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a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
a very-long-chain fatty acyl-CoA + sphinganine
a very-long-chain sphinganine + CoA
-
-
-
-
?
acyl-CoA + sphinganine
N-acylsphinganine + CoA
very low activity with sphinganine
-
-
?
behenoyl-CoA + dihydrosphingosine
CoA + N-behenoyldihydrosphingosine
-
-
-
?
behenyl-CoA + sphinganine
behenyl-sphinganine + CoA
-
-
-
-
?
cerotoyl-CoA + a sphingoid base
cerotoyl ceramide + CoA
-
-
-
-
?
cerotoyl-CoA + sphinganine
cerotoyl-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
D-erythro-sphinganine + nervonoyl-CoA
N-nervonoyl-D-sphinganine + CoA
dihydrosphingosine + lignoceroyl-CoA
N-lignoceroyldihydrosphingosine + CoA
dihydrosphingosine + nervonoyl-CoA
N-nervonoyldihydrosphingosine + CoA
dihydrosphingosine + palmitoyl-CoA
N-palmitoyldihydrosphingosine + CoA
low activity
-
-
?
dihydrosphingosine + stearoyl-CoA
N-stearoyldihydrosphingosine + CoA
low activity
-
-
?
DL-erythro-sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
DL-threo-sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
erucyl-CoA + a sphingoid base
erucyl ceramide + CoA
-
-
-
-
?
hexacosanoyl-CoA + phytosphingosine
CoA + N-hexacosanoylphytosphingosine
-
-
-
?
hexacosenoyl-CoA + a sphingoid base
hexacosenoyl ceramide + CoA
-
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
lignoceryl-CoA + a sphingoid base
lignoceryl ceramide + CoA
-
-
-
-
?
nervonoyl-CoA + NBD-sphinganine
CoA + N-nervonoyl-NBD-sphinganine
nervonyl-CoA + a sphingoid base
nervonyl ceramide + CoA
-
-
-
-
?
nervonyl-CoA + sphinganine
CoA + nervonyl-sphinganine
-
-
-
-
?
sphinganine + arachidoyl-CoA
N-arachidoylsphinganine + CoA
sphinganine + behenoyl-CoA
N-behenoylsphinganine + CoA
sphinganine + cerotoyl-CoA
N-cerotoylsphinganine + CoA
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
sphinganine + nervonoyl-CoA
N-nervonoylsphinganine + CoA
-
-
-
?
sphinganine + palmitoyl-CoA
N-palmitoylsphinganine + CoA
sphinganine + stearoyl-CoA
N-stearoylsphinganine + CoA
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 + arachidoyl-CoA
N-arachidoylsphingosine + CoA
low activity
-
-
?
sphingosine + behenoyl-CoA
N-behenoylsphingosine + CoA
sphingosine + cerotoyl-CoA
N-cerotoylsphingosine + CoA
-
-
-
?
sphingosine + eicosanoyl-CoA
N-eicosanoylsphingosine + CoA
-
-
-
?
sphingosine + hexacosanoyl-CoA
N-hexacosanoylsphingosine + CoA
low activity
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
-
-
-
?
sphingosine + stearoyl-CoA
N-stearoylsphingosine + CoA
additional information
?
-
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
-
-
-
?
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
-
-
-
?
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
the enzyme synthesizes ceramides with very-long (C22-C24) acyl chains
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
preferred substrate
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
preferred substrate
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + nervonoyl-CoA
N-nervonoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + nervonoyl-CoA
N-nervonoyl-D-sphinganine + CoA
-
-
-
-
?
dihydrosphingosine + lignoceroyl-CoA
N-lignoceroyldihydrosphingosine + CoA
-
-
-
?
dihydrosphingosine + lignoceroyl-CoA
N-lignoceroyldihydrosphingosine + CoA
low activity
-
-
?
dihydrosphingosine + nervonoyl-CoA
N-nervonoyldihydrosphingosine + CoA
-
-
-
?
dihydrosphingosine + nervonoyl-CoA
N-nervonoyldihydrosphingosine + CoA
highly preferred substrate
-
-
?
DL-erythro-sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
-
both the threo and erythro isomers are active as acceptors, the latter is preferred
-
-
?
DL-erythro-sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
-
both the threo and erythro isomers are active as acceptors, the latter is preferred
-
-
?
DL-threo-sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
-
both the threo and erythro isomers are active as acceptors, the latter is preferred
-
-
?
