Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/130442
Author(s): Reis, J.P.A
Figueiredo, S.A.C
Sousa, M.L
Leão, P.N.
Title: BrtB is an O-alkylating enzyme that generates fatty acid-bartoloside esters
Publisher: Nature Communications
Issue Date: 2020
Abstract: 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).
Subject: 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
URI: https://hdl.handle.net/10216/130442
Source: Nature Communications volume 11, Article number: 1458 (2020)
Document Type: Artigo em Revista Científica Internacional
Rights: openAccess
Appears in Collections:CIIMAR - Artigo em Revista Científica Internacional

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