ArticleNature communications2017
Biomimetic catalytic transformation of toxic α-oxoaldehydes to high-value chiral α-hydroxythioesters using artificial glyoxalase I.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Metabolic Mechanisms in Electroconvulsive Therapy for Schizophrenia: Role, Potential and Future Directions.International journal of molecular sciences · 2026Review
- Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary Systems.Journal of the American Chemical Society · 2021Article
- Oxidative-Antioxidant Imbalance and Impaired Glucose Metabolism in Schizophrenia.Biomolecules · 2020Review
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Authors and funding
4 authors.
Funding
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Abstract
Glyoxalase I plays a critical role in the enzymatic defence against glycation by catalysing the isomerization of hemithioacetal, formed spontaneously from cytotoxic α-oxoaldehydes and glutathione, to (S)-α-hydroxyacylglutathione derivatives. Upon the hydrolysis of the thioesters catalysed by glyoxalase II, inert (S)-α-hydroxy acids, that is, lactic acid, are then produced. Herein, we demonstrate highly enantioselective glyoxalase I mimic catalytic isomerization of in-situ-generated hemithioacetals, providing facile access to both enantiomers of α-hydroxy thioesters. Owing to the flexibility of thioesters, a family of optically pure α-hydroxyamides, which are highly important drug candidates in the pharmaceutical industry, were prepared without any coupling reagents. Similar to real enzymes, the enforced proximity of the catalyst and substrates by the chiral cage in situ formed by the incorporation of potassium salt can enhance the reactivity and efficiently transfer the stereochemical information.
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