DL-threo-sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
-
both the threo and erythro isomers are active as acceptors, the latter is preferred
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
high activity
-
-
?
nervonoyl-CoA + NBD-sphinganine
CoA + N-nervonoyl-NBD-sphinganine
C24:1-CoA substrate and NBD-labeled sphinganine substrate, i.e. omega(7-nitro-2-1,3-benzoxadiazole-4-yl)(2S,3R)-2-aminooctadecane-1,3-diol
-
-
?
nervonoyl-CoA + NBD-sphinganine
CoA + N-nervonoyl-NBD-sphinganine
C24:1-CoA substrate and NBD-labeled sphinganine substrate, i.e. omega(7-nitro-2-1,3-benzoxadiazole-4-yl)(2S,3R)-2-aminooctadecane-1,3-diol
-
-
?
sphinganine + arachidoyl-CoA
N-arachidoylsphinganine + CoA
-
-
-
?
sphinganine + arachidoyl-CoA
N-arachidoylsphinganine + CoA
low activity
-
-
?
sphinganine + behenoyl-CoA
N-behenoylsphinganine + CoA
-
-
-
?
sphinganine + behenoyl-CoA
N-behenoylsphinganine + CoA
-
-
-
?
sphinganine + behenoyl-CoA
N-behenoylsphinganine + CoA
moderate activity
-
-
?
sphinganine + cerotoyl-CoA
N-cerotoylsphinganine + CoA
-
-
-
?
sphinganine + cerotoyl-CoA
N-cerotoylsphinganine + CoA
low activity
-
-
?
sphinganine + cerotoyl-CoA
N-cerotoylsphinganine + CoA
low activity
-
-
?
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
-
-
-
?
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
-
-
-
?
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
high activity
-
-
?
sphinganine + palmitoyl-CoA
N-palmitoylsphinganine + CoA
-
-
-
?
sphinganine + palmitoyl-CoA
N-palmitoylsphinganine + CoA
low activity
-
-
?
sphinganine + stearoyl-CoA
N-stearoylsphinganine + CoA
-
-
-
?
sphinganine + stearoyl-CoA
N-stearoylsphinganine + CoA
preferred substrate
-
-
?
sphingosine + behenoyl-CoA
N-behenoylsphingosine + CoA
-
-
-
?
sphingosine + behenoyl-CoA
N-behenoylsphingosine + CoA
-
-
-
?
sphingosine + behenoyl-CoA
N-behenoylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
-
?
sphingosine + stearoyl-CoA
N-stearoylsphingosine + CoA
-
-
-
?
sphingosine + stearoyl-CoA
N-stearoylsphingosine + CoA
low 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
?
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
CERS2 preferentially transfers very long chain fatty acids (C22-C26)
-
-
?
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
?
-
CERS2 preferentially transfers very long chain fatty acids (C22:0-C26:0) to dihydrosphingosine. Improvement of a fluorescent assay, using HPLC using C16:0, C18:0 and C24:1 fatty acids and commercially available sphinganine-NBD, i.e. 7-nitro-2-1,3-benzoxadiazole-labelled dihydrosphingosine or (2S,3R)-2-amino-18((7-nitrobenzo[c][1,2,5]oxadiazol-4-yl)amino)octadecane-1-3-diol, as substrates, very accurate and sensitive method for quantification of CERS activity, method evaluation
-
-
?
additional information
?
-
substrate specificity, overview. Long-chain preference of CerS2
-
-
?
additional information
?
-
substrate specificity, overview. Long-chain preference of CerS2
-
-
?
additional information
?
-
ceramide synthase 2 catalyzes the synthesis of dihydroceramides from dihydrosphingosine and very long fatty acyl (C22-C24)-CoAs
-
-
?
additional information
?
-
-
ceramide synthase 2 catalyzes the synthesis of dihydroceramides from dihydrosphingosine and very long fatty acyl (C22-C24)-CoAs
-
-
?
additional information
?
-
both C22:0- and C24:0-CoAs are used effectively for Lass2- and Lass4-dependent ceramide synthesis, and C26:0-, C20:0-, and C18:0-CoAs also act as substrates, albeit weakly. Recombinant Lass2 produces longer ceramides such as C22:0 ceramides and C24:0 ceramides in transgenic HEK-293T cells
-
-
?
additional information
?
