Free ferrous ions sustain activity of mammalian stearoyl-CoA desaturase-1.
diiron
electron paramagnetic resonance (EPR)
labile iron
lipid desaturation
metalloenzyme
stearoyl-CoA desaturase (SCD)
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:
07 2023
07 2023
Historique:
received:
14
04
2023
revised:
26
05
2023
accepted:
05
06
2023
medline:
31
7
2023
pubmed:
9
6
2023
entrez:
8
6
2023
Statut:
ppublish
Résumé
Mammalian stearoyl-CoA desaturase-1 (SCD1) introduces a double-bond to a saturated long-chain fatty acid in a reaction catalyzed by a diiron center. The diiron center is well-coordinated by conserved histidine residues and is thought to remain with the enzyme. However, we find here that SCD1 progressively loses its activity during catalysis and becomes fully inactive after about nine turnovers. Further studies show that the inactivation of SCD1 is due to the loss of an iron (Fe) ion in the diiron center and that the addition of free ferrous ions (Fe
Identifiants
pubmed: 37290533
pii: S0021-9258(23)01925-7
doi: 10.1016/j.jbc.2023.104897
pmc: PMC10359943
pii:
doi:
Substances chimiques
Fatty Acids
0
Iron
E1UOL152H7
Stearoyl-CoA Desaturase
EC 1.14.19.1
Cations, Divalent
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
104897Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK122784
Pays : United States
Commentaires et corrections
Type : UpdateOf
Informations de copyright
Copyright © 2023 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.