ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis.
ATP-citrate lyase
acetyl coenzyme A (acetyl-CoA)
citrate synthase
coenzyme A (CoA)
enzyme mechanism
metabolism
protein assembly
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:
03 05 2019
03 05 2019
Historique:
received:
12
11
2018
revised:
05
03
2019
pubmed:
17
3
2019
medline:
8
1
2020
entrez:
17
3
2019
Statut:
ppublish
Résumé
ATP-citrate lyase (ACLY) is a major source of nucleocytosolic acetyl-CoA, a fundamental building block of carbon metabolism in eukaryotes. ACLY is aberrantly regulated in many cancers, cardiovascular disease, and metabolic disorders. However, the molecular mechanisms determining ACLY activity and function are unclear. To this end, we investigated the role of the uncharacterized ACLY C-terminal citrate synthase homology domain in the mechanism of acetyl-CoA formation. Using recombinant, purified ACLY and a suite of biochemical and biophysical approaches, including analytical ultracentrifugation, dynamic light scattering, and thermal stability assays, we demonstrated that the C terminus maintains ACLY tetramerization, a conserved and essential quaternary structure
Identifiants
pubmed: 30877197
pii: S0021-9258(20)36804-6
doi: 10.1074/jbc.RA118.006685
pmc: PMC6509486
doi:
Substances chimiques
ATP Citrate (pro-S)-Lyase
EC 2.3.3.8
Coenzyme A
SAA04E81UX
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
7259-7268Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118090
Pays : United States
Organisme : NCI NIH HHS
ID : F31 CA217070
Pays : United States
Organisme : NCI NIH HHS
ID : K00 CA212455
Pays : United States
Organisme : NCI NIH HHS
ID : F31 CA189559
Pays : United States
Organisme : NIA NIH HHS
ID : P01 AG031862
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA228339
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008275
Pays : United States
Informations de copyright
© 2019 Bazilevsky et al.
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