9SKH
Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives
Summary for 9SKH
| Entry DOI | 10.2210/pdb9skh/pdb |
| Descriptor | 2,4-diacetylphloroglucinol biosynthesis protein, ZINC ION, ... (5 entities in total) |
| Functional Keywords | c-formylation of phenolic substrates, transferase |
| Biological source | Chromobacterium sphagni More |
| Total number of polymer chains | 12 |
| Total formula weight | 389934.89 |
| Authors | Gal, L.,Rohan, S.,Tittmann, K.,Kroutil, W. (deposition date: 2025-09-02, release date: 2026-02-18, Last modification date: 2026-03-18) |
| Primary citation | Gal, L.,Rohan, S.,Zadlo-Dobrowolska, A.,Hilweg, B.,Muller, J.,Tittmann, K.,Kroutil, W. Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives. Angew.Chem.Int.Ed.Engl., 65:e19387-e19387, 2026 Cited by PubMed Abstract: 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. PubMed: 41612625DOI: 10.1002/anie.202519387 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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