ArticleProceedings of the National Academy of Sciences of the United States of America2009
Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 72 citations in OpenAlex.
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- The metal cofactor: stationary or mobile?Applied microbiology and biotechnology · 2024Review
- Specific base catalysis by yeast alcohol dehydrogenase I with substitutions of histidine-48 by glutamate or serine residues in the proton relay system.Chemico-biological interactions · 2023Article
- Aryl-n-hexanamide linked enaminones of usnic acid as promising antimicrobial agents.Molecular diversity · 2023Article
- Substrate Induced Movement of the Metal Cofactor between Active and Resting State.Angewandte Chemie (International ed. in English) · 2022Article
- Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.Angewandte Chemie (International ed. in English) · 2022Article
- Advanced Insights into Catalytic and Structural Features of the Zinc-Dependent Alcohol Dehydrogenase from Thauera aromatica.Chembiochem : a European journal of chemical biology · 2022Article
- Regulatory role of cysteines in (2R, 3R)-butanediol dehydrogenase BdhA of Bacillus velezensis strain GH1-13.Journal of microbiology (Seoul, Korea) · 2022Article
- Structural and Kinetic Insights Into the Molecular Basis of Salt Tolerance of the Short-Chain Glucose-6-Phosphate Dehydrogenase FromFrontiers in microbiology · 2021Article
- New insights into the operative network of FaEO, an enone oxidoreductase from Fragaria x ananassa Duch.Plant molecular biology · 2017Article
- Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
- Structure-guided engineering of Lactococcus lactis alcohol dehydrogenase LlAdhA for improved conversion of isobutyraldehyde to isobutanol.Journal of biotechnology · 2012Article
- Role of conserved glycine in zinc-dependent medium chain dehydrogenase/reductase superfamily.The Journal of biological chemistry · 2012Article
- Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis.Archives of biochemistry and biophysics · 2011Article
- Rational design, synthesis and evaluation of first generation inhibitors of the Giardia lamblia fructose-1,6-biphosphate aldolase.Journal of inorganic biochemistry · 2011Article
- Article
- Characterization of 5-chloro-5-deoxy-D-ribose 1-dehydrogenase in chloroethylmalonyl coenzyme A biosynthesis: substrate and reaction profiling.The Journal of biological chemistry · 2010Article
- Evaluation of the impact of functional diversification on Poaceae, Brassicaceae, Fabaceae, and Pinaceae alcohol dehydrogenase enzymes.Journal of molecular modeling · 2010Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Despite being the subject of intensive investigations, many aspects of the mechanism of the zinc-dependent medium chain alcohol dehydrogenase (MDR) superfamily remain contentious. We have determined the high-resolution structures of a series of binary and ternary complexes of glucose dehydrogenase, an MDR enzyme from Haloferax mediterranei. In stark contrast to the textbook MDR mechanism in which the zinc ion is proposed to remain stationary and attached to a common set of protein ligands, analysis of these structures reveals that in each complex, there are dramatic differences in the nature of the zinc ligation. These changes arise as a direct consequence of linked movements of the zinc ion, a zinc-bound bound water molecule, and the substrate during progression through the reaction. These results provide evidence for the molecular basis of proton traffic during catalysis, a structural explanation for pentacoordinate zinc ion intermediates, a unifying view for the observed patterns of metal ligation in the MDR family, and highlight the importance of dynamic fluctuations at the metal center in changing the electrostatic potential in the active site, thereby influencing the proton traffic and hydride transfer events.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.