Mechanism of Biocatalytic Friedel-Crafts Acylation by Acyltransferase from <i>Pseudomonas protegens</i>.

ABSTRACT: Acyltransferases isolated from Pseudomonas protegens (PpATase) and Pseudomonas fluorescens (PfATase) have recently been reported to catalyze the Friedel-Crafts acylation, providing a biological version of this classical organic reaction. These enzymes catalyze the cofactor-independent acylation of monoacetylphloroglucinol (MAPG) to diacetylphloroglucinol (DAPG) and phloroglucinol (PG) and have been demonstrated to have a wide substrate scope, making them valuable for potential applications in biocatalysis. Herein, we present a detailed reaction mechanism of PpATase on the basis of quantum chemical calculations, employing a large model of the active site. The proposed mechanism is consistent with available kinetics, mutagenesis, and structural data. The ro

SUBMITTER: Sheng X 

PROVIDER: S-EPMC6945686 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature