ArticleNature communications2015
Crystallographic and spectroscopic snapshots reveal a dehydrogenase in action.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- A sequence motif enables widespread use of noncanonical redox cofactors in natural enzymes.Nature chemical biology · 2026Article
- Response to "Addressing flaws in the Seq2Topt dataset for the prediction of enzyme optimal temperature".Briefings in bioinformatics · 2026Article
- Addressing flaws in the Seq2Topt dataset for the prediction of enzyme optimal temperature.Briefings in bioinformatics · 2026Article
- Diversity of Aromatic Aldehyde Dehydrogenases in Ceriporiopsis subvermispora: Insights into Fungal Vanillin Metabolism.Applied biochemistry and biotechnology · 2026Article
- α-Amino-β-carboxymuconate-ε-semialdehyde decarboxylase catalyzes enol/keto tautomerization of oxaloacetate.The Journal of biological chemistry · 2024Article
- Double-duty isomerases: a case study of isomerization-coupled enzymatic catalysis.Trends in biochemical sciences · 2024Review
- Characterization of a novel aromatic substrate-processing microcompartment in Actinobacteria.mBio · 2023Article
- Computational Study of Base-Catalyzed Thiohemiacetal Decomposition inThe journal of physical chemistry. B · 2023Article
- Kynurenine Pathway Regulation at Its Critical Junctions with Fluctuation of Tryptophan.Metabolites · 2023Article
- Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.The Journal of biological chemistry · 2019Article
- Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer.Journal of molecular biology · 2019Article
- Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.Redox biology · 2019Review
- NADFEBS letters · 2018Article
- Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism.The Journal of biological chemistry · 2018Article
- The aldehyde dehydrogenase AldA contributes to the hypochlorite defense and is redox-controlled by protein S-bacillithiolation in Staphylococcus aureus.Redox biology · 2018Article
- Combining X-ray and neutron crystallography with spectroscopy.Acta crystallographica. Section D, Structural biology · 2017Article
- A Pitcher-and-Catcher Mechanism Drives Endogenous Substrate Isomerization by a Dehydrogenase in Kynurenine Metabolism.The Journal of biological chemistry · 2016Article
- NADP-Dependent Aldehyde Dehydrogenase from ArchaeonArchaea (Vancouver, B.C.) · 2016Article
- What is the tryptophan kynurenine pathway and why is it important to neurotherapeutics?Expert review of neurotherapeutics · 2015Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Aldehydes are ubiquitous intermediates in metabolic pathways and their innate reactivity can often make them quite unstable. There are several aldehydic intermediates in the metabolic pathway for tryptophan degradation that can decay into neuroactive compounds that have been associated with numerous neurological diseases. An enzyme of this pathway, 2-aminomuconate-6-semialdehyde dehydrogenase, is responsible for 'disarming' the final aldehydic intermediate. Here we show the crystal structures of a bacterial analogue enzyme in five catalytically relevant forms: resting state, one binary and two ternary complexes, and a covalent, thioacyl intermediate. We also report the crystal structures of a tetrahedral, thiohemiacetal intermediate, a thioacyl intermediate and an NAD(+)-bound complex from an active site mutant. These covalent intermediates are characterized by single-crystal and solution-state electronic absorption spectroscopy. The crystal structures reveal that the substrate undergoes an E/Z isomerization at the enzyme active site before an sp(3)-to-sp(2) transition during enzyme-mediated oxidation.
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Registered trials
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.