9skm

Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives (CsATase C88S)

spinqualitylabelsall models 9skm, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9skm is a 12 chain structure with sequence from Chromobacterium sphagni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.87Å Ligands: ACT, GOL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Although aromatic formylation reactions are highly valuable from a synthetic perspective, a biocatalytic version has not yet been reported. Here, the cofactor-independent multimeric three-component acyltransferase from Chromobacterium sphagni (CsATase) was identified to enable the nonnatural promiscuous regioselective C-formylation of polyphenolic substrates, especially resorcinol derivatives, and thus extending the reaction scope of acyltransferases. Formylation of 4- and 5-substituted resorcinol derivatives gave access to regioselectively mono-formylated products with up to 99% conversion and up to 74% isolated yield. Formylation of phloroglucinol led to the di-formylated product with 99% conversion, outperforming chemical methods. Structural analysis of CsATase by X-ray crystallography provided insights into its active site. Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives.,Gal L, Rohan S, Zadlo-Dobrowolska A, Hilweg B, Muller J, Tittmann K, Kroutil W Angew Chem Int Ed Engl. 2026 Jan 29:e19387. doi: 10.1002/anie.202519387. PMID:41612625 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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