ArticleNature chemistry2025
Structural insights into two thiamine diphosphate-dependent enzymes and their synthetic applications in carbon-carbon linkage reactions.
Article in Nature chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- A guide to Direct Pathway Cloning (DiPaC) for natural product discovery.Essays in biochemistry · 2026Review
- C2α-carbanion-protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2-hydroxyacyl-CoA lyase.FEBS open bio · 2026Article
- Discovery of Pyranoquinolone Diterpenoids Biosynthesized through Oxidative Indole Rearrangement and Atypical Terpene Cyclization.Journal of the American Chemical Society · 2026Article
- N-Heterocyclic Carbene (NHC) Catalysis in Enzymatic Organic Synthesis.Coordination chemistry reviews · 2026Article
- A Chemo-Enzymatic Platform for Furanolide Synthesis and Functional Exploration.Journal of the American Chemical Society · 2025Article
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Authors and funding
12 authors.
Funding
Abstract
The α-hydroxy-β-keto acid synthases are thiamine diphosphate-dependent enzymes catalysing carbon-carbon linkage reactions in the biosynthesis of primary metabolites and various secondary metabolites. However, the substrate selectivity and catalytic stereoselectivity of α-hydroxy-β-keto acid synthases are poorly understood, greatly hindering their synthetic application in generating diverse carbon frameworks. We here report the discovery of two new α-hydroxy-β-keto acid synthases CsmA and BbmA, which show different substrate selectivities in catalysing carbon-carbon coupling reactions between two β-keto acids. Four crystal structures of CsmA or BbmA complexed with thiamine diphosphate and their substrates were determined, clearly revealing their structural bases of substrate selectivity and catalytic stereoselectivity. Substrate scope expansion enables us to generate 120 α-hydroxy-β-keto acids together with 240 NaBH
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