Pre-Steady-State Analysis of ATP Hydrolysis by Saccharomyces cerevisiae DNA Topoisomerase II. 2. Kinetic Mechanism for the Sequential Hydrolysis of Two ATP

• Published in: Biochemistry (Easton) Vol. 37; no. 20; pp. 7299 - 7312
• Main Authors: Harkins, Timothy T, Lewis, Timothy J, Lindsley, Janet E
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 19.05.1998
• Subjects: Adenosine Diphosphate - metabolism; Adenosine Triphosphate - chemistry; Adenosine Triphosphate - metabolism; Animals; Binding Sites; DNA Topoisomerases, Type II - chemistry; DNA Topoisomerases, Type II - metabolism; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Models, Chemical; Phosphates - metabolism; Rabbits; Saccharomyces cerevisiae; Saccharomyces cerevisiae - enzymology; Salmon; Time Factors

In the preceding paper, we showed that DNA topoisomerase II from Saccharomyces cerevisiae binds two ATP and rapidly hydrolyzes at least one of them before encountering a slow step in the reaction mechanism. These data are potentially consistent with two different types of reaction pathways:  (1) seq...