The Enzyme Database

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EC 1.14.19.18     
Accepted name: sphingolipid 8-(E)-desaturase
Reaction: a (4E)-sphing-4-enine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E,8E)-sphing-4,8-dienine ceramide + 2 ferricytochrome b5 + 2 H2O
Other name(s): 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous)
Systematic name: (4E)-sphing-4-enine ceramide,ferrocytochrome b5:oxygen oxidoreductase (8,9-trans dehydrogenating)
Comments: The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans [1] and from the diatom Thalassiosira pseudonana [2], introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase [3]. The homologous enzymes from higher plants, EC 1.14.19.29, sphingolipid 8-(E/Z)-desaturase, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Takakuwa, N., Kinoshita, M., Oda, Y. and Ohnishi, M. Isolation and characterization of the genes encoding Δ8-sphingolipid desaturase from Saccharomyces kluyveri and Kluyveromyces lactis. Curr. Microbiol. 45 (2002) 459–461. [DOI] [PMID: 12402089]
2.  Tonon, T., Sayanova, O., Michaelson, L.V., Qing, R., Harvey, D., Larson, T.R., Li, Y., Napier, J.A. and Graham, I.A. Fatty acid desaturases from the microalga Thalassiosira pseudonana. FEBS J. 272 (2005) 3401–3412. [DOI] [PMID: 15978045]
3.  Oura, T. and Kajiwara, S. Disruption of the sphingolipid Δ8-desaturase gene causes a delay in morphological changes in Candida albicans. Microbiology 154 (2008) 3795–3803. [DOI] [PMID: 19047747]
[EC 1.14.19.18 created 2015]
 
 
EC 1.14.19.19     
Accepted name: sphingolipid 10-desaturase
Reaction: a (4E,8E)-sphinga-4,8-dienine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E,8E,10E)-sphinga-4,8,10-trienine ceramide + 2 ferricytochrome b5 + 2 H2O
Other name(s): desA (gene name)
Systematic name: a (4E,8E)-sphinga-4,8-dienine ceramide,ferrocytochrome b5:oxygen oxidoreductase (10,11 trans-dehydrogenating)
Comments: The enzyme, characterized from the marine diatom Thalassiosira pseudonana, produces an all-trans product. Similar triunsaturated sphingoid bases are found in some marine invertebrates. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Michaelson, L.V., Markham, J.E., Zäuner, S., Matsumoto, M., Chen, M., Cahoon, E.B. and Napier, J.A. Identification of a cytochrome b5-fusion desaturase responsible for the synthesis of triunsaturated sphingolipid long chain bases in the marine diatom Thalassiosira pseudonana. Phytochemistry 90 (2013) 50–55. [DOI] [PMID: 23510654]
[EC 1.14.19.19 created 2015]
 
 
EC 2.1.1.317     
Accepted name: sphingolipid C9-methyltransferase
Reaction: S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide = S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
Systematic name: S-adenosyl-L-methionine:(4E,8E)-sphinga-4,8-dienine ceramide C-methyltransferase
Comments: The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ternes, P., Sperling, P., Albrecht, S., Franke, S., Cregg, J.M., Warnecke, D. and Heinz, E. Identification of fungal sphingolipid C9-methyltransferases by phylogenetic profiling. J. Biol. Chem. 281 (2006) 5582–5592. [DOI] [PMID: 16339149]
2.  Ramamoorthy, V., Cahoon, E.B., Thokala, M., Kaur, J., Li, J. and Shah, D.M. Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Eukaryot Cell 8 (2009) 217–229. [DOI] [PMID: 19028992]
[EC 2.1.1.317 created 2015]
 
 
EC 2.3.1.291     
Accepted name: sphingoid base N-palmitoyltransferase
Reaction: palmitoyl-CoA + a sphingoid base = an N-(palmitoyl)-sphingoid base + CoA
Other name(s): mammalian ceramide synthase 5; CERS5 (gene name); LASS5 (gene name)
Systematic name: palmitoyl-CoA:sphingoid base N-palmitoyltransferase
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lahiri, S. and Futerman, A.H. LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor. J. Biol. Chem. 280 (2005) 33735–33738. [PMID: 16100120]
2.  Xu, Z., Zhou, J., McCoy, D.M. and Mallampalli, R.K. LASS5 is the predominant ceramide synthase isoform involved in de novo sphingolipid synthesis in lung epithelia. J. Lipid Res. 46 (2005) 1229–1238. [PMID: 15772421]
3.  Mizutani, Y., Kihara, A. and Igarashi, Y. Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390 (2005) 263–271. [PMID: 15823095]
[EC 2.3.1.291 created 2019, modified 2019]
 
