The Enzyme Database

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EC 1.14.13.169      
Transferred entry: sphinganine C4-monooxygenase. Now EC 1.14.18.5, sphingolipid C4-monooxygenase
[EC 1.14.13.169 created 2012, deleted 2015]
 
 
EC 1.14.14.177     
Accepted name: ultra-long-chain fatty acid ω-hydroxylase
Reaction: an ultra-long-chain fatty acid + [reduced NADPH—hemoprotein reductase] + O2 = an ultra-long-chain ω-hydroxy fatty acid + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): CYP4F22 (gene name)
Systematic name: ultra-long-chain fatty acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)
Comments: The enzyme, which is expressed in the epidermis of mammals, catalyses the ω-hydroxylation of ultra-long-chain fatty acids (C28 to C36). The products are incorporated into acylceramides, epidermis-specific ceramide species that are very important for skin barrier formation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohno, Y., Nakamichi, S., Ohkuni, A., Kamiyama, N., Naoe, A., Tsujimura, H., Yokose, U., Sugiura, K., Ishikawa, J., Akiyama, M. and Kihara, A. Essential role of the cytochrome P450 CYP4F22 in the production of acylceramide, the key lipid for skin permeability barrier formation. Proc. Natl. Acad. Sci. USA 112 (2015) 7707–7712. [DOI] [PMID: 26056268]
[EC 1.14.14.177 created 2021]
 
 
EC 1.14.18.5     
Accepted name: sphingolipid C4-monooxygenase
Reaction: a dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Other name(s): sphinganine C4-monooxygenase; sphingolipid C4-hydroxylase; SUR2 (gene name); SBH1 (gene name); SBH2 (gene name); DEGS2 (gene name)
Systematic name: dihydroceramide,ferrocytochrome b5:oxygen oxidoreductase (C4-hydroxylating)
Comments: The enzyme, which belongs to the familiy of endoplasmic reticular cytochrome b5-dependent enzymes, is involved in the biosynthesis of sphingolipids in eukaryotes. Some enzymes are bifunctional and also catalyse EC 1.14.19.17, sphingolipid 4-desaturase [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Haak, D., Gable, K., Beeler, T. and Dunn, T. Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J. Biol. Chem. 272 (1997) 29704–29710. [DOI] [PMID: 9368039]
2.  Grilley, M.M., Stock, S.D., Dickson, R.C., Lester, R.L. and Takemoto, J.Y. Syringomycin action gene SYR2 is essential for sphingolipid 4-hydroxylation in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 11062–11068. [DOI] [PMID: 9556590]
3.  Sperling, P., Ternes, P., Moll, H., Franke, S., Zähringer, U. and Heinz, E. Functional characterization of sphingolipid C4-hydroxylase genes from Arabidopsis thaliana. FEBS Lett. 494 (2001) 90–94. [DOI] [PMID: 11297741]
4.  Ternes, P., Franke, S., Zähringer, U., Sperling, P. and Heinz, E. Identification and characterization of a sphingolipid Δ4-desaturase family. J. Biol. Chem. 277 (2002) 25512–25518. [DOI] [PMID: 11937514]
5.  Mizutani, Y., Kihara, A. and Igarashi, Y. Identification of the human sphingolipid C4-hydroxylase, hDES2, and its up-regulation during keratinocyte differentiation. FEBS Lett. 563 (2004) 93–97. [DOI] [PMID: 15063729]
[EC 1.14.18.5 created 2012 as EC 1.14.13.169, transferred 2015 to EC 1.14.18.5]
 