-
both C22:0- and C24:0-CoAs are used effectively for Lass2- and Lass4-dependent ceramide synthesis, and C26:0-, C20:0-, and C18:0-CoAs also act as substrates, albeit weakly. Recombinant Lass2 produces longer ceramides such as C22:0 ceramides and C24:0 ceramides in transgenic HEK-293T cells
-
-
?
additional information
?
-
-
both C22:0- and C24:0-CoAs are used effectively for Lass2- and Lass4-dependent ceramide synthesis, and C26:0-, C20:0-, and C18:0-CoAs also act as substrates, albeit weakly. Recombinant Lass2 produces longer ceramides such as C22:0 ceramides and C24:0 ceramides in transgenic HEK-293T cells
-
-
?
additional information
?
-
both C22:0- and C24:0-CoAs are used effectively for Lass2- and Lass4-dependent ceramide synthesis, and C26:0-, C20:0-, and C18:0-CoAs also act as substrates, albeit weakly. Recombinant Lass4 produces longer ceramides such as C22:0 and C24:0 ceramides in transgenic HEK-293T cells
-
-
?
additional information
?
-
both C22:0- and C24:0-CoAs are used effectively for Lass2- and Lass4-dependent ceramide synthesis, and C26:0-, C20:0-, and C18:0-CoAs also act as substrates, albeit weakly. Recombinant Lass4 produces longer ceramides such as C22:0 and C24:0 ceramides in transgenic HEK-293T cells
-
-
?
additional information
?
-
-
both C22:0- and C24:0-CoAs are used effectively for Lass2- and Lass4-dependent ceramide synthesis, and C26:0-, C20:0-, and C18:0-CoAs also act as substrates, albeit weakly. Recombinant Lass4 produces longer ceramides such as C22:0 and C24:0 ceramides in transgenic HEK-293T cells
-
-
?
additional information
?
-
CerS2 can utilize a wider range of fatty acyl-CoAs but uses mainly C22 to C24
-
-
?
additional information
?
-
-
CerS2 can utilize a wider range of fatty acyl-CoAs but uses mainly C22 to C24
-
-
?
additional information
?
-
CerS2 has a remarkable acyl-CoA specificity, it uses a wider range of acyl-CoAs, synthesizing ceramides containing C20:0, C22:0, C24:1, C24:0, C26:1, and C26:0 fatty acids, but does not synthesize ceramides containing C16:0 fatty acids and synthesizes only low, and statistically insignificant levels of C18:0-ceramide, overview
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-
?
additional information
?
-
enzyme LASS3 shows a relatively broad substrate specificity. Both LASS3 isoforms increase the production of several ceramide species, including C18:0- and C24:0-ceramides. LASS3 exhibits relatively low substrate specificity toward fatty acyl-CoAs. Lysates prepared from LASS3-overproducing cells show significant activity toward several fatty acyl-CoAs, including C18:0-, C22:0-, and C24:0-CoA, with the highest activity for C18:0. C16:0-, C20:0-, and C26:0-CoA are also used as substrates by LASS3, albeit with low activity. LASS3-overproducing cells synthesize ceramide from C18:0-CoA with the highest activity at all concentrations tested. This in vitro result is quite consistent with the in vivo results
-
-
?
additional information
?
-
-
enzyme LASS3 shows a relatively broad substrate specificity. Both LASS3 isoforms increase the production of several ceramide species, including C18:0- and C24:0-ceramides. LASS3 exhibits relatively low substrate specificity toward fatty acyl-CoAs. Lysates prepared from LASS3-overproducing cells show significant activity toward several fatty acyl-CoAs, including C18:0-, C22:0-, and C24:0-CoA, with the highest activity for C18:0. C16:0-, C20:0-, and C26:0-CoA are also used as substrates by LASS3, albeit with low activity. LASS3-overproducing cells synthesize ceramide from C18:0-CoA with the highest activity at all concentrations tested. This in vitro result is quite consistent with the in vivo results
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-
?
additional information
?
-
CerS2 has a remarkable acyl-CoA specificity, it uses a wider range of acyl-CoAs, synthesizing ceramides containing C20:0, C22:0, C24:1, C24:0, C26:1, and C26:0 fatty acids, but does not synthesize ceramides containing C16:0 fatty acids and synthesizes only low, and statistically insignificant levels of C18:0-ceramide, overview
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-
?
additional information
?
