Racemization of the substrate and product by serine palmitoyltransferase from Sphingobacterium multivorum yields two enantiomers of the product from D-serine.
PLP-dependent enzyme
X-ray crystallography
crystal structure
racemization
serine palmitoyltransferase
sphingolipid
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:
05 Feb 2024
05 Feb 2024
Historique:
received:
24
12
2023
revised:
25
01
2024
accepted:
02
02
2024
medline:
8
2
2024
pubmed:
8
2
2024
entrez:
7
2
2024
Statut:
aheadofprint
Résumé
Serine palmitoyltransferase (SPT) catalyzes the pyridoxal-5'-phosphate (PLP)-dependent decarboxylative condensation of L-serine and palmitoyl-CoA to form 3-ketodihydrosphingosine (KDS). Although SPT was shown to synthesize corresponding products from amino acids other than L-serine, it is still arguable whether SPT catalyzes the reaction with D-serine, which is a question of biological importance. Using high substrate and enzyme concentrations, KDS was detected after the incubation of SPT from Sphingobacterium multivorum with D-serine and palmitoyl-CoA. Furthermore, the KDS comprised equal amounts of 2S- and 2R-isomers.
Identifiants
pubmed: 38325740
pii: S0021-9258(24)00104-2
doi: 10.1016/j.jbc.2024.105728
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105728Informations de copyright
Copyright © 2024 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.