 
EC 2.3.1.297     
Accepted name: very-long-chain ceramide synthase
Reaction: a very-long-chain fatty acyl-CoA + a sphingoid base = a very-long-chain ceramide + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterised by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2
Other name(s): sphingoid base N-very-long-chain fatty acyl-coA transferase; mammalian ceramide synthase 2; CERS3 (gene name); LASS3 (gene name); LAG1 (gene name); LAC1 (gene name); LOH1 (gene name); LOH3 (gene name)
Systematic name: very-long-chain fatty acyl-CoA:sphingoid base N-acyltransferase
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Guillas, I., Kirchman, P.A., Chuard, R., Pfefferli, M., Jiang, J.C., Jazwinski, S.M. and Conzelmann, A. C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p. EMBO J. 20 (2001) 2655–2665. [PMID: 11387200]
2.  Pan, H., Qin, W.X., Huo, K.K., Wan, D.F., Yu, Y., Xu, Z.G., Hu, Q.D., Gu, K.T., Zhou, X.M., Jiang, H.Q., Zhang, P.P., Huang, Y., Li, Y.Y. and Gu, J.R. Cloning, mapping, and characterization of a human homologue of the yeast longevity assurance gene LAG1. Genomics 77 (2001) 58–64. [PMID: 11543633]
3.  Schorling, S., Vallee, B., Barz, W.P., Riezman, H. and Oesterhelt, D. Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisae. Mol. Biol. Cell 12 (2001) 3417–3427. [PMID: 11694577]
4.  Mizutani, Y., Kihara, A. and Igarashi, Y. Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390 (2005) 263–271. [PMID: 15823095]
5.  Laviad, E.L., Albee, L., Pankova-Kholmyansky, I., Epstein, S., Park, H., Merrill, A.H., Jr. and Futerman, A.H. Characterization of ceramide synthase 2: tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate. J. Biol. Chem. 283 (2008) 5677–5684. [PMID: 18165233]
6.  Imgrund, S., Hartmann, D., Farwanah, H., Eckhardt, M., Sandhoff, R., Degen, J., Gieselmann, V., Sandhoff, K. and Willecke, K. Adult ceramide synthase 2 (CERS2)-deficient mice exhibit myelin sheath defects, cerebellar degeneration, and hepatocarcinomas. J. Biol. Chem. 284 (2009) 33549–33560. [PMID: 19801672]
[EC 2.3.1.297 created 2019]
 
 
EC 2.3.1.298     
Accepted name: ultra-long-chain ceramide synthase
Reaction: an ultra-long-chain fatty acyl-CoA + a sphingoid base = an ultra-long-chain ceramide + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
an ultra-long-chain fatty acyl-CoA = an acyl-CoA with a chain length of 28 or longer.
Other name(s): mammalian ceramide synthase 3; sphingoid base N-ultra-long-chain fatty acyl-coA transferase; CERS3 (gene name)
Systematic name: ultra-long-chain fatty acyl-coA:sphingoid base N-acyltransferase
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 ω-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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mizutani, Y., Kihara, A. and Igarashi, Y. LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity. Biochem. J. 398 (2006) 531–538. [PMID: 16753040]
2.  Mizutani, Y., Kihara, A., Chiba, H., Tojo, H. and Igarashi, Y. 2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis for the preference of FA chain length. J. Lipid Res. 49 (2008) 2356–2364. [PMID: 18541923]
3.  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., Grone, H.J. and Sandhoff, R. Loss of ceramide synthase 3 causes lethal skin barrier disruption. Hum. Mol. Genet. 21 (2012) 586–608. [PMID: 22038835]
4.  Mizutani, Y., Sun, H., Ohno, Y., Sassa, T., Wakashima, T., Obara, M., Yuyama, K., Kihara, A. and Igarashi, Y. Cooperative synthesis of ultra long-chain fatty acid and ceramide during keratinocyte differentiation. PLoS One 8:e67317 (2013). [PMID: 23826266]
[EC 2.3.1.298 created 2019]
 