-
ceramide synthase 2 catalyzes the synthesis of dihydroceramides from dihydrosphingosine and very long fatty acyl (C22-C24)-CoAs
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
a very-long-chain fatty acyl-CoA + sphinganine
a very-long-chain sphinganine + CoA
-
-
-
-
?
behenoyl-CoA + dihydrosphingosine
CoA + N-behenoyldihydrosphingosine
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
D-erythro-sphinganine + nervonoyl-CoA
N-nervonoyl-D-sphinganine + CoA
dihydrosphingosine + lignoceroyl-CoA
N-lignoceroyldihydrosphingosine + CoA
-
-
-
?
dihydrosphingosine + nervonoyl-CoA
N-nervonoyldihydrosphingosine + CoA
-
-
-
?
hexacosanoyl-CoA + phytosphingosine
CoA + N-hexacosanoylphytosphingosine
-
-
-
?
lignoceroyl-CoA + phytosphingosine
N-lignoceroylphytosphinganine + CoA
-
-
-
?
sphinganine + arachidoyl-CoA
N-arachidoylsphinganine + CoA
-
-
-
?
sphinganine + behenoyl-CoA
N-behenoylsphinganine + CoA
sphinganine + cerotoyl-CoA
N-cerotoylsphinganine + CoA
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
sphinganine + nervonoyl-CoA
N-nervonoylsphinganine + CoA
-
-
-
?
sphinganine + palmitoyl-CoA
N-palmitoylsphinganine + CoA
-
-
-
?
sphinganine + stearoyl-CoA
N-stearoylsphinganine + CoA
-
-
-
?
sphingosine + behenoyl-CoA
N-behenoylsphingosine + CoA
sphingosine + cerotoyl-CoA
N-cerotoylsphingosine + CoA
-
-
-
?
sphingosine + eicosanoyl-CoA
N-eicosanoylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
sphingosine + nervonoyl-CoA
N-nervonoylsphingosine + CoA
-
-
-
?
sphingosine + stearoyl-CoA
N-stearoylsphingosine + CoA
-
-
-
?
additional information
?
-
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
-
-
-
?
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
-
-
-
?
a very-long-chain fatty acyl-CoA + a sphingoid base
a very-long-chain ceramide + CoA
-
the enzyme synthesizes ceramides with very-long (C22-C24) acyl chains
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + arachidoyl-CoA
N-arachidoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + behenoyl-CoA
N-behenoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + cerotoyl-CoA
N-cerotoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + lignoceroyl-CoA
N-lignoceroyl-D-sphinganine + CoA
-
-
-
-
?
D-erythro-sphinganine + nervonoyl-CoA
N-nervonoyl-D-sphinganine + CoA
-
-
-
?
D-erythro-sphinganine + nervonoyl-CoA
N-nervonoyl-D-sphinganine + CoA
-
-
-
-
?
sphinganine + behenoyl-CoA
N-behenoylsphinganine + CoA
-
-
-
?
sphinganine + behenoyl-CoA
N-behenoylsphinganine + CoA
-
-
-
?
sphinganine + cerotoyl-CoA
N-cerotoylsphinganine + CoA
-
-
-
?
sphinganine + cerotoyl-CoA
N-cerotoylsphinganine + CoA
low activity
-
-
?
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
-
-
-
?
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
-
-
-
?
sphingosine + behenoyl-CoA
N-behenoylsphingosine + CoA
-
-
-
?
sphingosine + behenoyl-CoA
N-behenoylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
-
?
additional information
?
-
CERS2 preferentially transfers very long chain fatty acids (C22-C26)
-
-
?
additional information
?
-
ceramide synthase 2 catalyzes the synthesis of dihydroceramides from dihydrosphingosine and very long fatty acyl (C22-C24)-CoAs
-
-
?
additional information
?
-
-
ceramide synthase 2 catalyzes the synthesis of dihydroceramides from dihydrosphingosine and very long fatty acyl (C22-C24)-CoAs
-
-
?
additional information
?
-
ceramide synthase 2 catalyzes the synthesis of dihydroceramides from dihydrosphingosine and very long fatty acyl (C22-C24)-CoAs
-
-
?
