Regioselective O-acetylation of various glucosides catalyzed by Escherichia coli maltose O-acetyltransferase.
Alkaloidal glucoside
Escherichia coli
Flavonoid glucoside
Iridoid glucoside
Maltose O-acetyltransferase
O-acetylation
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
07
06
2023
accepted:
11
09
2023
revised:
05
09
2023
medline:
13
11
2023
pubmed:
20
9
2023
entrez:
20
9
2023
Statut:
ppublish
Résumé
Escherichia coli, a well-known prokaryotic organism, has been widely employed as a versatile host for heterologous overexpression of proteins/biocatalysts and the production of pharmaceutically important intermediates/small molecules. However, some E. coli endogenous enzymes showing substrate promiscuity may disturb the heterologous metabolic flux, which will result in the reduction of substrates, intermediates, and target products. Here we reported an unexpected E. coli-catalyzed regioselective O-acetylation of various glucosides. The regioselectively O-acetylated products, 6'-O-acetyl-loganin and 6'-O-acetyl-loganic acid, were obtained and characterized from the enzymatic reaction in which the supernatants of E. coli expressing either CaCYP72A565 and CaCPR, the key enzymes involved in camptothecin biosynthesis, or empty vector were used as catalyst and loganin and loganic acid as independent substrate. An alkaloidal glucoside strictosamide was converted into the regioselectively O-acetylated product 6'-O-acetyl-strictosamide, implying substrate promiscuity of the E. coli-catalyzed O-acetylation reaction. Furthermore, 8 glucosides, including 5 iridoid glucosides and 3 flavonoid glucosides, were successfully converted into the regioselectively O-acetylated products by E. coli, indicating the wide substrate range for the unexpected E. coli-catalyzed O-acetylation. E. coli maltose O-acetyltransferase was demonstrated to be responsible for the mentioned regioselective O-acetylation at the 6-OH of the glucopyranosyl group of multiple classes of natural product glucosides through candidate acetyltransferase-encoding gene analysis, gene knock-out, gene complementation, and the relevant enzymatic reaction activity assays. The present study not only provides an efficient biocatalyst for regioselective O-acetylation but also notifies cautions for metabolic engineering and synthetic biology applications in E. coli. KEY POINTS: • 6-OH of glucosyl of multiple glucosides was regioselectively O-acetylated by E. coli. • Endogenous EcMAT is responsible for the regioselective O-acetylation reaction.
Identifiants
pubmed: 37728626
doi: 10.1007/s00253-023-12790-z
pii: 10.1007/s00253-023-12790-z
doi:
Substances chimiques
loganin
H7WJ16Q93C
Glucosides
0
loganic acid
22255-40-9
Maltose
69-79-4
Acetyltransferases
EC 2.3.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7031-7042Subventions
Organisme : National Natural Science Foundation of China
ID : 22177112
Organisme : Natural Science Foundation of Sichuan Province
ID : 2022NSFC0616
Organisme : Chinese Academy of Sciences
ID : KFJ-BRP-008
Organisme : CAS Key Laboratory of Environmental and Applied Microbiology & Environmental Microbiology Key Laboratory of Sichuan Province
ID : KLEAMCAS202301
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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