 
EC 1.14.18.6     
Accepted name: 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase
Reaction: a phytoceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (2′R)-2′-hydroxyphytoceramide + 2 ferricytochrome b5 + H2O
Glossary: a phytoceramide = a (4R)-4-hydroxysphinganine ceramide = an N-acyl-4-hydroxysphinganine
Other name(s): FA2H (gene name); SCS7 (gene name)
Systematic name: (4R)-4-hydroxysphinganine ceramide,ferrocytochrome-b5:oxygen oxidoreductase (fatty acyl 2-hydroxylating)
Comments: The enzyme, characterized from yeast and mammals, catalyses the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis. The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The newly introduced 2-hydroxyl group has R-configuration. cf. EC 1.14.18.7, dihydroceramide fatty acyl 2-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Mitchell, A.G. and Martin, C.E. Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the α-hydroxylation of sphingolipid-associated very long chain fatty acids. J. Biol. Chem. 272 (1997) 28281–28288. [DOI] [PMID: 9353282]
2.  Dunn, T.M., Haak, D., Monaghan, E. and Beeler, T.J. Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain. Yeast 14 (1998) 311–321. [DOI] [PMID: 9559540]
3.  Alderson, N.L., Rembiesa, B.M., Walla, M.D., Bielawska, A., Bielawski, J. and Hama, H. The human FA2H gene encodes a fatty acid 2-hydroxylase. J. Biol. Chem. 279 (2004) 48562–48568. [DOI] [PMID: 15337768]
4.  Eckhardt, M., Yaghootfam, A., Fewou, S.N., Zoller, I. and Gieselmann, V. A mammalian fatty acid hydroxylase responsible for the formation of α-hydroxylated galactosylceramide in myelin. Biochem. J. 388 (2005) 245–254. [DOI] [PMID: 15658937]
5.  Guo, L., Zhang, X., Zhou, D., Okunade, A.L. and Su, X. Stereospecificity of fatty acid 2-hydroxylase and differential functions of 2-hydroxy fatty acid enantiomers. J. Lipid Res. 53 (2012) 1327–1335. [DOI] [PMID: 22517924]
[EC 1.14.18.6 created 2015]
 
 
EC 1.14.18.7     
Accepted name: dihydroceramide fatty acyl 2-hydroxylase
Reaction: a dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (2′R)-2′-hydroxydihydroceramide + 2 ferricytochrome b5 + H2O
Glossary: a dihydroceramide = an N-acylsphinganine
Other name(s): FAH1 (gene name); FAH2 (gene name); plant sphingolipid fatty acid 2-hydroxylase
Systematic name: dihydroceramide,ferrocytochrome-b5:oxygen oxidoreductase (fatty acyl 2-hydroxylating)
Comments: The enzyme, characterized from plants, catalyses the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to sphinganine during de novo ceramide synthesis. The enzyme requires an external cytochrome b5 as the electron donor. The newly introduced 2-hydroxyl group has R-configuration. cf. EC 1.14.18.6, 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nagano, M., Ihara-Ohori, Y., Imai, H., Inada, N., Fujimoto, M., Tsutsumi, N., Uchimiya, H. and Kawai-Yamada, M. Functional association of cell death suppressor, Arabidopsis Bax inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b5. Plant J. 58 (2009) 122–134. [DOI] [PMID: 19054355]
2.  Nagano, M., Takahara, K., Fujimoto, M., Tsutsumi, N., Uchimiya, H. and Kawai-Yamada, M. Arabidopsis sphingolipid fatty acid 2-hydroxylases (AtFAH1 and AtFAH2) are functionally differentiated in fatty acid 2-hydroxylation and stress responses. Plant Physiol. 159 (2012) 1138–1148. [DOI] [PMID: 22635113]
3.  Nagano, M., Uchimiya, H. and Kawai-Yamada, M. Plant sphingolipid fatty acid 2-hydroxylases have unique characters unlike their animal and fungus counterparts. Plant Signal. Behav. 7 (2012) 1388–1392. [DOI] [PMID: 22918503]
[EC 1.14.18.7 created 2015]
 
