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Information on EC 2.3.1.298 - ultra-long-chain ceramide synthase
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2.3.1.298 ultra-long-chain ceramide synthaseIUBMB Comments
Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 3 (CERS3) is the only enzyme that is active with ultra-long-chain acyl-CoA donors (C28 or longer). It is active in the epidermis, where its products are incorporated into acylceramides. CERS3 also accepts (2R)-2-hydroxy fatty acids and omega-hydroxy fatty acids, and can accept very-long-chain acyl-CoA substrates (see EC 2.3.1.297, very-long-chain ceramide synthase). It can use multiple sphingoid bases including sphinganine, sphingosine, phytosphingosine, and (6R)-6-hydroxysphingosine.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
an ultra-long-chain fatty acyl-CoA
+
=
an ultra-long-chain ceramide
+
Synonyms
(dihydro)ceramide synthase, ceramide synthase, ceramide synthase 3, CerS3, LASS3, LASS3-long, longevity assurance homologue 3, mammalian ceramide synthase 3, phytoceramide synthase, sphingoid base N-ultra-long-chain fatty acyl-coA transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ceramide synthase
ceramide synthase 3
CerS3
LASS3
mammalian ceramide synthase 3
-
-
-
-
sphingoid base N-ultra-long-chain fatty acyl-coA transferase
CerS3
-
-
-
-
sphingoid base N-ultra-long-chain fatty acyl-coA transferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an ultra-long-chain fatty acyl-CoA + a sphingoid base = an ultra-long-chain ceramide + CoA
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ultra-long-chain fatty acyl-coA:sphingoid base N-acyltransferase
Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 3 (CERS3) is the only enzyme that is active with ultra-long-chain acyl-CoA donors (C28 or longer). It is active in the epidermis, where its products are incorporated into acylceramides. CERS3 also accepts (2R)-2-hydroxy fatty acids and omega-hydroxy fatty acids, and can accept very-long-chain acyl-CoA substrates (see EC 2.3.1.297, very-long-chain ceramide synthase). It can use multiple sphingoid bases including sphinganine, sphingosine, phytosphingosine, and (6R)-6-hydroxysphingosine.
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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
an ultra-long-chain fatty acyl-CoA + phytosphingosine
phytoceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + sphingosine
an ultra-long-chain ceramide + CoA
-
the enzyme uses acyl-CoAs longer than 26 carbon atoms in length
-
-
?
arachidoyl-CoA + dihydrosphingosine
CoA + N-arachidoyl-dihydrosphingosine
weak activity
-
-
?
cerotoyl-CoA + dihydrosphingosine
CoA + N-cerotoyl-dihydrosphingosine
weak activity
-
-
?
palmitoyl-CoA + dihydrosphingosine
CoA + N-palmitoyldihydrosphingosine
high activity
-
-
?
sphingosine + 2-hydroxybehenoyl-CoA
N-2-hydroxybehenoylsphingosine + CoA
-
-
-
?
sphingosine + 2-hydroxyeicosanoyl-CoA
N-2-hydroxyeicosanoylsphingosine + CoA
-
-
-
?
sphingosine + 2-hydroxylignoceroyl-CoA
N-2-hydroxylignoceroylsphingosine + CoA
-
-
-
?
sphingosine + 2-hydroxypalmitoyl-CoA
N-2-hydroxypalmitoylsphingosine + CoA
-
-
-
?
sphingosine + 2-hydroxystearoyl-CoA
N-2-hydroxystearoylsphingosine + CoA
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
C26-C36
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
C26-C34
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
C26-C36
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
behenoyl-CoA + dihydrosphingosine
CoA + N-behenoyldihydrosphingosine
-
-
-
?
behenoyl-CoA + dihydrosphingosine
CoA + N-behenoyldihydrosphingosine
-
-
-
?
hexacosanoyl-CoA + sphinganine
hexacosanoyl ceramide + CoA
-
main substrate
-
-
?
lignoceroyl-CoA + dihydrosphingosine
CoA + N-lignoceroyldihydrosphingosine
highest activity
-
-
?
lignoceroyl-CoA + dihydrosphingosine
CoA + N-lignoceroyldihydrosphingosine
-
-
-
?
montanoyl-CoA + sphingosine
montanoyl ceramide + CoA
-
bona fide substrate
-
-
?
montanoyl-CoA + sphingosine
montanoyl ceramide + CoA
-
bona fide substrate
-
-
?
stearoyl-CoA + dihydrosphingosine
CoA + N-stearoyldihydrosphingosine
-
-
-
?
stearoyl-CoA + dihydrosphingosine
CoA + N-stearoyldihydrosphingosine
highest activity
-
-
?
additional information
?
