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Publication Abstract from PubMed

C-C bond forming reactions are key transformations to set up the carbon framework of organic molecules. In this context, the Friedel-Crafts acylation is commonly used for the synthesis of aryl ketones, which are common motifs in many fine chemicals and natural products. A bacterial multi-component acyltransferase from Pseudomonas protegens (PpATase) catalyzes such a Friedel-Crafts C-acylation of phenolic substrates in aqueous solution reaching up to >99% conversion without the need of CoA-activated reagents. We determined x-ray crystal structures of the native and ligand-bound complex. This multimeric enzyme consists of three subunits - PhlA, PhlB and PhlC which are arranged in a Phl(A2C2)2B4 composition. The structure of a reaction intermediate obtained from crystals soaked with the natural substrate monoacetylphloroglucinol together with site-directed mutagenesis studies revealed that only residues from the PhlC subunits are involved in the acyl transfer reaction, with Cys88 very likely playing a significant role during catalysis. These structural and mechanistic insights form the basis of further enzyme engineering efforts towards enhancing the substrate scope of this enzyme.

Structure and catalytic mechanism of a bacterial Friedel-Crafts acylase.,Pavkov-Keller T, Schmidt NG, Zadlo-Dobrowolska A, Kroutil W, Gruber K Chembiochem. 2018 Oct 14. doi: 10.1002/cbic.201800462. PMID:30318713^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.