EC
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2.4.99.9
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Transferred entry: | lactosylceramide α-2,3-sialyltransferase. Now EC 2.4.3.9, lactosylceramide α-2,3-sialyltransferase
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[EC 2.4.99.9 created 1984, modified 1986, deleted 2022] |
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EC
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2.4.99.10
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Transferred entry: | neolactotetraosylceramide α-2,3-sialyltransferase. Now included in
EC 2.4.3.6, N-acetyllactosaminide α-2,3-sialyltransferase
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[EC 2.4.99.10 created 1986, deleted 2017] |
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EC
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2.4.99.11
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Deleted entry: | lactosylceramide α-2,6-N-sialyltransferase. Now included with EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase |
[EC 2.4.99.11 created 1992, deleted 2017] |
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EC |
2.7.1.138 |
Accepted name: |
ceramide kinase |
Reaction: |
ATP + ceramide = ADP + ceramide 1-phosphate |
Other name(s): |
acylsphingosine kinase |
Systematic name: |
ATP:ceramide 1-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 123175-68-8 |
References: |
1. |
Bajjalieh, S.M., Martin, T.F.J. and Floor, E. Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase that co-purifies with brain synaptic vesicles. J. Biol. Chem. 264 (1989) 14354–14360. [PMID: 2547795] |
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[EC 2.7.1.138 created 1992] |
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EC |
2.7.1.227 |
Accepted name: |
inositol phosphorylceramide synthase |
Reaction: |
1-phosphatidyl-1D-myo-inositol + a very-long-chain (2′R)-2′-hydroxy-phytoceramide = 1,2-diacyl-sn-glycerol + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine |
Glossary: |
a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine = a very-long-chain inositol phospho-α hydroxyphytoceramide = IPC |
Other name(s): |
AUR1 (gene name); KEI1 (gene name) |
Systematic name: |
1-phosphatidyl-1D-myo-inositol:a very-long-chain (2′R)-2′-hydroxy-phytoceramide phosphoinositoltransferase |
Comments: |
The enzyme, characterized from yeast, attaches a phosphoinositol headgroup to α-hydroxyphytoceramides, generating a very-long-chain inositol phospho-α hydroxyphytoceramide (IPC), the simplest of the three complex sphingolipids produced by yeast. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Nagiec, M.M., Nagiec, E.E., Baltisberger, J.A., Wells, G.B., Lester, R.L. and Dickson, R.C. Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J. Biol. Chem. 272 (1997) 9809–9817. [PMID: 9092515] |
2. |
Levine, T.P., Wiggins, C.A. and Munro, S. Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae. Mol. Biol. Cell 11 (2000) 2267–2281. [PMID: 10888667] |
3. |
Sato, K., Noda, Y. and Yoda, K. Kei1: a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization. Mol. Biol. Cell 20 (2009) 4444–4457. [PMID: 19726565] |
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[EC 2.7.1.227 created 2019] |
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EC |
2.7.1.228 |
Accepted name: |
mannosyl-inositol-phosphoceramide inositolphosphotransferase |
Reaction: |
1-phosphatidyl-1D-myo-inositol + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine = 1,2-diacyl-sn-glycerol + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(6-O-{6-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]-α-D-mannosyl}-1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine |
Glossary: |
a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine = a very-long-chain mannosylinositol phospho-α-hydroxyphytoceramide = MIPC
