Fifty years of lyase and a moment of truth: sphingosine phosphate lyase from discovery to disease.
SGPL1
sphingolipids
sphingosine phosphate lyase insufficiency syndrome
sphingosine-1-phosphate
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:
03 2019
03 2019
Historique:
received:
18
11
2018
revised:
31
12
2018
pubmed:
13
1
2019
medline:
18
6
2020
entrez:
13
1
2019
Statut:
ppublish
Résumé
Sphingosine phosphate lyase (SPL) is the final enzyme in the sphingolipid degradative pathway, catalyzing the irreversible cleavage of long-chain base phosphates (LCBPs) to yield a long-chain aldehyde and ethanolamine phosphate (EP). SPL guards the sole exit point of sphingolipid metabolism. Its inactivation causes product depletion and accumulation of upstream sphingolipid intermediates. The main substrate of the reaction, sphingosine-1-phosphate (S1P), is a bioactive lipid that controls immune-cell trafficking, angiogenesis, cell transformation, and other fundamental processes. The products of the SPL reaction contribute to phospholipid biosynthesis and programmed cell-death activation. The main features of SPL enzyme activity were first described in detail by Stoffel et al. in 1969. The first SPL-encoding gene was cloned from budding yeast in 1997. Reverse and forward genetic strategies led to the rapid identification of other genes in the pathway and their homologs in other species. Genetic manipulation of SPL-encoding genes in model organisms has revealed the contribution of sphingolipid metabolism to development, physiology, and host-pathogen interactions. In 2017, recessive mutations in the human SPL gene
Identifiants
pubmed: 30635364
pii: S0022-2275(20)32608-0
doi: 10.1194/jlr.S091181
pmc: PMC6399507
doi:
Substances chimiques
Phosphates
0
Aldehyde-Lyases
EC 4.1.2.-
sphingosine 1-phosphate lyase (aldolase)
EC 4.1.2.27
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
456-463Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK115669
Pays : United States
Informations de copyright
Copyright © 2019 Saba.
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