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evolution
Lass proteins are known to contain a TLC [TRAM/Lag1p/CLN8 (ceroid-lipofuscinoses, neuronal 8)] homology domain with the Lag1 motif. Lass family members Lass2, Lass4 and Lass5, but not Lass1, also contain a HOX (homeobox) domain
malfunction
CerS2-deficient (gene trap) mice exhibit myelin and behavioral abnormalities
malfunction
CerS2 null mouse show ceramide and downstream sphingolipids devoid of very long (C22-C24) acyl chains, consistent with the substrate specificity of CerS2 toward acyl-CoAs. C16-ceramide levels are elevated, and as a result, total ceramide levels are unaltered. C16-ceramide synthesis in vitro is not increased. Levels of C22-, C24:0-, and C24:1-sphingolipids are reduced by 10-100fold in the CerS2 null mouse, but no significant reduction is seen in C20-sphingolipids. Levels of C26:1- and C26:0-sphingolipids are relatively low in the wild-type, and only a small reduction is observed in the CerS2 null mouse. Levels of sphinganine are significantly elevated by up to 50fold, reminiscent of the effect of the ceramide synthase inhibitor fumonisin B1. With the exceptions of glucosylceramide synthase and neutral sphingomyelinase 2, none of the other enzymes tested in either the sphingolipid biosynthetic or degradative pathways are significantly changed. Total glycerophospholipid and cholesterol levels are unaltered, although there is a marked elevation in C18:1 and C18:2 fatty acids in phosphatidylethanolamine, concomitant with a reduction in C18:0 and C20:4 fatty acids. Liver microsomal membranes from CerS2 null mice display higher membrane fluidity and show morphological changes. Expression of CerS5 is increased in the Cers2 mutants, and of CerS6 slightly. Mutant phenotype, overview
malfunction
in HeLa cells overproducing the fatty acid 2-hydroxylase FA2H, knockdown of CerS2 results in a reduction in total long-chain 2-hydroxy-ceramides, confirming enzyme substrate specificity for chain length. Profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
malfunction
inhibition of CerS is able to protect from cell death. Moreover, this protection occurs downstream or independently of mitochondrial permeabilization. Inhibition of CerS greatly inhibits plasma membrane permeabilization. Individual CerS knockdown does not significantly inhibit total ceramide accumulation. Knockdown of CerS2 in untreated cells reduces very long-chain Cer and increases long-chain Cer both in untreated and UV-C-treated cells. Inhibition of CerS but not de novo synthesis inhibits plasma membrane rupture that is not specific to UV-C irradiation or MCF-7 cells
malfunction
Lass4 overproduction caused increases in both middle- and long-chain ceramides
malfunction
overexpression of CerS2 results in partial protection from IR-induced apoptosis. Knockdown studies determines that CerS2 is responsible for all observable IR-induced C24:0 CerS activity. CerS2 and CerS5 overexpression significantly alters apoptosis
malfunction
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
malfunction
-
about 50% of enzyme-null mice develop pheochromocytoma by about 13 months, and the rest shows signs of medullary hyperplasia
malfunction
-
ceramide synthase 2 null mice are more susceptible to dextran sodium sulfate-induced colitis, and their survival rate is markedly decreased compared with that of wild type littermates. In the colon of enzyme-deficient mice, the expression of junctional adhesion molecule-A is markedly decreased and the phosphorylation of myosin light chain 2 is increased. Enzyme deficiency influences intestinal barrier function and the severity of experimental colitis
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
malfunction
-
enzyme-deficient mice show increased susceptibility to LCMV infection. Reduced levels of invariant natural killer T cells in the thymus of enzyme-null mice is due to their impaired maturation in the thymus
malfunction
-
CerS2-deficient (gene trap) mice exhibit myelin and behavioral abnormalities
-
metabolism
regulation of CerS isozymes, overview. The interplay among the CerS proteins takes place in a stress stimulus-, cell type-, and subcellular compartment-specific manner. CerS2 and CerS5 overexpression significantly alters apoptosis. Determination of ionizing radiation-induced mitochondrial ceramide elevations via CerS2, 5, and 6, overview. CerS2 and CerS5 overexpressions defines opposing roles in radiation-induced mitochondrial apoptosis
metabolism
regulation of sphingolipid metabolism by UV-C irradiation, overview. Ceramide species that are the least abundant (e.g. C18-Cer, C18:1-Cer, C20-Cer, C22:1-Cer, etc.) exhibit the greatest fold increases. More abundant ceramide species (e.g. C16-Cer, C24-Cer, and C24:1-Cer) show more modest fold changes, although they account for much more of the overall increase in ceramides
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
critical role for ceramide synthase 2 in liver homeostasis, molecular changes leading to hepatopathy, overview. Isozyme CerS2 can utilize a wider range of fatty acyl-CoAs but uses mainly C22 to C24. In addition, CerS2 displays complex modes of regulation and has genomic features characteristic of a housekeeping gene, no other CerS genes display these characteristics
physiological function
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