a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(6-O-{6-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]-α-D-mannosyl}-1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine = a very-long-chain mannosyl-diphosphoinositol-α-hydroxyphytoceramide = MIP2C |
Other name(s): |
IPT1 (gene name) |
Systematic name: |
1-phosphatidyl-1D-myo-inositol:(4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine phosphoinositoltransferase |
Comments: |
This enzyme catalyses the ultimate reaction in the yeast sphingolipid biosynthesis pathway. It transfers a second phosphoinositol group to mannosyl-inositol-phospho-α-hydroxyphytoceramide (MIPC), forming the final and most abundant yeast sphingolipid, mannosyl-diphosphoinositol-ceramide (MIP2C). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Dickson, R.C., Nagiec, E.E., Wells, G.B., Nagiec, M.M. and Lester, R.L. Synthesis of mannose-(inositol-P)2-ceramide, the major sphingolipid in Saccharomyces cerevisiae, requires the IPT1 (YDR072c) gene. J. Biol. Chem. 272 (1997) 29620–29625. [DOI] [PMID: 9368028] |
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[EC 2.7.1.228 created 2019] |
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EC |
2.7.8.3 |
Accepted name: |
ceramide cholinephosphotransferase |
Reaction: |
CDP-choline + a ceramide = CMP + sphingomyelin |
Glossary: |
a ceramide = an N-acylsphingosine |
Other name(s): |
phosphorylcholine-ceramide transferase |
Systematic name: |
CDP-choline:N-acylsphingosine cholinephosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-14-6 |
References: |
1. |
Kennedy, E.P. Phosphorylcholine-glyceride transferase. Methods Enzymol. 5 (1962) 484–486. |
2. |
Sribney, M. and Kennedy, E.P. The enzymatic synthesis of sphingomyelin. J. Biol. Chem. 233 (1958) 1315–1322. [PMID: 13610834] |
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[EC 2.7.8.3 created 1965] |
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EC |
2.7.8.27 |
Accepted name: |
sphingomyelin synthase |
Reaction: |
a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol |
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For diagram of reaction, click here |
Glossary: |
sphingomyelin = a ceramide-1-phosphocholine
ceramide = an N-acylsphingoid. The fatty acids of naturally occurring ceramides range in chain length from about C16 to about C26 and may contain one or more double bonds and/or hydroxy substituents at C-2
sphingoid = sphinganine, i.e. D-erythro-2-aminooctadecane-1,3-diol, and its homologues and stereoisomers (see also Lip-1.4) |
Other name(s): |
SM synthase; SMS1; SMS2 |
Systematic name: |
ceramide:phosphatidylcholine cholinephosphotransferase |
Comments: |
The reaction can occur in both directions [3]. This enzyme occupies a central position in sphingolipid and glycerophospholipid metabolism [4]. Up- and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signalling in a variety of mammalian cell types [4]. Unlike EC 2.7.8.3, ceramide cholinephosphotransferase, CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 58703-97-2 |
References: |
1. |
Ullman, M.D. and Radin, N.S. The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver. J. Biol. Chem. 249 (1974) 1506–1512. [PMID: 4817756] |
2. |
Voelker, D.R. and Kennedy, E.P. Cellular and enzymic synthesis of sphingomyelin. Biochemistry 21 (1982) 2753–2759. [PMID: 7093220] |
3. |
Huitema, K., van den Dikkenberg, J., Brouwers, J.F. and Holthuis, J.C. Identification of a family of animal sphingomyelin synthases. EMBO J. 23 (2004) 33–44. [DOI] [PMID: 14685263] |
4. |
Tafesse, F.G., Ternes, P. and Holthuis, J.C. The multigenic sphingomyelin synthase family. J. Biol. Chem. 281 (2006) 29421–29425. [DOI] [PMID: 16905542] |
5. |
Yamaoka, S., Miyaji, M., Kitano, T., Umehara, H. and Okazaki, T. Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J. Biol. Chem. 279 (2004) 18688–18693. [DOI] [PMID: 14976195] |
