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Information on EC 2.3.1.297 - very-long-chain ceramide synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38703
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2.3.1.297 very-long-chain ceramide synthaseIUBMB Comments
This entry describes ceramide synthase enzymes that are specific for very-long-chain fatty acyl-CoA substrates. The two isoforms from yeast and the plant LOH1 and LOH3 isoforms transfer 24:0 and 26:0 acyl chains preferentially and use phytosphingosine as the preferred sphingoid base. The mammalian CERS2 isoform is specific for acyl donors of 20-26 carbons, which can be saturated or unsaturated. The mammalian CERS3 isoform catalyses this activity, but has a broader substrate range and also catalyses the activity of EC 2.3.1.298, ultra-long-chain ceramide synthase. Both mammalian enzymes can use multiple sphingoid bases, including sphinganine, sphingosine, and phytosphingosine.
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Word Map
- 2.3.1.297
- sphingolipids
- sphingomyelins
- dihydroceramide
-
cers1-6
- elovl1
- pnpla1
- cyp4f22
- alox12b
-
sdr9c7
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nipal4
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abca12
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cerss
- aloxe3
- diagnostics
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
a very-long-chain fatty acyl-CoA
+
=
a very-long-chain ceramide
+
Synonyms
cers2, lass2, cers3, ceramide synthase 2, ceramide synthase 3, lass4, lass3, longevity assurance homologue 2, lag13, lag11, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CerS3
-
-
-
-
LAC1
-
-
-
-
LAG1
-
-
-
-
LASS3
-
-
-
-
LOH1
-
-
-
-
LOH3
-
-
-
-
mammalian ceramide synthase 2
-
-
-
-
sphingoid base N-very-long-chain fatty acyl-coA transferase
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
very-long-chain fatty acyl-coA:sphingoid base N-acyltransferase
This entry describes ceramide synthase enzymes that are specific for very-long-chain fatty acyl-CoA substrates. The two isoforms from yeast and the plant LOH1 and LOH3 isoforms transfer 24:0 and 26:0 acyl chains preferentially and use phytosphingosine as the preferred sphingoid base. The mammalian CERS2 isoform is specific for acyl donors of 20-26 carbons, which can be saturated or unsaturated. The mammalian CERS3 isoform catalyses this activity, but has a broader substrate range and also catalyses the activity of EC 2.3.1.298, ultra-long-chain ceramide synthase. Both mammalian enzymes can use multiple sphingoid bases, including sphinganine, sphingosine, and phytosphingosine.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Lac1p and Lag1p are integral membrane proteins with six to eight predicted transmembrane domains. Co-subunit Lip1 is also an integral membrane protein, with one transmembrane domain. Its short N-terminal part is cytoplasmic and not required for ceramide synthesis. Analysis of membrane topology of the heterotrimer for ceramide synthase catalytic activity, overview
transmembrane topology of topology of the Lag1p and Lac1p subunits in yeast using insertion of glycosylation sites and factor Xa-cleavage sites in the loops between the predicted transmembrane segments, method, overview. The N- and C-termini of the proteins are in the cytoplasm and eight putative membrane-spanning domains are identified in Lag1p and Lac1p. The conserved Lag motif, potentially containing the active site, is most likely embedded in the membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
the conserved Lag motif, potentially containing the active site, is most likely embedded in the membrane. Histidine and aspartic acid residues in the Lag motif are essential for the function of Lag1p in vivo
physiological function
Lag1p, Lac1p and Lip1p comprise the ceramide synthase. Lag1p and Lac1p are subunits of the acyl-CoA-dependent ceramide synthase. The other essential component of the ceramide synthase, Lip1p, which forms a heteromeric complex with Lac1p and Lag1p. Lip1p is required for ceramide synthesis in vivo and in vitro
physiological function
proteins Lag1p, Lac1p, and Lip1p are required for ceramide synthase activity in Saccharomyces cerevisiae
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
subunits Lac1p, Lag1p, and Lip1p
additional information
Lag1p, Lac1p and Lip1p comprise the ceramide synthase. Lag1p/Lac1p interacting protein, 28 kDa, Lip1p is an essential component of the ceramide synthase, which forms a heteromeric complex with Lac1p and Lag1p. Lip1p is required for ceramide synthesis in vivo and in vitro. It is possible that Lip1p is modified by O-linked glycosylation. Its short, highly charged N-terminus is cytoplasmic and dispensible for ceramide synthase activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
topology study of Lag1p and Lac1p using insertion of glycosylation sites and fXa (factor Xa)-cleavage sites in the loops between the predicted transmembrane segments, hydropathy profiles of Lag1p and Lac1p and positions of fusion insertions, method, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 3420fold subunits from isolated digitonin-treated membranes by solubilization with 1% Triton X-100 and affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes LAC1, LAG1, and LIP1. LIP1 DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of all three subunits as N-terminally FLAG- or HA-tagged proteins in Saccharomyces cerevisiae strains
genes LAG1, LAC1 and LIP1, encodes the three subunits of the hetereotrimeric enzyme, sequence comparisons, recombinant expression of wild-type and point/insertion mutant FLAG- and/or c-Myc-tagged subunits in Saccharomyces cerevisiae strains, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kageyama-Yahara, N.; Riezman, H.
Transmembrane topology of ceramide synthase in yeast
Biochem. J.
398
585-593
2006
Saccharomyces cerevisiae (P28496 AND P38703 AND Q03579), Saccharomyces cerevisiae RH382 (P28496 AND P38703 AND Q03579)
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