksamernaia purinnukleozidfosforilaza II Escherichia coli K-12. Kineticheskiĭ analiz, mekhanizm reaktsii.