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[EC 2.7.8.27 created 2006] |
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EC |
2.7.8.48 |
Accepted name: |
ceramide phosphoethanolamine synthase |
Reaction: |
CDP-ethanolamine + a ceramide = a ceramide phosphorylethanolamine + CMP |
Other name(s): |
Cpes (gene name); CPE synthase |
Systematic name: |
CDP-ethanolamine:ceramide phosphoethanolaminyltransferase |
Comments: |
The enzyme, studied from the fly Drosophila melanogaster, has homologues among the invertebrates, but not in other animal phyla. Its product, ceramide phosphoethanolamine, is synthesized as the main sphingolipid in cell membranes of arthropods, such as Drosophila and Musca, and is common in worms, bees, spiders, and scorpions. It has also been reported in deep-sea mussels and some sea snails, as well as protozoans and oomycetes. The enzyme requires a Mn(II) cofactor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Vacaru, A.M., Tafesse, F.G., Ternes, P., Kondylis, V., Hermansson, M., Brouwers, J.F., Somerharju, P., Rabouille, C. and Holthuis, J.C. Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER. J. Cell Biol. 185 (2009) 1013–1027. [DOI] [PMID: 19506037] |
2. |
Vacaru, A.M., van den Dikkenberg, J., Ternes, P. and Holthuis, J.C. Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen. J. Biol. Chem. 288 (2013) 11520–11530. [DOI] [PMID: 23449981] |
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[EC 2.7.8.48 created 2022] |
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EC |
2.8.2.11 |
Accepted name: |
galactosylceramide sulfotransferase |
Reaction: |
3′-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3′,5′-bisphosphate + a galactosylceramidesulfate |
Glossary: |
3′-phosphoadenylyl sulfate = PAPS |
Other name(s): |
GSase; 3′-phosphoadenosine-5′-phosphosulfate-cerebroside sulfotransferase; galactocerebroside sulfotransferase; galactolipid sulfotransferase; glycolipid sulfotransferase; glycosphingolipid sulfotransferase; 3′-phosphoadenylyl-sulfate:galactosylceramide 3′-sulfotransferase |
Systematic name: |
3′-phosphoadenylyl-sulfate:galactosylceramide 3′-sulfonotransferase |
Comments: |
Also acts on lactosylceramide. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9081-06-5 |
References: |
1. |
McKhann, G.M., Levy, R. and Ho, W. Metabolism of sulfatides. I. The effect of galactocerebrosides on the synthesis of sulfatides. Biochem. Biophys. Res. Commun. 20 (1965) 109–113. [DOI] [PMID: 5850675] |
2. |
Sakakibara, N., Gasa, S., Kamio, K., Makita, A. and Koyanagi, T. Association of elevated sulfatides and sulfotransferase activities with human renal cell carcinoma. Cancer Res. 49 (1989) 335–339. [PMID: 2562926] |
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[EC 2.8.2.11 created 1972, modified 1976] |
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EC |
3.1.4.12 |
Accepted name: |
sphingomyelin phosphodiesterase |
Reaction: |
a sphingomyelin + H2O = a ceramide + phosphocholine |
Glossary: |
a ceramide = an N-acylsphingosine |
Other name(s): |
neutral sphingomyelinase |
Systematic name: |
sphingomyelin cholinephosphohydrolase |
Comments: |
Has very little activity on phosphatidylcholine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-54-3 |
References: |
1. |
Barnholz, Y., Roitman, A. and Gatt, S. Enzymatic hydrolysis of sphingolipids. II. Hydrolysis of sphingomyelin by an enzyme from rat brain. J. Biol. Chem. 241 (1966) 3731–3737. [PMID: 5916388] |
2. |
Chatterjee, S. and Ghosh, N. Neutral sphingomyelinase from human urine. Purification and preparation of monospecific antibodies. J. Biol. Chem. 264 (1989) 12554–12561. [PMID: 2545711] |
3. |
Heller, M. and Shapiro, B. Enzymic hydrolysis of sphingomyelin by rat liver. Biochem. J. 98 (1966) 763–769. [PMID: 5911524] |
4. |
