Discovery and structural characterization of a thermostable bacterial monoamine oxidase.
FAD
flavoenzyme
monoamine oxidase
n-alkylamines
n-heptylamine
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
09 Oct 2023
09 Oct 2023
Historique:
revised:
01
09
2023
received:
22
06
2023
accepted:
29
09
2023
pubmed:
10
10
2023
medline:
10
10
2023
entrez:
10
10
2023
Statut:
aheadofprint
Résumé
Monoamine oxidases (MAOs) are pivotal regulators of neurotransmitters in mammals, while microbial MAOs have been shown to be valuable biocatalysts for enantioselective synthesis of pharmaceutical compounds or precursors thereof. To extend the knowledge of how MAOs function at the molecular level and in order to provide more biocatalytic tools, we set out to identify and study a robust bacterial variant: a MAO from the thermophile Thermoanaerobacterales bacterium (MAO
Banques de données
RefSeq
['MBO2502335.1']
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : EU#x2010;H2020#x2010;FNR
ID : OXIPRO Grant 101000607
Organisme : PNRR MUR
ID : NODES ECS00000036
Informations de copyright
© 2023 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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