ArticleNature chemical biology2011
Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism.
Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
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- Synthesis of biologically active cefpodoxime and vanillin-based schiff base metal complexes with the detailed biological evaluations.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Unravelling Enzymatic Features in a Supramolecular Iridium Catalyst by Computational Calculations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Mapping Enzyme Landscapes by Time-Resolved Crystallography with Synchrotron and X-Ray Free Electron Laser Light.Annual review of biophysics · 2022Review
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- Structural basis for antibiotic action of the BNature chemical biology · 2020Article
- How the Destabilization of a Reaction Intermediate Affects Enzymatic Efficiency: The Case of Human Transketolase.ACS catalysis · 2020Article
- Biological and catalytic potential of sustainable low and high valent metal-Schiff base sulfonate salicylidene pincer complexes.RSC advances · 2019Article
- Characterizing posttranslational modifications in prokaryotic metabolism using a multiscale workflow.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Biocatalytic Aldol Addition of Simple Aliphatic Nucleophiles to Hydroxyaldehydes.ACS catalysis · 2018Article
- Complete Switch of Reaction Specificity of an Aldolase by Directed Evolution In Vitro: Synthesis of Generic Aliphatic Aldol Products.Angewandte Chemie (International ed. in English) · 2018Article
- Acyclic and cyclic imines and their metal complexes: recent progress in biomaterials and corrosion applications.RSC advances · 2018Review
- Fabrication of SbRSC advances · 2018Article
- Substrate Distortion and the Catalytic Reaction Mechanism of 5-Carboxyvanillate Decarboxylase.Journal of the American Chemical Society · 2016Article
- Identification of allosteric disulfides from prestress analysis.Biophysical journal · 2014Article
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
- Adherence to Bürgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Sub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate.Nature chemistry · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We examined the catalytic cycle of transaldolase (TAL) from Thermoplasma acidophilum by cryocrystallography and were able to structurally characterize--for the first time, to our knowledge--different genuine TAL reaction intermediates. These include the Schiff base adducts formed between the catalytic lysine and the donor ketose substrates fructose-6-phosphate and sedoheptulose-7-phosphate as well as the Michaelis complex with acceptor aldose erythrose-4-phosphate. These structural snapshots necessitate a revision of the accepted reaction mechanism with respect to functional roles of active site residues, and they further reveal fundamental insights into the general structural features of enzymatic Schiff base intermediates and the role of conformational dynamics in enzyme catalysis, substrate binding and discrimination. A nonplanar arrangement of the substituents around the Schiff base double bond was observed, suggesting that a structurally encoded reactant-state destabilization is a driving force of catalysis. Protein dynamics and the intrinsic hydrogen-bonding pattern appear to be crucial for selective recognition and binding of ketose as first substrate.
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