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Information on EC 2.3.1.24 - sphingosine N-acyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession A6ZZV7

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IUBMB Comments
Acts on sphingosine or its 2-epimer.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: A6ZZV7
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
ceramide synthase, cers6, cers5, cers4, lass5, ceramide synthase 6, lass6, ceramide synthase 5, sphinganine n-acyltransferase, (dihydro)ceramide synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyltransferase, sphingosine
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ceramide synthetase
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sphingosine acyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:sphingosine N-acyltransferase
Acts on sphingosine or its 2-epimer.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-09-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a fatty acyl-CoA + phytosphingosine
CoA + an N-acylphytosphingosine
show the reaction diagram
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?
acyl-CoA + phytosphingosine
CoA + N-acylphytosphingosine
show the reaction diagram
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?
fatty acyl-CoA + dihydrosphingosine
CoA + an N-acyldihydrosphingosine
show the reaction diagram
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additional information
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Lag1 preferentially synthesizes phytosphingolipids
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fumonisin B1
competitive, a refolding of activation loop during fumonisin binding results in catalytic inhibition
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Lag1 is uniquely required for the establishment of a lateral diffusion barrier in the nuclear envelope, which depends on phytoceramide
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure, binding of inhibitor fumonisin B1 and comparison with structure of Trichoderma guizhouense enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sharma, S.; Ahmed, M.; Akhter, Y.
The revelation of selective sphingolipid pathway inhibition mechanism on fumonisin toxin binding to ceramide synthases in susceptible organisms and survival mechanism in resistant species
Biochimie
149
41-50
2018
Trichoderma guizhouense (A0A1T3CVR0), Trichoderma guizhouense, Saccharomyces cerevisiae (P38703), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Megyeri, M.; Prasad, R.; Volpert, G.; Sliwa-Gonzalez, A.; Haribowo, A.; Aguilera-Romero, A.; Riezman, H.; Barral, Y.; Futerman, A.; Schuldiner, M.
Yeast ceramide synthases, Lag1 and Lac1, have distinct substrate specificity
J. Cell Sci.
132
jcs228411
2019
Saccharomyces cerevisiae
Manually annotated by BRENDA team