-
CERS3 transfers much longer chain fatty acids (C26, C28), forming highly hydrophobic ceramides that are a very important part of the water barrier function of skin
-
-
?
additional information
?
-
CERS activity is assayed using LC-MS/MS for product quantification, crude extracts containing cell membranes are firstly prepared from tissues or cultured cells, reactions contain deuterated dihydrosphingosine (or sphingosine) and a fatty acid substrate linked to CoA (C16:0 to C24:0/24:1), detailed method descritpion and evaluation, overview
-
-
?
additional information
?
-
-
isozyme CerS3 exhibits broad substrate specificity toward medium- to long-chain fatty acyl-CoAs (short-chain having less than C18, medium-chain with C18-C22, and long-chain with more than C22). In HEK-293T cells overproducing both CerS3 and 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase (FA2H), no 2-hydroxy-C16:0-ceramide is detected, but both medium- and long-chain 2-hydroxy-ceramides. CerS3 may use both medium- and long-chain 2-hydroxy-fatty acyl-CoAs as substrates
-
-
?
additional information
?
-
isozyme CerS3 exhibits broad substrate specificity toward medium- to long-chain fatty acyl-CoAs (short-chain having less than C18, medium-chain with C18-C22, and long-chain with more than C22). In HEK-293T cells overproducing both CerS3 and 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase (FA2H), no 2-hydroxy-C16:0-ceramide is detected, but both medium- and long-chain 2-hydroxy-ceramides. CerS3 may use both medium- and long-chain 2-hydroxy-fatty acyl-CoAs as substrates
-
-
?
additional information
?
-
-
the enzyme also uses long-chain and very-long-chain fatty acyl-CoAs as substrate
-
-
?
additional information
?
-
-
the enzyme can also use both medium- and long-chain 2-hydroxy-fatty acyl-CoAs as substrates
-
-
?
additional information
?
-
the enzyme can also use both medium- and long-chain 2-hydroxy-fatty acyl-CoAs as substrates
-
-
?
additional information
?
-
-
the enzyme also accepts long or very long fatty acyl-CoAs as substrate
-
-
?
additional information
?
-
-
the enzyme also uses long-chain and very-long-chain fatty acyl-CoAs as substrate
-
-
?
additional information
?
-
the enzyme exhibits relatively low substrate specificity toward fatty-acyl CoAs
-
-
?
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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
an ultra-long-chain fatty acyl-CoA + phytosphingosine
phytoceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + sphingosine
an ultra-long-chain ceramide + CoA
-
the enzyme uses acyl-CoAs longer than 26 carbon atoms in length
-
-
?
additional information
?
-
CERS3 transfers much longer chain fatty acids (C26, C28), forming highly hydrophobic ceramides that are a very important part of the water barrier function of skin
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
C26-C36
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
-
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
C26-C34
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
-
C26-C36
-
-
?
