ArticleNature chemistry2013
Sub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate.
Article in Nature chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 87 citations in OpenAlex.
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- Structural and Computational Insights into Transketolase-like 1 (TKTL-1): Distinction from TKT and Implications for Cancer Metabolism and Therapeutic Targeting.Molecules (Basel, Switzerland) · 2025Article
- An efficient and flexible approach for local distortion: distortion distribution analysis enabled by fragmentation.Chemical science · 2025Article
- Aldehyde-based Activation of C2α-lactylthiamin Diphosphate Decarboxylation on Bacterial 1-deoxy-d-xylulose 5-phosphate Synthase.Chembiochem : a European journal of chemical biology · 2024Article
- Structural Snapshots ofACS catalysis · 2024Article
- Disruption of an Active Site Network Leads to Activation of C2α-Lactylthiamin Diphosphate on the Antibacterial Target 1-Deoxy-d-xylulose-5-phosphate Synthase.Biochemistry · 2024Article
- Posttranslational Acylations of the Rat Brain Transketolase Discriminate the Enzyme Responses to Inhibitors of ThDP-Dependent Enzymes or Thiamine Transport.International journal of molecular sciences · 2024Article
- New Role of Water in Transketolase Catalysis.International journal of molecular sciences · 2023Article
- Unravelling Enzymatic Features in a Supramolecular Iridium Catalyst by Computational Calculations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Demystifying DPP III Catalyzed Peptide Hydrolysis-Computational Study of the Complete Catalytic Cycle of Human DPP III Catalyzed Tynorphin Hydrolysis.International journal of molecular sciences · 2022Article
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- Heme-binding enables allosteric modulation in an ancient TIM-barrel glycosidase.Nature communications · 2021Article
- Low barrier hydrogen bonds in protein structure and function.Biochimica et biophysica acta. Proteins and proteomics · 2021Review
- Assessing the Thiamine Diphosphate Dependent Pyruvate Dehydrogenase E1 Subunit for Carboligation Reactions with Aliphatic Ketoacids.International journal of molecular sciences · 2020Article
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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
- A 'Split-Gene' Transketolase From the Hyper-Thermophilic BacteriumFrontiers in microbiology · 2020Article
- Low-barrier hydrogen bonds in enzyme cooperativity.Nature · 2019Article
- The human transketolase-like proteins TKTL1 and TKTL2 are bona fide transketolases.BMC structural biology · 2019Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is recognized widely that enzymes promote reactions by providing a pathway that proceeds through a transition state of lower energy. In principle, further rate enhancements could be achieved if intermediates are prevented from relaxing to their lowest energy state, and thereby reduce the barrier to the subsequent transition state. Here, we report sub-ångström-resolution crystal structures of genuine covalent reaction intermediates of transketolase. These structures reveal a pronounced out-of-plane distortion of over 20° for the covalent bond that links cofactor and substrate, and a specific elongation of the scissile substrate carbon-carbon bond (d > 1.6 Å). To achieve these distortions, the protein's conformation appears to prevent relaxation of a substrate-cofactor intermediate. The results implicate a reduced barrier to the subsequent step that is consistent with an intermediate of raised energy and leads to a more efficient overall process.
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