 
EC 2.3.1.299     
Accepted name: sphingoid base N-stearoyltransferase
Reaction: stearoyl-CoA + a sphingoid base = an N-(stearoyl)-sphingoid base + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
Other name(s): mammalian ceramide synthase 1; LASS1 (gene name); UOG1 (gene name); CERS1 (gene name)
Systematic name: stearoyl-CoA:sphingoid base N-stearoyltransferase
Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 1 (CERS1) is structurally and functionally distinctive from all other CERS enzymes, and is specific for stearoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Venkataraman, K., Riebeling, C., Bodennec, J., Riezman, H., Allegood, J.C., Sullards, M.C., Merrill, A.H., Jr. and Futerman, A.H. Upstream of growth and differentiation factor 1 (uog1), a mammalian homolog of the yeast longevity assurance gene 1 (LAG1), regulates N-stearoyl-sphinganine (C18-(dihydro)ceramide) synthesis in a fumonisin B1-independent manner in mammalian cells. J. Biol. Chem. 277 (2002) 35642–35649. [PMID: 12105227]
2.  Kim, H.J., Qiao, Q., Toop, H.D., Morris, J.C. and Don, A.S. A fluorescent assay for ceramide synthase activity. J. Lipid Res. 53 (2012) 1701–1707. [PMID: 22661289]
3.  Wang, Z., Wen, L., Zhu, F., Wang, Y., Xie, Q., Chen, Z. and Li, Y. Overexpression of ceramide synthase 1 increases C18-ceramide and leads to lethal autophagy in human glioma. Oncotarget 8 (2017) 104022–104036. [PMID: 29262618]
4.  Turpin-Nolan, S.M., Hammerschmidt, P., Chen, W., Jais, A., Timper, K., Awazawa, M., Brodesser, S. and Bruning, J.C. CerS1-derived C18:0 ceramide in skeletal muscle promotes obesity-induced insulin resistance. Cell Rep. 26 (2019) 1–10.e7. [PMID: 30605666]
[EC 2.3.1.299 created 2019]
 
 
EC 2.7.1.91     
Accepted name: sphingosine kinase
Reaction: ATP + a sphingoid base = ADP + a sphingoid base 1-phosphate
Other name(s): SPHK1 (gene name); SPHK2 (gene name); dihydrosphingosine kinase; dihydrosphingosine kinase (phosphorylating); sphingosine kinase (phosphorylating); sphingoid base kinase; sphinganine kinase; ATP:sphinganine 1-phosphotransferase
Systematic name: ATP:sphingoid base 1-phosphotransferase
Comments: The enzyme is involved in the production of sphingolipid metabolites. It phosphorylates various sphingoid long-chain bases, such as sphingosine, D-erythro-dihydrosphingosine (sphinganine), phytosphingosine (4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine and D-threo-dihydrosphingosine and L-threo-dihydrosphingosine. The exact substrate range depends on the species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 50864-48-7
References:
1.  Stoffel, W., Heimann, G. and Hellenbroich, B. Sphingosine kinase in blood platelets. Hoppe-Seyler's Z. Physiol. Chem. 354 (1973) 562–566. [PMID: 4372149]
2.  Stoffel, W., Bauer, E. and Stahl, J. The metabolism of sphingosine bases in Tetrahymena pyriformis. Sphingosine kinase and sphingosine-1-phosphate lyase. Hoppe-Seyler's Z. Physiol. Chem. 355 (1974) 61–74. [PMID: 4373374]
3.  Nagiec, M.M., Skrzypek, M., Nagiec, E.E., Lester, R.L. and Dickson, R.C. The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases. J. Biol. Chem. 273 (1998) 19437–19442. [DOI] [PMID: 9677363]
4.  Kohama, T., Olivera, A., Edsall, L., Nagiec, M.M., Dickson, R. and Spiegel, S. Molecular cloning and functional characterization of murine sphingosine kinase. J. Biol. Chem. 273 (1998) 23722–23728. [DOI] [PMID: 9726979]
5.  Liu, H., Sugiura, M., Nava, V.E., Edsall, L.C., Kono, K., Poulton, S., Milstien, S., Kohama, T. and Spiegel, S. Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform. J. Biol. Chem. 275 (2000) 19513–19520. [DOI] [PMID: 10751414]
6.  Worrall, D., Liang, Y.K., Alvarez, S., Holroyd, G.H., Spiegel, S., Panagopulos, M., Gray, J.E. and Hetherington, A.M. Involvement of sphingosine kinase in plant cell signalling. Plant J. 56 (2008) 64–72. [DOI] [PMID: 18557834]
[EC 2.7.1.91 created 1976, modified 1980, modified 2016]
 
 


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