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
good correlation between CerS2 mRNA levels and levels of ceramide and sphingomyelin containing long acyl chains in tissues with CerS2 mRNA expression at high levels. The activity of CerS2 can be regulated by another bioactive sphingolipid, sphingosine 1-phosphate (S1P), via interaction of S1P with two residues that are part of an S1P receptor-like motif found only in CerS2
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
overproduction of LASS3 causes increased levels of C18:0-, C22:0-, and C24:0-ceramides
physiological function
proteins Lag1p, Lac1p, and Lip1p are required for ceramide synthase activity in Saccharomyces cerevisiae
physiological function
selective tissue and subcellular distribution of the six mammalian CerS isoforms, combined with distinct fatty acyl chain length substrate preferences, implicate differential functions of specific ceramide species in cellular signaling. Ionizing radiation (IR) induces de novo synthesis of ceramide to influence HeLa cell apoptosis by specifically activating isozymes CerS isoforms 2, 5, and 6 that generate opposing anti- and pro-apoptotic ceramides in mitochondrial membranes. Isozyme CerS2 is responsible for all observable IR-induced C24:0 CerS activity. IR-induced CerS-mediated ceramide generation, and subsequent apoptosis, occurs in a cell-type specific manner. CerS2 and CerS5 overexpressions defines opposing roles in radiation-induced mitochondrial apoptosis
physiological function
sphingolipid ceramides are widely implicated in the regulation of programmed cell death or apoptosis. CerS2 regulates very long-chain Cer synthesis. CerS2 and CerS6 are the major very long-chain and long-chain CerS isoforms in MCF-7 cells, respectively
physiological function
very long chain ceramides synthesized by CERS2 are essential constituents of myelin. CERS2 demonstrates a preference for the monounsaturated C24:1 fatty acid substrate compared to the saturated C24:0 substrate, potentially explaining why myelin is enriched in ceramides containing the monounsaturated form of very long chain fatty acids
physiological function
-
the enzyme is essential for plant growth and development
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
-
good correlation between CerS2 mRNA levels and levels of ceramide and sphingomyelin containing long acyl chains in tissues with CerS2 mRNA expression at high levels. The activity of CerS2 can be regulated by another bioactive sphingolipid, sphingosine 1-phosphate (S1P), via interaction of S1P with two residues that are part of an S1P receptor-like motif found only in CerS2
-
physiological function
-
proteins Lag1p, Lac1p, and Lip1p are required for ceramide synthase activity in Saccharomyces cerevisiae
-
additional information
chimeric mutant CerS5:TM:CerS2-HA displays slightly more activity using C16-CoA as substrate than CerS5, but remarkably, CerS2 activity measured using C22-CoA is elevated by 3fold. Isozymes CerS5 and CerS6 modulate CerS2 activity upon co-expression. This increase in CerS2 activity is abolished using a noncatalytically active form of CerS5 in the constitutive dimer (CerS5HH:TM:CerS2-HA), demonstrating that optimal CerS2 activity depends on an interaction with a catalytically active form of CerS5
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
additional information
the N-terminus is essential for catalytic activity
additional information
the N-terminus is essential for catalytic activity
additional information
-
the N-terminus is essential for catalytic activity
additional information
two transcriptional variants of mouse LASS3 cDNA encoding the LASS3 isoforms, which differ in transcriptional initiation sites and polypeptides length, LASS3 and LASS3-long
additional information
-
two transcriptional variants of mouse LASS3 cDNA encoding the LASS3 isoforms, which differ in transcriptional initiation sites and polypeptides length, LASS3 and LASS3-long
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
-
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Cell-type-specific expression pattern of ceramide synthase 2 protein in mouse tissues
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Mus musculus (Q924Z4), Mus musculus, Mus musculus C57BL/6 (Q924Z4)
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Increased ceramide synthase 2 and 6 mRNA levels in breast cancer tissues and correlation with sphingosine kinase expression
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Mammalian Lass6 and its related family members regulate synthesis of specific ceramides
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Transmembrane topology of ceramide synthase in yeast
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398
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Substrate specificity, kinetic properties and inhibition by fumonisin B1 of ceramide synthase isoforms from Arabidopsis
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Enzymatic synthesis of ceramide
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Cavia porcellus, Gallus gallus
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Solubilization and partial characterization of fatty acyl-CoA sphingosine acyltransferase (ceramide synthetase) from rat liver and brain
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24
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