Isotopic labelings for mechanistic studies.
Absolute configuration determination
Biosynthesis
Carbocation chemistry
Enzyme mechanisms
Isotopic labeling
NMR spectroscopy
Oligoprenyl pyrophosphates
Reprotonation
Stereoselective synthesis
Terpene synthases
Journal
Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271
Informations de publication
Date de publication:
2024
2024
Historique:
medline:
29
6
2024
pubmed:
29
6
2024
entrez:
28
6
2024
Statut:
ppublish
Résumé
The intricate mechanisms in the biosynthesis of terpenes belong to the most challenging problems in natural product chemistry. Methods to address these problems include the structure-based site-directed mutagenesis of terpene synthases, computational approaches, and isotopic labeling experiments. The latter approach has a long tradition in biosynthesis studies and has recently experienced a revival, after genome sequencing enabled rapid access to biosynthetic genes and enzymes. Today, this allows for a combined approach in which isotopically labeled substrates can be incubated with recombinant terpene synthases. These clearly defined reaction setups can give detailed mechanistic insights into the reactions catalyzed by terpene synthases, and recent developments have substantially deepened our understanding of terpene biosynthesis. This chapter will discuss the state of the art and introduce some of the most important methods that make use of isotopic labelings in mechanistic studies on terpene synthases.
Identifiants
pubmed: 38942502
pii: S0076-6879(24)00014-4
doi: 10.1016/bs.mie.2024.01.011
pii:
doi:
Substances chimiques
Alkyl and Aryl Transferases
EC 2.5.-
terpene synthase
EC 2.5.1.-
Terpenes
0
Recombinant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
163-186Informations de copyright
Copyright © 2024. Published by Elsevier Inc.