ArticleProceedings of the National Academy of Sciences of the United States of America2008
The associative nature of adenylyl transfer catalyzed by T4 DNA ligase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 22 citations in OpenAlex.
- Light-Induced Uncaging for Time-Resolved Observations of Biochemical Reactions by MAS NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Theoretical Studies on Mechanism of Inactivation of Kanamycin A by 4'-O-Nucleotidyltransferase.Frontiers in chemistry · 2018Article
- DNA ligase-mediated translation of DNA into densely functionalized nucleic acid polymers.Journal of the American Chemical Society · 2013Article
- Kinetic characterization of single strand break ligation in duplex DNA by T4 DNA ligase.The Journal of biological chemistry · 2011Article
- Interfacial enzyme kinetics of a membrane bound kinase analyzed by real-time MAS-NMR.Nature chemical biology · 2011Article
- NMR data do not implicate a phosphorane in the T4 DNA ligase reaction.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
DNA ligase seals nicks in dsDNA using chemical energy of the phosphoanhydride bond in ATP or NAD(+) and assistance of a divalent metal cofactor Mg(2+). Molecular details of ligase catalysis are essential for understanding the mechanism of metal-promoted phosphoryl transfer reactions in the living cell responsible for a wide range of processes, e.g., DNA replication and transcription, signaling and differentiation, energy coupling and metabolism. Here we report a single-turnover (31)P solid-state NMR study of adenylyl transfer catalyzed by DNA ligase from bacteriophage T4. Formation of a high-energy covalent ligase-nucleotide complex is triggered in situ by the photo release of caged Mg(2+), and sequentially formed intermediates are monitored by NMR. Analyses of reaction kinetics and chemical-shift changes indicate that the pentacoordinated phosphorane intermediate builds up to 35% of the total reacting species after 4-5 h of reaction. This is direct experimental evidence of the associative nature of adenylyl transfer catalyzed by DNA ligase. NMR spectroscopy in rotating solids is introduced as an analytical tool for recording molecular movies of reaction processes. Presented work pioneers a promising direction in structural studies of biochemical transformations.
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