Kanfer, J.N., Young, O.M., Shapiro, D. and Brady, R.O. The metabolism of sphingomyelin. I. Purification and properties of a sphingomyelin-cleaving enzyme from rat liver tissue. J. Biol. Chem. 241 (1966) 1081–1084. [PMID: 5933867] |
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[EC 3.1.4.12 created 1972] |
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EC |
3.1.4.41 |
Accepted name: |
sphingomyelin phosphodiesterase D |
Reaction: |
sphingomyelin + H2O = ceramide phosphate + choline |
Other name(s): |
sphingomyelinase D |
Systematic name: |
sphingomyelin ceramide-phosphohydrolase |
Comments: |
Does not act on phosphatidylcholine, but hydrolyses 2-lysophosphatidylcholine to choline and 2-lysophosphatidate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54992-31-3 |
References: |
1. |
Carne, H.R. and Onon, E. Action of Corynebacterium ovis exotoxin on endothelial cells of blood vessels. Nature 271 (1978) 246–248. [PMID: 622164] |
2. |
Soucek, A., Michalec, C. and Souckov, A. Identification and characterization of a new enzyme of the group phospholipase D isolated from Corynebacterium ovis. Biochim. Biophys. Acta 227 (1971) 116–128. [DOI] [PMID: 5543581] |
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[EC 3.1.4.41 created 1978] |
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EC |
3.2.1.45 |
Accepted name: |
glucosylceramidase |
Reaction: |
a D-glucosyl-N-acylsphingosine + H2O = D-glucose + a ceramide |
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For diagram of glycolipid biosynthesis, click here |
Glossary: |
a ceramide = an N-acylsphingosine |
Other name(s): |
psychosine hydrolase; glucosphingosine glucosylhydrolase; GlcCer-β-glucosidase; β-D-glucocerebrosidase; glucosylcerebrosidase; β-glucosylceramidase; ceramide glucosidase; glucocerebrosidase; glucosylsphingosine β-glucosidase; glucosylsphingosine β-D-glucosidase |
Systematic name: |
D-glucosyl-N-acylsphingosine glucohydrolase |
Comments: |
Also acts on glucosylsphingosine (cf. EC 3.2.1.62 glycosylceramidase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37228-64-1 |
References: |
1. |
Brady, R.O., Kanfer, J.N. and Shapiro, D. The metabolism of glucocerebrosides. I. Preparation and properties of a glucocerebroside-cleaving enzyme from spleen tissue. J. Biol. Chem. 240 (1966) 39–43. [PMID: 14253443] |
2. |
Vaccaro, A.M., Muscillo, M. and Suzuki, K. Characterization of human glucosylsphingosine glucosyl hydrolase and comparison with glucosylceramidase. Eur. J. Biochem. 146 (1985) 315–321. [DOI] [PMID: 3967661] |
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[EC 3.2.1.45 created 1972] |
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EC |
3.2.1.46 |
Accepted name: |
galactosylceramidase |
Reaction: |
a D-galactosyl-N-acylsphingosine + H2O = D-galactose + a ceramide |
Glossary: |
a ceramide = an N-acylsphingosine |
Other name(s): |
cerebroside galactosidase; galactocerebroside.β-galactosidase; galactosylcerebrosidase; galactocerebrosidase; ceramide galactosidase; galactocerebroside galactosidase; galactosylceramide.β-galactosidase; cerebroside β-galactosidase; galactosylceramidase I; β-galactosylceramidase; galactocerebroside-β-D-galactosidase; lactosylceramidase I; β-galactocerebrosidase; lactosylceramidase |
Systematic name: |
D-galactosyl-N-acylsphingosine galactohydrolase |
Comments: |
cf. EC 3.2.1.62 glycosylceramidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-89-8 |
References: |
1. |
Brady, R.O., Gal, A.E., Kanfer, J.N. and Bradley, R.M. The metabolism of glucocerebrosides. 3. Purification and properties of a glucosyl- and galactosylceramide-cleaving enzyme from rat intestinal tissue. J. Biol. Chem. 240 (1965) 3766–3770. [PMID: 5320641] |
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[EC 3.2.1.46 created 1972] |
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EC
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3.2.1.47
