[Mechanism of reaction catalyzed by RNA-ligase from bacteriophage T4].
The dissociation constants of the complexes of RNA-ligase with acceptors, donors and the adenylylated donor A(5')ppAp have been determined on the basis of the inhibition of ATP-pyrophosphate exchange reaction. The dissociation constants of the complexes of the enzyme with "poor" acceptors (oligouridilates) have been shown to be slightly different from those with "good" acceptors (oligoadenylates). The dependence of the reaction velocity of the formation of ligation products on the concentration of acceptors (pA)4, (pU)4 and the adenylylated donor A(5)ppAp has been studied. On the basis of the data obtained the conclusion about the random addition mechanism has been drawn. The reaction takes place in the steady-state conditions in the case of (pA)4 and in the equilibrium conditions--in the case of (pU)4.
D000255:Adenosine Triphosphate / Q000378:metabolism; D002384:Catalysis; D011756:Diphosphates / Q000378:metabolism; D007700:Kinetics; D008954:Models, Biological; D011061:Poly A / Q000378:metabolism; D011118:Polynucleotide Ligases / Q000378:metabolism*; D011130:RNA Ligase (ATP) / Q000378:metabolism*; D013604:T-Phages / Q000201:enzymology*
D011756:Diphosphates; D011061:Poly A; D000255:Adenosine Triphosphate; D011118:Polynucleotide Ligases; D011130:RNA Ligase (ATP)
Izuchenie mekhanizma reaktsii, kataliziruemoĭ RNK-ligazoĭ bakteriofaga T4.