an ultra-long-chain fatty acyl-CoA + a sphingoid base
an ultra-long-chain ceramide + CoA
the enzyme exhibits a broad acyl chain preference synthesizing C26-C32 acyl chain ceramides
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acyl-coenzyme A-binding protein
-
increases the activity of the enzyme by 7fold
-
additional information
-
high-speed liver cytosol from wild type mice activates enzyme activity, whereas cytosol from acyl-coenzyme A-binding protein knock-out mice does not
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
epidermal, expression analysis of the CerS family members during keratinocyte differentiation, overview. Upon differentiation, CerS3 mRNA expression significantly increases and remains high throughout differentiation
brenda
-
the enzyme localizes to upper stratum spinosum and stratum granulosum
brenda
aged skin shows decreased levels of stratum corneum ceramides. Comparison of activities of epidermal A-SMase, ceramide synthase, and ceramidase in chronologically aged versus young hairless mouse skin. Reduced A-SMase and ceramide synthase activities are found in the epidermis of aged mice, but ceramidase activity is not age-dependent
brenda
-
the enzyme is expressed in the upper stratum spinosum and stratum granulosumof the skin
brenda
-
the enzyme localizes to upper stratum spinosum and stratum granulosum
brenda
Mus musculus SKH-1
-
aged skin shows decreased levels of stratum corneum ceramides. Comparison of activities of epidermal A-SMase, ceramide synthase, and ceramidase in chronologically aged versus young hairless mouse skin. Reduced A-SMase and ceramide synthase activities are found in the epidermis of aged mice, but ceramidase activity is not age-dependent
-
brenda
aged skin shows decreased levels of stratum corneum ceramides
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
enzyme deficiency in mice results in complete loss of ultra-long-chain acyl moities (C26 or higher), lack of continuous extracellular lipid lamellae and a non-functional cornified lipid envelope. Consequently newborn mutant mice die shortly after birth from transepidermal water loss. Mutant skin is also prone to Candida albicans infection
malfunction
-
enzyme knockdown causes a reduction in the elongase activities toward ultra-long-chain acyl-CoAs
malfunction
-
enzyme knockdown causes a reduction in the elongase activities toward ultra-long-chain acyl-CoAs
malfunction
-
enzyme loss leads to tubular atrophy and apoptosis of predominantly primary spermatocytes
malfunction
-
enzyme mutations are associated with skin ichthyosis. Enzyme-deficient mice show death after birth due to transepidermal water loss, hyperkeratosis, deficient cornification, and increased susceptibility to Candida albicans infection
malfunction
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
metabolism
-
the enzyme positively regulates very-long chain and ultra-long-chain fatty acid synthesis in keratinocytes. The enzyme regulates activities of ELOVL1 and ELOVL4 in differentiated keratinocytes
metabolism
-
the enzyme positively regulates very-long chain and ultra-long-chain fatty acid synthesis in keratinocytes. The enzyme regulates activities of ELOVL1 and ELOVL4 in differentiated keratinocytes
physiological function
ceramides are synthesized by ceramide synthases through the addition of a variable length fatty acid to the amine group of a sphingoid base. In mammalian cells, the sphingoid base used for de novo ceramide synthesis is usually the C18:0 lipid dihydrosphingosine. Ceramide synthesis is catalyzed by a family of six ceramide synthases (CERS1-6), each of which preferentially transfers fatty acids of different lengths to the amine group of dihydrosphingosine
physiological function
epidermal ceramides are generated by sphingomyelin hydrolysis or synthesis from sphingosin and fatty acids and are degraded by ceramidase. In aged skin occur decreased levels of stratum corneum ceramides. Epidermal acid sphingomyelinase (A-SMase) generates ceramides with structural function in the stratum corneum lipid bilayers, which provide for the permeability barrier function of the skin. Reduced A-SMase and ceramide synthase activities are found in the epidermis of aged mice, but ceramidase activity is not age-dependent
physiological function
isozyme CerS3 may be important in ceramide and 2-hydroxy-ceramide synthesis in epidermis. Differences in the expression patterns of CerS family members may play an important role in the production of the CER/2-hydroxy ceramide (CER) compositions of different chain lengths observed in different cell types and even in the altered production that occurring during keratinocyte differentiation
physiological function
-
the enzyme is essential for spermatogenesis and fertility
physiological function
Mus musculus SKH-1
-
epidermal ceramides are generated by sphingomyelin hydrolysis or synthesis from sphingosin and fatty acids and are degraded by ceramidase. In aged skin occur decreased levels of stratum corneum ceramides. Epidermal acid sphingomyelinase (A-SMase) generates ceramides with structural function in the stratum corneum lipid bilayers, which provide for the permeability barrier function of the skin. Reduced A-SMase and ceramide synthase activities are found in the epidermis of aged mice, but ceramidase activity is not age-dependent
-
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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). CERS3_HUMAN
383
5
46316
Swiss-Prot
Secretory Pathway (Reliability: 4)
CERS3_MOUSE
383
5
46081
Swiss-Prot
other Location (Reliability: 5)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation mildly increases the catalytic activity of the enzyme by 28%
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
additional information
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells
expressed in HeLa cells
gene CERS3, recombinant expression in HEK-293T cells, quantitative real-time quantitative PCR enzyme expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity is significantly reduced in the testes of acyl-coenzyme A-binding protein-deficient mice
-
enzyme mRNA expression significantly increases and remains high throughout keratinocyte differentiation
enzyme mRNA increases during keratinocyte differentiation
the enzyme is upregulated first during meiosis and later on in mid-late spermiogenesis, in spermatocytes and in elongated spermatids
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mizutani, Y.; Kihara, A.; Igarashi, Y.
LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity
Biochem. J.
398
531-538
2006
Mus musculus (Q1A3B0)
brenda
Park, J.; Park, W.; Futerman, A.
Ceramide synthases as potential targets for therapeutic intervention in human diseases
Biochim. Biophys. Acta
1841
671-681
2014
Mus musculus
brenda
Holmes, R.S.; Barron, K.A.; Krupenko, N.I.
Ceramide synthase 6 comparative analysis, phylogeny and evolution
Biomolecules
8
111
2018
Danio rerio (A0A140LFW4), Gallus gallus (F1N8P2), Mus musculus (Q1A3B0), Homo sapiens (Q8IU89)
brenda
Jensen, J.M.; Forl, M.; Winoto-Morbach, S.; Seite, S.; Schunck, M.; Proksch, E.; Schutze, S.
Acid and neutral sphingomyelinase, ceramide synthase, and acid ceramidase activities in cutaneous aging
Exp. Dermatol.
14
609-618
2005
Mus musculus (Q1A3B0), Mus musculus SKH-1 (Q1A3B0)
brenda
Georgopapadakou, N.
Antifungals targeted to sphingolipid synthesis Focus on inositol phosphorylceramide synthase
Expert Opin. Investig. Drugs
9
1787-1796
2000
Saccharomyces cerevisiae
brenda
Sandhoff, R.
Very long chain sphingolipids tissue expression, function and synthesis
FEBS Lett.
584
1907-1913
2010
Mus musculus
brenda
Jennemann, R.; Rabionet, M.; Gorgas, K.; Epstein, S.; Dalpke, A.; Rothermel, U.; Bayerle, A.; van der Hoeven, F.; Imgrund, S.; Kirsch, J.; Nickel, W.; Willecke, K.; Riezman, H.; Groene, H.J.; Sandhoff, R.
Loss of ceramide synthase 3 causes lethal skin barrier disruption
Hum. Mol. Genet.
21
586-608
2012
Homo sapiens, Mus musculus
brenda
Rabionet, M.; Bayerle, A.; Jennemann, R.; Heid, H.; Fuchser, J.; Marsching, C.; Porubsky, S.; Bolenz, C.; Guillou, F.; Groene, H.J.; Gorgas, K.; Sandhoff, R.
Male meiotic cytokinesis requires ceramide synthase 3-dependent sphingolipids with unique membrane anchors
Hum. Mol. Genet.
24
4792-4808
2015
Mus musculus
brenda
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
brenda
Ferreira, N.S.; Engelsby, H.; Neess, D.; Kelly, S.L.; Volpert, G.; Merrill, A.H.; Futerman, A.H.; Faergeman, N.J.
Regulation of very-long acyl chain ceramide synthesis by acyl-CoA-binding protein
J. Biol. Chem.
292
7588-7597
2017
Mus musculus
brenda
Mizutani, Y.; Kihara, A.; Chiba, H.; Tojo, H.; Igarashi, Y.
2-Hydroxy-ceramide synthesis by ceramide synthase family enzymatic basis for the preference of FA chain length
J. Lipid Res.
49
2356-2364
2008
Homo sapiens, Homo sapiens (Q8IU89)
brenda
Lim, X.Y.; Pickford, R.; Don, A.S.
Assaying ceramide synthase activity in vitro and in living cells using liquid chromatography-mass spectrometry
Methods Mol. Biol.
1376
11-22
2016
Homo sapiens (Q8IU89)
brenda
Mizutani, Y.; Sun, H.; Ohno, Y.; Sassa, T.; Wakashima, T.; Obara, M.; Yuyama, K.; Kihara, A.; Igarashi, Y.
Cooperative synthesis of ultra long-chain fatty acid and ceramide during keratinocyte differentiation
PLoS ONE
8
e67317
2013
Homo sapiens, Mus musculus
brenda
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