ArticleThe Journal of biological chemistry2013
Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
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- Assembly and engineering of BioBricks to develop an efficient NADH regeneration system.Applied and environmental microbiology · 2025Article
- Ion-combination specific effects driving the enzymatic activity of halophilic alcohol dehydrogenase 2 fromRSC sustainability · 2024Article
- Temperature-dependent hydrogen deuterium exchange shows impact of analog binding on adenosine deaminase flexibility but not embedded thermal networks.The Journal of biological chemistry · 2022Article
- Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts.Current opinion in structural biology · 2022Review
- Identification of Thermal Conduits That Link the Protein-Water Interface to the Active Site Loop and Catalytic Base in Enolase.Journal of the American Chemical Society · 2021Article
- Enzyme dynamics: Looking beyond a single structure.ChemCatChem · 2020Article
- Structure and Dynamics of a Thermostable Alcohol Dehydrogenase from the Antarctic PsychrophileACS omega · 2020Article
- Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catecholProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Oscillatory Active-site Motions Correlate with Kinetic Isotope Effects in Formate Dehydrogenase.ACS catalysis · 2019Article
- Moving Through Barriers in Science and Life.Annual review of biochemistry · 2019Article
- A Biophysical Perspective on Enzyme Catalysis.Biochemistry · 2019Article
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
- Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State.Angewandte Chemie (International ed. in English) · 2018Article
- Contribution of buried distal amino acid residues in horse liver alcohol dehydrogenase to structure and catalysis.Protein science : a publication of the Protein Society · 2018Article
- Activity-Related Microsecond Dynamics Revealed by Temperature-Jump Förster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase.Journal of the American Chemical Society · 2018Article
- Origins of Enzyme Catalysis: Experimental Findings for C-H Activation, New Models, and Their Relevance to Prevailing Theoretical Constructs.Journal of the American Chemical Society · 2017Article
- Calcium-driven DNA synthesis by a high-fidelity DNA polymerase.Nucleic acids research · 2017Article
- Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling.ACS central science · 2017Article
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3 authors at 1 institution in 1 country.
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Abstract
A tetrameric thermophilic alcohol dehydrogenase from Bacillus stearothermophilus (ht-ADH) has been mutated at an aromatic side chain in the active site (Trp-87). The ht-W87A mutation results in a loss of the Arrhenius break seen at 30 °C for the wild-type enzyme and an increase in cold lability that is attributed to destabilization of the active tetrameric form. Kinetic isotope effects (KIEs) are nearly temperature-independent over the experimental temperature range, and similar in magnitude to those measured above 30 °C for the wild-type enzyme. This suggests that the rigidification in the wild-type enzyme below 30 °C does not occur for ht-W87A. A mutation at the dimer-dimer interface in a thermolabile psychrophilic homologue of ht-ADH, ps-A25Y, leads to a more thermostable enzyme and a change in the rate-determining step at low temperature. The reciprocal mutation in ht-ADH, ht-Y25A, results in kinetic behavior similar to that of W87A. Collectively, the results indicate that flexibility at the active site is intimately connected to a subunit interaction 20 Å away. The convex Arrhenius curves previously reported for ht-ADH (Kohen, A., Cannio, R., Bartolucci, S., and Klinman, J. P. (1999) Nature 399, 496-499) are proposed to arise, at least in part, from a change in subunit interactions that rigidifies the substrate-binding domain below 30 °C, and impedes the ability of the enzyme to sample the catalytically relevant conformational landscape. These results implicate an evolutionarily conserved, long-range network of dynamical communication that controls C-H activation in the prokaryotic alcohol dehydrogenases.
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