Use of isotopically labeled substrates reveals kinetic differences between human and bacterial serine palmitoyltransferase.
biosynthesis
mechanism
membrane protein
regulation
sphingolipid
Journal
Journal of lipid research
ISSN: 1539-7262
Titre abrégé: J Lipid Res
Pays: United States
ID NLM: 0376606
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
17
08
2018
revised:
14
02
2019
pubmed:
23
2
2019
medline:
14
8
2020
entrez:
23
2
2019
Statut:
ppublish
Résumé
Isotope labels are frequently used tools to track metabolites through complex biochemical pathways and to discern the mechanisms of enzyme-catalyzed reactions. Isotopically labeled l-serine is often used to monitor the activity of the first enzyme in sphingolipid biosynthesis, serine palmitoyltransferase (SPT), as well as labeling downstream cellular metabolites. Intrigued by the effect that isotope labels may be having on SPT catalysis, we characterized the impact of different l-serine isotopologues on the catalytic activity of recombinant SPT isozymes from humans and the bacterium
Identifiants
pubmed: 30792183
pii: S0022-2275(20)32265-3
doi: 10.1194/jlr.M089367
pmc: PMC6495160
pii:
doi:
Substances chimiques
Serine
452VLY9402
Serine C-Palmitoyltransferase
EC 2.3.1.50
Types de publication
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
953-962Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M003493/1
Pays : United Kingdom
Commentaires et corrections
Type : ErratumIn
Informations de copyright
Copyright © 2019 Harrison et al.
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