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Information on EC 2.3.1.297 - very-long-chain ceramide synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q6NQI8
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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: Arabidopsis thaliana
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
-
-
-
-
LOH1
-
-
-
-
LOH3
-
-
-
-
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
acyl-CoA + sphinganine
N-acylsphinganine + CoA
very low activity with sphinganine
-
-
?
hexacosanoyl-CoA + phytosphingosine
CoA + N-hexacosanoylphytosphingosine
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
-
-
-
?
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
-
-
-
?
acyl-CoA + sphinganine
N-acylsphinganine + CoA
very low activity with sphinganine
-
-
?
hexacosanoyl-CoA + phytosphingosine
CoA + N-hexacosanoylphytosphingosine
-
-
-
?
hexacosenoyl-CoA + a sphingoid base
hexacosenoyl ceramide + CoA
-
-
-
-
?
nervonyl-CoA + a sphingoid base
nervonyl ceramide + CoA
-
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
high activity
-
-
?
additional information
?
-
specificity of three different isoforms of ceramide synthase, denoted LOH1, 2 and 3, for a range of long-chain base (LCB) and acyl-CoA substrates. The contribution of each of these isoforms to the synthesis of ceramide is investigated by in vitro ceramide synthase assays, overview. The plant LCB phytosphingosine is efficiently used by the LOH1 and 3 isoforms, with LOH1 having the lowest Km for the LCB substrate of the three isoforms. In contrast, sphinganine is used efficiently only by the LOH2 isoform. Acyl-CoA specificity is also distinguished between the three isoforms with LOH2 being almost completely specific for palmitoyl-CoA, while the LOH1 isoform shows greatest activity with lignoceroyl- and hexacosanoyl-CoA. Unsaturated acyl-CoAs are not used efficiently by any isoform while unsaturated LCB substrates are preferred by LOH2 and 3. LOH3 has at least twice as much activity with t18:1 substrates as LOH1. Both LOH1 and LOH3 demonstrate a strong preference for very long chain acyl-CoAs (>C18) although LOH1 has the greatest activity toward 24 and 26 carbon acyl-CoAs, while LOH3 shows little preference for acyl-CoAs between 20 and 26 carbons in length
-
-
?
additional information
?
-
specificity of three different isoforms of ceramide synthase, denoted LOH1, 2 and 3, for a range of long-chain base (LCB) and acyl-CoA substrates. The contribution of each of these isoforms to the synthesis of ceramide is investigated by in vitro ceramide synthase assays, overview. The plant LCB phytosphingosine is efficiently used by the LOH1 and 3 isoforms, with LOH1 having the lowest Km for the LCB substrate of the three isoforms. In contrast, sphinganine is used efficiently only by the LOH2 isoform. Acyl-CoA specificity is also distinguished between the three isoforms with LOH2 being almost completely specific for palmitoyl-CoA, while the LOH1 isoform shows greatest activity with lignoceroyl- and hexacosanoyl-CoA. Unsaturated acyl-CoAs are not used efficiently by any isoform while unsaturated LCB substrates are preferred by LOH2 and 3. LOH3 has at least twice as much activity with t18:1 substrates as LOH1. Both LOH1 and LOH3 demonstrate a strong preference for very long chain acyl-CoAs (>C18) although LOH1 has the greatest activity toward 24 and 26 carbon acyl-CoAs, while LOH3 shows little preference for acyl-CoAs between 20 and 26 carbons in length
-
-
?
additional information
?
-
specificity of three different isoforms of ceramide synthase, denoted LOH1, 2 and 3, for a range of long-chain base (LCB) and acyl-CoA substrates. The contribution of each of these isoforms to the synthesis of ceramide is investigated by in vitro ceramide synthase assays, overview. The plant LCB phytosphingosine is efficiently used by the LOH1 and 3 isoforms, with LOH1 having the lowest Km for the LCB substrate of the three isoforms. In contrast, sphinganine is used efficiently only by the LOH2 isoform. Acyl-CoA specificity is also distinguished between the three isoforms with LOH2 being almost completely specific for palmitoyl-CoA, while the LOH1 isoform shows greatest activity with lignoceroyl- and hexacosanoyl-CoA. Unsaturated acyl-CoAs are not used efficiently by any isoform while unsaturated LCB substrates are preferred by LOH2 and 3. LOH3 has at least twice as much activity with t18:1 substrates as LOH1. Both LOH1 and LOH3 demonstrate a strong preference for very long chain acyl-CoAs (>C18) although LOH1 has the greatest activity toward 24 and 26 carbon acyl-CoAs, while LOH3 shows little preference for acyl-CoAs between 20 and 26 carbons in length
-
-
?
additional information
?
-
specificity of three different isoforms of ceramide synthase, denoted LOH1, 2 and 3, for a range of long-chain base (LCB) and acyl-CoA substrates. The contribution of each of these isoforms to the synthesis of ceramide is investigated by in vitro ceramide synthase assays, overview. The plant LCB phytosphingosine is efficiently used by the LOH1 and 3 isoforms, with LOH1 having the lowest Km for the LCB substrate of the three isoforms. In contrast, sphinganine is used efficiently only by the LOH2 isoform. Acyl-CoA specificity is also distinguished between the three isoforms with LOH2 being almost completely specific for palmitoyl-CoA, while the LOH1 isoform shows greatest activity with lignoceroyl- and hexacosanoyl-CoA. Unsaturated acyl-CoAs are not used efficiently by any isoform while unsaturated LCB substrates are preferred by LOH2 and 3. LOH3 has at least twice as much activity with t18:1 substrates as LOH1. Both LOH1 and LOH3 demonstrate a strong preference for very long chain acyl-CoAs (>C18) although LOH1 has the greatest activity toward 24 and 26 carbon acyl-CoAs, while LOH3 shows little preference for acyl-CoAs between 20 and 26 carbons in length
-
-
?
