ArticleApplied microbiology and biotechnology2020
An unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactions.
Article in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Enhanced Stereochemical Analysis of β‑Diastereomeric Amino Acids with Variants of Marfey's Reagent.ACS omega · 2025Article
- Recent advances in enzymatic carbon-carbon bond formation.RSC advances · 2024Review
- Discovery of L-threonine transaldolases for enhanced biosynthesis of beta-hydroxylated amino acids.Communications biology · 2023Article
- Fluorinated Protein and Peptide Materials for Biomedical Applications.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Biocatalytic synthesis of 2-fluoro-3-hydroxypropionic acid.Frontiers in bioengineering and biotechnology · 2022Article
- Enzymatic synthesis of fluorinated compounds.Applied microbiology and biotechnology · 2021Review
- Genomic scanning enabling discovery of a new antibacterial bicyclic carbamate-containing alkaloid.Synthetic and systems biotechnology · 2021Article
- l-Threonine Transaldolase Activity Is Enabled by a Persistent Catalytic Intermediate.ACS chemical biology · 2021Article
- Discovery of New Antibacterial Accramycins from a Genetic Variant of the Soil Bacterium,Biomolecules · 2020Article
- Identification of 5-Fluoro-5-Deoxy-Ribulose as a Shunt Fluorometabolite inBiomolecules · 2020Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
β-Hydroxy-α-amino acids (βH-AAs) are key components of many bioactive molecules as well as exist as specialised metabolites. Among these βH-AAs, 4-fluorothreonine (4-FT) is the only naturally occurring fluorinated AA discovered thus far. Here we report overexpression and biochemical characterisation of 4-fluorothreonine transaldolase from Streptomyces sp. MA37 (FTaseMA), a homologue of FTase previously identified in the biosynthesis of 4-FT in S. cattleya. FTaseMA displays considerable substrate plasticity to generate 4-FT as well as other β-hydroxy-α-amino acids with various functionalities at C4 position, giving the prospect of new chemo-enzymatic applications. The enzyme has a hybrid of two catalytic domains, serine hydroxymethyltransferase (S) and aldolase (A). Site-directed mutagenesis allowed the identification of the key residues of FTases, suggesting that the active site of A domain has a historical reminiscent feature in metal-dependent aldolases. Elemental analysis demonstrated that FTaseMA is indeed a Zn
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