Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer.
CntA
EPR
carnitine oxygenase
gut microbiota
inhibitor
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Historique:
received:
15
09
2020
revised:
27
10
2020
accepted:
06
11
2020
pubmed:
8
11
2020
medline:
28
8
2021
entrez:
7
11
2020
Statut:
ppublish
Résumé
Microbial metabolism of carnitine to trimethylamine (TMA) in the gut can accelerate atherosclerosis and heart disease, and these TMA-producing enzymes are therefore important drug targets. Here, we report the first structures of the carnitine oxygenase CntA, an enzyme of the Rieske oxygenase family. CntA exists in a head-to-tail α
Identifiants
pubmed: 33158989
pii: S0021-9258(20)00024-1
doi: 10.1074/jbc.RA120.016019
pmc: PMC7948474
pii:
doi:
Substances chimiques
Mixed Function Oxygenases
EC 1.-
Carnitine
S7UI8SM58A
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100038Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
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