Adaptive laboratory evolution recruits the promiscuity of succinate semialdehyde dehydrogenase to repair different metabolic deficiencies.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
15 Oct 2024
15 Oct 2024
Historique:
received:
15
04
2024
accepted:
03
10
2024
medline:
16
10
2024
pubmed:
16
10
2024
entrez:
15
10
2024
Statut:
epublish
Résumé
Promiscuous enzymes often serve as the starting point for the evolution of novel functions. Yet, the extent to which the promiscuity of an individual enzyme can be harnessed several times independently for different purposes during evolution is poorly reported. Here, we present a case study illustrating how NAD(P)
Identifiants
pubmed: 39406738
doi: 10.1038/s41467-024-53156-x
pii: 10.1038/s41467-024-53156-x
doi:
Substances chimiques
Succinate-Semialdehyde Dehydrogenase
EC 1.2.1.24
Pyridoxal Phosphate
5V5IOJ8338
Escherichia coli Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
8898Subventions
Organisme : EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020)
ID : 862087
Organisme : EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020)
ID : 862087
Informations de copyright
© 2024. The Author(s).
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