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Enzyme Nomenclature
Information on EC 2.3.1.291 - sphingoid base N-palmitoyltransferase and Organism(s) Mus musculus and UniProt Accession Q9D6K9
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2.3.1.291 sphingoid base N-palmitoyltransferaseIUBMB Comments
Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 5 (CERS5) is specific for palmitoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CerS5
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LASS5
-
-
-
-
mammalian ceramide synthase 5
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-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA:sphingoid base N-palmitoyltransferase
Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 5 (CERS5) is specific for palmitoyl-CoA as the acyl donor. It 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
myristoyl-CoA + a sphingoid base
N-(myristoyl)-sphingoid base + CoA
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-
-
?
palmitoyl-CoA + a sphingoid base
an N-(palmitoyl)-sphingoid base + CoA
-
-
-
?
stearoyl-CoA + a sphingoid base
an N-(stearoyl)-sphingoid base + CoA
about 10% of the activity with palmitoyl-CoA
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-
?
additional information
?
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isoform LASS5 preferentially produces C14:0 and C16:0 ceramides
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-
?
additional information
?
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the enzyme is higly selective toward palmitoyl-CoA as acyl donor
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?
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
palmitoyl-CoA + a sphingoid base
an N-(palmitoyl)-sphingoid base + CoA
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-
-
?
additional information
?
-
isoform LASS5 preferentially produces C14:0 and C16:0 ceramides
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the expression of CerS1 and CerS5 mRNA, encoding the ceramide synthases with substrate preference for C16:0 and C18:0 acyl chains, respectively, is downregulated in skeletal muscle of aged mice
CerS5 mRNA is detected in most cells within gray and white matter of all brain regions
LASS5 is the predominant ceramide synthase isoform detected in lung epithelia
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
CerS5 is essential to maintain cellular C16:0 sphingolipid pools in lung, spleen, muscle, liver, and white adipose tissue. In CerS5-deficient mice, glycerophospholipid levels are not altered, while in skeletal muscle, liver, and spleen, C16:0-ceramide levels aere altered independent of feeding conditions. The loss of CerS5 is associated with reduced weight gain and improved systemic health, including maintenance of glucose homeostasis and reduced white adipose tissue inflammation after high fat diet challenge
physiological function
exogenously expressed LASS5 in lung epithelia triggers increased ceramide synthesis, knockdown studies using fumonisin B1 or LASS5 siRNA reduce ceramide synthase activity by 78% or 45%, respectively. Overexpression of LASS5 also reduces phosphatidylcholine synthesis. Maximal inhibition is achieved when LASS5 is coexpressed with a plasmid encoding a neutral sphingomyelinase involved in sphingomyelin hydrolysis
physiological function
inhibition of isoform Cers5 by fuminisin B1 or siRNA suppresses myristate-induced C14-ceramide generation and X-box binding protein XBP1 splicing. Increased XBP1 splicing induces the downstream expression of IL-6 in a isoforms CerS5/6-dependent manner. A myristate-enriched milk fat-based diet, but not a lard-based diet, increases C14-ceramide, XBP1 splicing, and IL-6 expression in vivo
physiological function
overexpression of LASS elevates the synthesis of (dihydro)ceramides selectively enriched in palmitic acid
physiological function
skeletal muscle from mice deficient of either CerS1 or CerS5 shows reduced caliber sizes of both slow (type 1) and fast (type 2) muscle fibers, fiber grouping, and fiber switch to type 1 fibers. CerS1- and CerS5-deficient mice exhibit reduced twitch and tetanus forces of musculus extensor digitorum longus
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CERS5_MOUSE
414
5
48167
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
dephosphorylation of endogenous ceramide synthases in the mouse brain leads to modestly reduced activity toward the Cers5/6 substrate C16:0-CoA
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
pulmonary LASS5 is developmentally regulated, but its expression is spatially and gender nonspecific
the expression of CerS1 and CerS5 mRNA, encoding the ceramide synthases with substrate preference for C16:0 and C18:0 acyl chains, respectively, is downregulated in skeletal muscle of aged mice
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
CerS5-dependent ceramide synthesis has a strong impact in white adipose tissue after high fat diet feeding
medicine
long-chain ceramides are upregulated whereas very long-chain ceramides are downregulated in cell lines, mouse animal model, and patients with cystic fibrosis, compared with their controls. Treatment with fenretinide decreases the levels of long-chain ceramides and increases the levels of very long-chain ceramides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tosetti, B.; Brodesser, S.; Brunn, A.; Deckert, M.; Blueher, M.; Doehner, W.; Anker, S.D.; Wenzel, D.; Fleischmann, B.; Pongratz, C.; Peters, F.; Utermoehlen, O.; Kroenke, M.