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Deleted entry: | galactosylgalactosylglucosylceramidase. Now known to be catalyzed by EC 3.2.1.22, α-galactosidase. |
[EC 3.2.1.47 created 1972, modified 2011, deleted 2021] |
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EC |
3.2.1.62 |
Accepted name: |
glycosylceramidase |
Reaction: |
(1) a β-D-glucosyl-N-acylsphingosine + H2O = a ceramide + β-D-glucose (2) a β-D-galactosyl-N-acylsphingosine + H2O = a ceramide + β-D-galactose (3) a flavonoid-O-β-D-glucoside + H2O = a flavonoid + β-D-glucose |
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For diagram of phloretin biosynthesis, click here and for diagram of glycolipid biosynthesis, click here |
Glossary: |
a ceramide = an N-acylsphingosine |
Other name(s): |
phlorizin hydrolase; phloretin-glucosidase; glycosyl ceramide glycosylhydrolase; cerebrosidase; phloridzin β-glucosidase; lactase-phlorizin hydrolase; phloridzin glucosidase; LPH (gene name); LCT (gene name); glycosyl-N-acylsphingosine glycohydrolase |
Systematic name: |
β-D-glucosyl-N-acylsphingosine glycohydrolase (configuration-retaining) |
Comments: |
The enzyme, found in the intestinal mucosa, hydrolyses β-D-glucosyl and β-D-galactosyl residues from a very broad range of substrates using a retaining mechanism. Characterized substrates include glucosyl- and galactosyl-ceramides [3], O3-, O4′ and O7-glucosylated flavonoids [6], and the 2′-O-glucosylated dihydrochalcone phlorizin [1]. The enzyme includes two glycosyl hydrolase domains, both belonging to the GH1 family. While one domain is responsible for the activity described here, the other catalyses the reaction of EC 3.2.1.108, lactase [4,5]. cf. EC 3.2.1.45, glucosylceramidase and EC 3.2.1.46, galactosylceramidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-10-7 |
References: |
1. |
Malathi, P. and Crane, R.K. Phlorizin hydrolase: a β-glucosidase of hamster intestinal brush border membrane. Biochim. Biophys. Acta 173 (1969) 245–256. [DOI] [PMID: 5774775] |
2. |
Lorenz-Meyer, H., Blum, A.L., Haemmerli, H.P. and Semenza, G. A second enzyme defect in acquired lactase deficiency: lack of small-intestinal phlorizin-hydrolase. Eur. J. Clin. Invest. 2 (1972) 326–331. [DOI] [PMID: 5082068] |
3. |
Leese, H.J. and Semenza, G. On the identity between the small intestinal enzymes phlorizin hydrolase and glycosylceramidase. J. Biol. Chem. 248 (1973) 8170–8173. [DOI] [PMID: 4752949] |
4. |
Zecca, L., Mesonero, J.E., Stutz, A., Poiree, J.C., Giudicelli, J., Cursio, R., Gloor, S.M. and Semenza, G. Intestinal lactase-phlorizin hydrolase (LPH): the two catalytic sites; the role of the pancreas in pro-LPH maturation. FEBS Lett. 435 (1998) 225–228. [DOI] [PMID: 9762914] |
5. |
Arribas, J.C., Herrero, A.G., Martin-Lomas, M., Canada, F.J., He, S. and Withers, S.G. Differential mechanism-based labeling and unequivocal activity assignment of the two active sites of intestinal lactase/phlorizin hydrolase. Eur. J. Biochem. 267 (2000) 6996–7005. [DOI] [PMID: 11106409] |
6. |
Nemeth, K., Plumb, G.W., Berrin, J.G., Juge, N., Jacob, R., Naim, H.Y., Williamson, G., Swallow, D.M. and Kroon, P.A. Deglycosylation by small intestinal epithelial cell β-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans. Eur J Nutr 42 (2003) 29–42. [DOI] [PMID: 12594539] |
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[EC 3.2.1.62 created 1972, modified 1976, modified 2022] |
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EC |
3.2.1.123 |
Accepted name: |
endoglycosylceramidase |
Reaction: |
oligoglycosylglucosyl-(1↔1)-ceramide + H2O = ceramide + oligoglycosylglucose |
Other name(s): |
endoglycoceramidase; EGCase; glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase; oligoglycosylglucosylceramide glycohydrolase; oligoglycosylglucosyl(1↔1)ceramide glycohydrolase |
Systematic name: |
oligoglycosylglucosyl-(1↔1)-ceramide glycohydrolase |
Comments: |
