ArticleThe FEBS journal2014
On the catalytic mechanism and stereospecificity of Escherichia coli L-threonine aldolase.
Article in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 78 citations in OpenAlex.
- Article
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- Efficient production of glycine from glucose via a two-stage biosynthetic strategy.Microbial cell factories · 2026Article
- Enhanced Stereochemical Analysis of β‑Diastereomeric Amino Acids with Variants of Marfey's Reagent.ACS omega · 2025Article
- Profiling of Diverse Pyridoxal-5'-Phosphate Dependent Enzymes Reveals Promiscuous Aldolase Activity with (2-Azaaryl)methanamines.Journal of the American Chemical Society · 2025Article
- From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the BacteriumBiomolecules · 2024Article
- A recombinant L-threonine aldolase with high catalytic efficiency for the asymmetric synthesis of L-threo-phenylserine and L-threo-4-fluorophenylserine.Biotechnology letters · 2024Article
- Biocatalytic asymmetric aldol addition into unactivated ketones.Nature chemistry · 2024Article
- Synergistic Photoenzymatic Catalysis Enables Synthesis ofJournal of the American Chemical Society · 2024Article
- One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse.Nature communications · 2024Article
- Structure of pyridoxal 5'-phosphate-bound D-threonine aldolase from Chlamydomonas reinhardtii.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Comprehensive screening strategy coupled with structure-guided engineering of l-threonine aldolase fromFrontiers in bioengineering and biotechnology · 2023Article
- Biocatalytic synthesis of non-standard amino acids by a decarboxylative aldol reaction.Nature catalysis · 2022Article
- Scalable and Selective β-Hydroxy-α-Amino Acid Synthesis Catalyzed by Promiscuous l-Threonine Transaldolase ObiH.Chembiochem : a European journal of chemical biology · 2022Article
- Chemoenzymatic synthesis of 3-ethyl-2,5-dimethylpyrazine by L-threonine 3-dehydrogenase and 2-amino-3-ketobutyrate CoA ligase/L-threonine aldolase.Communications chemistry · 2021Article
- Heterologous gene expression and characterization of two serine hydroxymethyltransferases from Thermoplasma acidophilum.Extremophiles : life under extreme conditions · 2021Article
- l-Threonine Transaldolase Activity Is Enabled by a Persistent Catalytic Intermediate.ACS chemical biology · 2021Article
- L-Carnitine Production Through Biosensor-Guided Construction of theFrontiers in bioengineering and biotechnology · 2021Article
- An Engineered Escherichia coli Strain with Synthetic Metabolism for in-Cell Production of Translationally Active Methionine Derivatives.Chembiochem : a European journal of chemical biology · 2020Article
- Comparison of L-Threonine Aldolase Variants in the Aldol and Retro-Aldol Reactions.Frontiers in bioengineering and biotechnology · 2019Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
L-threonine aldolases (L-TAs) represent a family of homologous pyridoxal 5'-phosphate-dependent enzymes found in bacteria and fungi, and catalyse the reversible cleavage of several L-3-hydroxy-α-amino acids. L-TAs have great biotechnological potential, as they catalyse the formation of carbon-carbon bonds, and therefore may be exploited for the bioorganic synthesis of L-3-hydroxyamino acids that are biologically active or constitute building blocks for pharmaceutical molecules. Many L-TAs, showing different stereospecificity towards the Cβ configuration, have been isolated. Because of their potential to carry out diastereoselective syntheses, L-TAs have been subjected to structural, functional and mechanistic studies. Nevertheless, their catalytic mechanism and the structural bases of their stereospecificity have not been elucidated. In this study, we have determined the crystal structure of low-specificity L-TA from Escherichia coli at 2.2-Å resolution, in the unliganded form and cocrystallized with L-serine and L-threonine. Furthermore, several active site mutants have been functionally characterized in order to elucidate the reaction mechanism and the molecular bases of stereospecificity. No active site catalytic residue was revealed, and a structural water molecule was assumed to act as the catalytic base in the retro-aldol cleavage reaction. Interestingly, the very large active site opening of E. coli L-TA suggests that much larger molecules than L-threonine isomers may be easily accommodated, and L-TAs may actually have diverse physiological functions in different organisms. Substrate recognition and reaction specificity seem to be guided by the overall microenvironment that surrounds the substrate at the enzyme active site, rather than by one ore more specific residues.
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