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
hexacosanoyl-CoA + phytosphingosine
CoA + N-hexacosanoylphytosphingosine
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
-
-
-
?
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
-
-
-
?
hexacosanoyl-CoA + phytosphingosine
CoA + N-hexacosanoylphytosphingosine
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
LOH3 is inhibited by most or all divalent cations tested
additional information
LOH3 is inhibited by most or all divalent cations tested
additional information
LOH1 is inhibited by most or all divalent cations tested
additional information
LOH1 is inhibited by most or all divalent cations tested
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fumonisin B1
mixed mode of inhibition with respect to the laong-chain base
fumonisin B1
mixed mode of inhibition with respect to the long-chain base
additional information
LOH3 is inhibited by most or all divalent cations tested
-
additional information
LOH3 is inhibited by most or all divalent cations tested
-
additional information
LOH1 is inhibited by most or all divalent cations tested
-
additional information
LOH1 is inhibited by most or all divalent cations tested
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
distinct roles and modes of regulation for each of the ceramide synthases in Arabidopsis thaliana sphingolipid metabolism. Ceramides are organizing components of sphingolipids in the eukaryotic cell. Three ceramide synthase isoforms are found in Arabidopsis thaliana each with specific substrate preferences and sensitivity to inhibitors and activators, overview. Isozymes LOH1 and LOH3 are responsible for the synthesis of ceramides with trihydroxy long-chain bases and very long chain fatty acids (VLCFA)
malfunction
physiological function
malfunction
-
disruption of the enzyme enhances plant sensitivity to dark submergence, but displays more resistance to submergence under light than wild type
malfunction
-
enzyme inhibition leads to altered root development and auxin transport
physiological function
distinct roles and modes of regulation for each of the ceramide synthases in Arabidopsis thaliana sphingolipid metabolism. Ceramides are organizing components of sphingolipids in the eukaryotic cell. Three ceramide synthase isoforms are found in Arabidopsis thaliana each with specific substrate preferences and sensitivity to inhibitors and activators, overview. Isozymes LOH1 and LOH3 are responsible for the synthesis of ceramides with trihydroxy long-chain bases and very long chain fatty acids (VLCFA)
physiological function
-
the enzyme is essential for plant growth and development
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). PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
complementation of the growth defect of DELTAlag1/DELTAlac1 yeast deletion mutant by recombinant GST-/FLAG-tagged LOH3. Upon isolation of a microsomal membrane fraction from yeast expressing the construct, LOH3 shows significant activity by an in vitro ceramide synthase assay
additional information
complementation of the growth defect of DELTAlag1/DELTAlac1 yeast deletion mutant by recombinant GST-/FLAG-tagged LOH3. Upon isolation of a microsomal membrane fraction from yeast expressing the construct, LOH3 shows significant activity by an in vitro ceramide synthase assay
additional information
complementation of the growth defect of DELTAlag1/DELTAlac1 yeast deletion mutant by recombinant GST-/FLAG-tagged LOH1. Upon isolation of a microsomal membrane fraction from yeast expressing the construct, LOH1 shows significant activity by an in vitro ceramide synthase assay
additional information
complementation of the growth defect of DELTAlag1/DELTAlac1 yeast deletion mutant by recombinant GST-/FLAG-tagged LOH1. Upon isolation of a microsomal membrane fraction from yeast expressing the construct, LOH1 shows significant activity by an in vitro ceramide synthase assay
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LAG3, recombinant expression of codon-optimized LAG3 as N-terminally FLAG-tagged enzyme in Saccharomyces cerevisiae membranes
gene LAG1, recombinant expression of codon-optimized LAG1 as N-terminally FLAG-tagged enzyme in Saccharomyces cerevisiae membranes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luttgeharm, K.D.; Cahoon, E.B.; Markham, J.E.
Substrate specificity, kinetic properties and inhibition by fumonisin B1 of ceramide synthase isoforms from Arabidopsis
Biochem. J.
473
593-603
2016
Arabidopsis thaliana (Q6NQI8), Arabidopsis thaliana (Q9LDF2)
Markham, J.E.; Molino, D.; Gissot, L.; Bellec, Y.; Hematy, K.; Marion, J.; Belcram, K.; Palauqui, J.C.; Satiat-Jeunemaitre, B.; Faure, J.D.
Sphingolipids containing very-long-chain fatty acids define a secretory pathway for specific polar plasma membrane protein targeting in Arabidopsis
Plant Cell
23
2362-2378
2011
Arabidopsis thaliana
Xie, L.; Chen, Q.; Chen, M.; Yu, L.; Huang, L.; Chen, L.; Wang, F.; Xia, F.; Zhu, T.; Wu, J.; Yin, J.; Liao, B.; Shi, J.; Zhang, J.; Aharoni, A.; Yao, N.; Shu, W.; Xiao, S.
Unsaturation of very-long-chain ceramides protects plant from hypoxia-induced damages by modulating ethylene signaling in Arabidopsis
PLoS Genet.
11
e1005143
2015
Arabidopsis thaliana
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