An enzyme from Rhodococcus sp. that degrades various acidic and neutral glycosphingolipids to oligosaccharides and ceramides, by cleaving a glucosyl bond. Does not act on monoglycosylceramides. cf. EC 3.2.1.62 glycosylceramidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105503-61-5 |
References: |
1. |
Ito, M. and Yamagata, T. A novel glycosphingolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids. J. Biol. Chem. 261 (1986) 14278–14282. [PMID: 3771534] |
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[EC 3.2.1.123 created 1989] |
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EC |
3.5.1.23 |
Accepted name: |
ceramidase |
Reaction: |
a ceramide + H2O = a carboxylate + sphingosine |
Glossary: |
a ceramide = an N-acylsphingosine |
Other name(s): |
acylsphingosine deacylase; glycosphingolipid ceramide deacylase |
Systematic name: |
N-acylsphingosine amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-06-8 |
References: |
1. |
Nilsson, A. The presence of spingomyelin- and ceramide-cleaving enzymes in the small intestinal tract. Biochim. Biophys. Acta 176 (1969) 339–347. [DOI] [PMID: 5775951] |
2. |
Yavin, E. and Gatt, S. Enzymatic hydrolysis of sphingolipids. 8. Further purification and properties of rat brain ceramidase. Biochemistry 8 (1969) 1692–1698. [PMID: 5805303] |
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[EC 3.5.1.23 created 1972, modified 1990] |
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EC |
3.5.1.69 |
Accepted name: |
glycosphingolipid deacylase |
Reaction: |
Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives |
Other name(s): |
glycosphingolipid ceramide deacylase |
Systematic name: |
glycosphingolipid amidohydrolase |
Comments: |
Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122544-53-0 |
References: |
1. |
Hirabayashi, Y., Kimura, M., Matsumoto, M., Yamamoto, K., Kadowaki, S. and Tochikura, T. A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid ceramide deacylase, which cleaves the linkage between the fatty acid and sphingosine base in glycosphingolipids. J. Biochem. (Tokyo) 103 (1988) 1–4. [PMID: 3360750] |
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[EC 3.5.1.69 created 1990] |
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EC |
3.5.1.109 |
Accepted name: |
sphingomyelin deacylase |
Reaction: |
(1) an N-acyl-sphingosylphosphorylcholine + H2O = a fatty acid + sphingosylphosphorylcholine
(2) a D-glucosyl-N-acylsphingosine + H2O = a fatty acid + D-glucosyl-sphingosine |
Glossary: |
sphingomyelin = N-acyl-sphingosylphosphorylcholine
D-glucosyl-N-acylsphingosine = glucosylceramide |
Other name(s): |
SM deacylase; GcSM deacylase; glucosylceramide sphingomyelin deacylase; sphingomyelin glucosylceramide deacylase; SM glucosylceramide GCer deacylase; SM-GCer deacylase; SMGCer deacylase |
Systematic name: |
N-acyl-sphingosylphosphorylcholine amidohydrolase |
Comments: |
The enzyme is involved in the sphingolipid metabolism in the epidermis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hara, J., Higuchi, K., Okamoto, R., Kawashima, M. and Imokawa, G. High-expression of sphingomyelin deacylase is an important determinant of ceramide deficiency leading to barrier disruption in atopic dermatitis. J. Invest. Dermatol. 115 (2000) 406–413. [DOI] [PMID: 10951276] |
2. |
Higuchi, K., Hara, J., Okamoto, R., Kawashima, M. and Imokawa, G. The skin of atopic dermatitis patients contains a novel enzyme, glucosylceramide sphingomyelin deacylase, which cleaves the N-acyl linkage of sphingomyelin and glucosylceramide. Biochem. J. 350 (2000) 747–756. [PMID: 10970788] |
3. |
Ishibashi, M., Arikawa, J., Okamoto, R., Kawashima, M., Takagi, Y., Ohguchi, K. and Imokawa, G. Abnormal expression of the novel epidermal enzyme, glucosylceramide deacylase, and the accumulation of its enzymatic reaction product, glucosylsphingosine, in the skin of patients with atopic dermatitis. Lab. Invest. 83 (2003) 397–408. [PMID: 12649340] |