A tissue-specific screen of ceramide expression in aged mice identifies ceramide synthase-1 and ceramide synthase-5 as potential regulators of fiber size and strength in skeletal muscle
Aging Cell
19
e13049
2019
Homo sapiens (Q8N5B7), Mus musculus (Q9D6K9)
Mizutani, Y.; Kihara, A.; Igarashi, Y.
Mammalian Lass6 and its related family members regulate synthesis of specific ceramides
Biochem. J.
390
263-271
2005
Mus musculus (Q9D6K9)
Choi, S.; Snider, J.M.; Olakkengil, N.; Lambert, J.M.; Anderson, A.K.; Ross-Evans, J.S.; Cowart, L.A.; Snider, A.J.
Myristate-induced endoplasmic reticulum stress requires ceramide synthases 5/6 and generation of C14-ceramide in intestinal epithelial cells
FASEB J.
32
5724-5736
2018
Mus musculus (Q9D6K9)
Becker, I.; Wang-Eckhardt, L.; Yaghootfam, A.; Gieselmann, V.; Eckhardt, M.
Differential expression of (dihydro)ceramide synthases in mouse brain oligodendrocyte-specific expression of CerS2/Lass2
Histochem. Cell Biol.
129
233-241
2008
Mus musculus (Q9D6K9)
Lahiri, S.; Futerman, A.H.
LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor
J. Biol. Chem.
280
33735-33738
2005
Mus musculus (Q9D6K9)
Gosejacob, D.; Jaeger, P.S.; Vom Dorp, K.; Frejno, M.; Carstensen, A.C.; Koehnke, M.; Degen, J.; Doermann, P.; Hoch, M.
Ceramide synthase 5 is essential to maintain C16 0-ceramide pools and contributes to the development of diet-induced obesity
J. Biol. Chem.
291
6989-7003
2016
Mus musculus (Q9D6K9)
Sassa, T.; Hirayama, T.; Kihara, A.
Enzyme activities of the ceramide synthases CERS2-6 are regulated by phosphorylation in the C-terminal region
J. Biol. Chem.
291
7477-7487
2016
Homo sapiens (Q8N5B7), Mus musculus (Q9D6K9)
Xu, Z.; Zhou, J.; McCoy, D.M.; Mallampalli, R.K.
LASS5 is the predominant ceramide synthase isoform involved in de novo sphingolipid synthesis in lung epithelia
J. Lipid Res.
46
1229-1238
2005
Mus musculus (Q9D6K9)
Garic, D.; De Sanctis, J.B.; Wojewodka, G.; Houle, D.; Cupri, S.; Abu-Arish, A.; Hanrahan, J.W.; Hajduch, M.; Matouk, E.; Radzioch, D.
Fenretinide differentially modulates the levels of long- and very long-chain ceramides by downregulating Cers5 enzyme evidence from bench to bedside
J. Mol. Med.
95
1053-1064
2017
Homo sapiens (Q8N5B7), Mus musculus (Q9D6K9)
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Release 2023.1 (January 2023)
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