Structure and Catalytic Mechanism of a Bacterial Friedel-Crafts Acylase.

ABSTRACT: C-C bond-forming reactions are key transformations for setting up the carbon frameworks of organic compounds. In this context, 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 multicomponent acyltransferase from Pseudomonas protegens (PpATase) catalyzes such Friedel-Crafts C-acylation of phenolic substrates in aqueous solution, reaching up to >99 % conversion without the need for CoA-activated reagents. We determined X-ray crystal structures of the native and ligand-bound complexes. This multimeric enzyme consists of three subunits: PhlA, PhlB, and PhlC, arranged in a Phl(A₂ C₂ )₂ B₄ composition. The structure of a reaction intermediate ob

SUBMITTER: Pavkov-Keller T 

PROVIDER: S-EPMC6392133 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature