Pre-Steady-State Analysis of ATP Hydrolysis by Saccharomyces cerevisiae DNA Topoisomerase II. 2. Kinetic Mechanism for the Sequential Hydrolysis of Two ATP
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...
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Published in | Biochemistry (Easton) Vol. 37; no. 20; pp. 7299 - 7312 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
19.05.1998
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Abstract | 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) sequential ATP hydrolysis or (2) simultaneous hydrolysis of both ATP. Here, we present results that are consistent only with topoisomerase II hydrolyzing its two bound ATP sequentially. Additionally, these results indicate that the products of the first hydrolysis are released from the enzyme before the second ATP is hydrolyzed. Release of products from both the first and second hydrolyses contributes to the rate-determining process. The proposed mechanism for ATP hydrolysis by topoisomerase II is complex, having nine rate constants. To calculate values for each of these rate constants, a technique of kinetic parameter estimation was developed. This technique involved using singular perturbation theory in order to estimate rate constants, and consequently identify kinetic steps following the rate-determining step. |
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AbstractList | 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) sequential ATP hydrolysis or (2) simultaneous hydrolysis of both ATP. Here, we present results that are consistent only with topoisomerase II hydrolyzing its two bound ATP sequentially. Additionally, these results indicate that the products of the first hydrolysis are released from the enzyme before the second ATP is hydrolyzed. Release of products from both the first and second hydrolyses contributes to the rate-determining process. The proposed mechanism for ATP hydrolysis by topoisomerase II is complex, having nine rate constants. To calculate values for each of these rate constants, a technique of kinetic parameter estimation was developed. This technique involved using singular perturbation theory in order to estimate rate constants, and consequently identify kinetic steps following the rate-determining step. |
Author | Harkins, Timothy T Lewis, Timothy J Lindsley, Janet E |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9585544$$D View this record in MEDLINE/PubMed |
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Notes | This work was supported by Grant GM51194 from the National Institutes of Health, and in part by a grant from the Lucille P. Markey Charitable Trust. T.T.H. was supported in part by NCI Training Grant CA09602-06. T.J.L. was supported in part by NFS Grant DMS-9626334. J.E.L. was supported in part by ACS Grant JFRA-622. istex:539307E329C0D77D22613AF38B1CB2B580B71E3E ark:/67375/TPS-K6HQS9V3-M ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
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SubjectTerms | 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 |
Title | Pre-Steady-State Analysis of ATP Hydrolysis by Saccharomyces cerevisiae DNA Topoisomerase II. 2. Kinetic Mechanism for the Sequential Hydrolysis of Two ATP |
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