Prenylation of aromatic amino acids and plant phenolics by an aromatic prenyltransferase from Rasamsonia emersonii.
Alkylation
Biocatalysis
DMATS
Fungal PT
Tryptophan
aPT
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
18 Jul 2024
18 Jul 2024
Historique:
received:
20
02
2024
accepted:
08
07
2024
revised:
17
06
2024
medline:
18
7
2024
pubmed:
18
7
2024
entrez:
18
7
2024
Statut:
epublish
Résumé
Dimethylallyl tryptophan synthases (DMATSs) are aromatic prenyltransferases that catalyze the transfer of a prenyl moiety from a donor to an aromatic acceptor during the biosynthesis of microbial secondary metabolites. Due to their broad substrate scope, DMATSs are anticipated as biotechnological tools for producing bioactive prenylated aromatic compounds. Our study explored the substrate scope and product profile of a recombinant RePT, a novel DMATS from the thermophilic fungus Rasamsonia emersonii. Among a variety of aromatic substrates, RePT showed the highest substrate conversion for L-tryptophan and L-tyrosine (> 90%), yielding two mono-prenylated products in both cases. Nine phenolics from diverse phenolic subclasses were notably converted (> 10%), of which the stilbenes oxyresveratrol, piceatannol, pinostilbene, and resveratrol were the best acceptors (37-55% conversion). The position of prenylation was determined using NMR spectroscopy or annotated using MS
Identifiants
pubmed: 39023782
doi: 10.1007/s00253-024-13254-8
pii: 10.1007/s00253-024-13254-8
doi:
Substances chimiques
Amino Acids, Aromatic
0
Dimethylallyltranstransferase
EC 2.5.1.1
Phenols
0
Stilbenes
0
Tryptophan
8DUH1N11BX
Recombinant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
421Informations de copyright
© 2024. The Author(s).
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