[HTML][HTML] Kinetic mechanism of human DNA ligase I reveals magnesium-dependent changes in the rate-limiting step that compromise ligation efficiency
MR Taylor, JA Conrad, D Wahl, PJ O'Brien - Journal of Biological Chemistry, 2011 - ASBMB
DNA ligase I (LIG1) catalyzes the ligation of single-strand breaks to complete DNA
replication and repair. The energy of ATP is used to form a new phosphodiester bond in
DNA via a reaction mechanism that involves three distinct chemical steps: enzyme
adenylylation, adenylyl transfer to DNA, and nick sealing. We used steady state and pre-
steady state kinetics to characterize the minimal mechanism for DNA ligation catalyzed by
human LIG1. The ATP dependence of the reaction indicates that LIG1 requires multiple Mg …
replication and repair. The energy of ATP is used to form a new phosphodiester bond in
DNA via a reaction mechanism that involves three distinct chemical steps: enzyme
adenylylation, adenylyl transfer to DNA, and nick sealing. We used steady state and pre-
steady state kinetics to characterize the minimal mechanism for DNA ligation catalyzed by
human LIG1. The ATP dependence of the reaction indicates that LIG1 requires multiple Mg …