BrtB is an O-alkylating enzyme that generates fatty acid-bartoloside esters

• Autor(a) principal: Reis, J.P.A
• Data de Publicação: 2020
• Outros Autores: Figueiredo, S.A.C, Sousa, M.L, Leão, P.N.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
• Texto Completo: https://hdl.handle.net/10216/130442
• topic: alcohol; carbon; carboxylic acid; enzyme; fatty acid bartoloside ester; fatty acid ester; halide; nucleophile; oxygen; protein brtb; unclassified drug; alkylating agent; bacterial protein; ester; fatty acid; polycyclic aromatic hydrocarbon; transferase; catalysis; catalyst; chemical bonding; chemical compound; chemical reaction; enzyme; enzyme activity; Article; catalysis; chemical binding; chemical bond; controlled study; esterification; gene cluster; nonhuman; nucleophilicity; synthesis; alkylation; enzymology; genetics; metabolism; multigene family; procedures; Synechocystis; Alkylating Agents; Alkylation; Bacterial Proteins; Chemistry Techniques, Synthetic; Esterification; Esters; Fatty Acids; Multigene Family; Polycyclic Aromatic Hydrocarbons; Synechocystis; Transferases

Esterification reactions are central to many aspects of industrial and biological chemistry. The formation of carboxyesters typically occurs through nucleophilic attack of an alcohol onto the carboxylate carbon. Under certain conditions employed in organic synthesis, the carboxylate nucleophile can be alkylated to generate esters from alkyl halides, but this reaction has only been observed transiently in enzymatic chemistry. Here, we report a carboxylate alkylating enzyme – BrtB – that catalyzes O-C bond formation between free fatty acids of varying chain length and the secondary alkyl halide moieties found in the bartolosides. Guided by this reactivity, we uncovered a variety of natural fatty acid-bartoloside esters, previously unrecognized products of the bartoloside biosynthetic gene cluster. © 2020, The Author(s).