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[EC 3.5.1.109 created 2011] |
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EC |
4.6.1.14 |
Accepted name: |
glycosylphosphatidylinositol diacylglycerol-lyase |
Reaction: |
6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol |
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For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here |
Other name(s): |
(glycosyl)phosphatidylinositol-specific phospholipase C; GPI-PLC; GPI-specific phospholipase C; VSG-lipase; glycosyl inositol phospholipid anchor-hydrolyzing enzyme; glycosylphosphatidylinositol-phospholipase C; glycosylphosphatidylinositol-specific phospholipase C; variant-surface-glycoprotein phospholipase C; 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming) |
Systematic name: |
6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase [6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate-forming] |
Comments: |
This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. It is not identical with EC 3.1.4.50, glycosylphosphatidylinositol phospholipase D. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129070-68-4 |
References: |
1. |
Hereld, D., Krakow, J.L., Bangs, J.D., Hart, G.W. and Englund, P.T. A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein. J. Biol. Chem. 261 (1986) 13813–13819. [PMID: 3759991] |
2. |
Carnall, N., Webb, H. and Carrington, M. Mutagenesis study of the glycosylphosphatidylinositol phospholipase C of Trypanosoma brucei. Mol. Biochem. Parasitol. 90 (1997) 423–432. [DOI] [PMID: 9476790] |
3. |
Armah, D.A. and Mensa-Wilmot, K. Tetramerization of glycosylphosphatidylinositol-specific phospholipase C from Trypanosoma brucei. J. Biol. Chem. 275 (2000) 19334–19342. [DOI] [PMID: 10764777] |
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[EC 4.6.1.14 created 1989 as EC 3.1.4.47, transferred 2002 to EC 4.6.1.14] |
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EC |
7.6.2.1 |
Accepted name: |
P-type phospholipid transporter |
Reaction: |
ATP + H2O + phospholipid[side 1] = ADP + phosphate + phospholipid[side 2] |
Other name(s): |
Mg2+-ATPase (ambiguous); flippase (ambiguous); aminophospholipid-transporting ATPase (ambiguous); phospholipid-translocating ATPase (ambiguous); phospholipid-transporting ATPase (ambiguous) |
Systematic name: |
ATP phosphohydrolase (P-type, phospholipid-flipping) |
Comments: |
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other (‘flippase’). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823–832. [PMID: 8136700] |
2. |
Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95–102. [PMID: 8839453] |
3. |
Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429–10434. [DOI] [PMID: 9099684] |
4. |
Auland, M.E., Roufogalis, B.D., Devaux, P.F. and Zachowski, A. Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes. Proc. Natl. Acad. Sci. USA 91 (1994) 10938–10942. [DOI] [PMID: 7971987] |
5. |
Alder-Baerens, N., Lisman, Q., Luong, L., Pomorski, T. and Holthuis, J.C. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17 (2006) 1632–1642. [DOI] [PMID: 16452632] |
6. |
Lopez-Marques, R.L., Poulsen, L.R., Hanisch, S., Meffert, K., Buch-Pedersen, M.J., Jakobsen, M.K., Pomorski, T.G. and Palmgren, M.G. Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA α-subunit. Mol. Biol. Cell 21 (2010) 791–801. [DOI] [PMID: 20053675] |
7. |
Jensen, M.S., Costa, S.R., Duelli, A.S., Andersen, P.A., Poulsen, L.R., Stanchev, L.D., Gourdon, P., Palmgren, M., Günther Pomorski, T. and Lopez-Marques, R.L. Phospholipid flipping involves a central cavity in P4 ATPases. Sci. Rep. 7:17621 (2017). [PMID: 29247234] |
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[EC 7.6.2.1 created 2000 as EC 3.6.3.1 (EC 3.6.3.13 created 2000, incorporated 2001), transferred 2018 to EC 7.6.2.1] |
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