 
EC 1.14.19.17     
Accepted name: sphingolipid 4-desaturase
Reaction: a dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E)-sphing-4-enine ceramide + 2 ferricytochrome b5 + 2 H2O
Glossary: a dihydroceramide = an N-acylsphinganine
Other name(s): dehydroceramide desaturase
Systematic name: dihydroceramide,ferrocytochrome b5:oxygen oxidoreductase (4,5-dehydrogenating)
Comments: The enzyme, which has been characterized from plants, fungi, and mammals, generates a trans double bond at position 4 of sphinganine bases in sphingolipids [1]. The preferred substrate is dihydroceramide, but the enzyme is also active with dihydroglucosylceramide [2]. Unlike EC 1.14.19.29, sphingolipid 8-desaturase, this enzyme does not contain an integral cytochrome b5 domain [4] and requires an external cytochrome b5 [3]. The product serves as an important signalling molecules in mammals and is required for spermatide differentiation [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Stoffel, W., Assmann, G. and Bister, K. Metabolism of sphingosine bases. XVII. Stereospecificities in the introduction of the 4t-double bond into sphinganine yielding 4t-sphingenine (sphingosine). Hoppe-Seylers Z. Physiol. Chem. 352 (1971) 1531–1544. [PMID: 5140816]
2.  Michel, C., van Echten-Deckert, G., Rother, J., Sandhoff, K., Wang, E. and Merrill, A.H., Jr. Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide. J. Biol. Chem. 272 (1997) 22432–22437. [DOI] [PMID: 9312549]
3.  Causeret, C., Geeraert, L., Van der Hoeven, G., Mannaerts, G.P. and Van Veldhoven, P.P. Further characterization of rat dihydroceramide desaturase: tissue distribution, subcellular localization, and substrate specificity. Lipids 35 (2000) 1117–1125. [DOI] [PMID: 11104018]
4.  Ternes, P., Franke, S., Zähringer, U., Sperling, P. and Heinz, E. Identification and characterization of a sphingolipid Δ4-desaturase family. J. Biol. Chem. 277 (2002) 25512–25518. [DOI] [PMID: 11937514]
5.  Michaelson, L.V., Zäuner, S., Markham, J.E., Haslam, R.P., Desikan, R., Mugford, S., Albrecht, S., Warnecke, D., Sperling, P., Heinz, E. and Napier, J.A. Functional characterization of a higher plant sphingolipid Δ4-desaturase: defining the role of sphingosine and sphingosine-1-phosphate in Arabidopsis. Plant Physiol. 149 (2009) 487–498. [DOI] [PMID: 18978071]
[EC 1.14.19.17 created 2015]
 
 
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 1.14.19.29     
Accepted name: sphingolipid 8-(E/Z)-desaturase
Reaction: (1) a (4R)-4-hydroxysphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R,8E)-4-hydroxysphing-8-enine ceramide + 2 ferricytochrome b5 + 2 H2O
(2) a (4R)-4-hydroxysphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R,8Z)-4-hydroxysphing-8-enine ceramide + 2 ferricytochrome b5 + 2 H2O
Glossary: a (4R)-4-hydroxysphinganine-ceramide = a phytoceramide
(4R)-4-hydroxysphinganine = phytosphinganine
Other name(s): 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous)
Systematic name: (4R)-4-hydroxysphinganine ceramide,ferrocytochrome b5:oxygen oxidoreductase (8,9 cis/trans-dehydrogenating)
Comments: The enzymes from higher plants convert sphinganine, 4E-sphing-4-enine and phytosphinganine into E/Z-mixtures of Δ8-desaturated products displaying different proportions of geometrical isomers depending on plant species. The nature of the actual desaturase substrate has not yet been studied experimentally. The enzymes contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase [1]. The homologous enzymes from some yeasts and diatoms, EC 1.14.19.18, sphingolipid 8-(E)-desaturase, act on sphing-4-enine ceramides and produce only the trans isomer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sperling, P., Zähringer, U. and Heinz, E. A sphingolipid desaturase from higher plants. Identification of a new cytochrome b5 fusion protein. J. Biol. Chem. 273 (1998) 28590–28596. [DOI] [PMID: 9786850]
2.  Sperling, P., Blume, A., Zähringer, U., and Heinz, E. Further characterization of Δ8-sphingolipid desaturases from higher plants. Biochem Soc Trans. 28 (2000) 638–641. [PMID: 11171153]
3.  Sperling, P., Libisch, B., Zähringer, U., Napier, J.A. and Heinz, E. Functional identification of a Δ8-sphingolipid desaturase from Borago officinalis. Arch. Biochem. Biophys. 388 (2001) 293–298. [DOI] [PMID: 11368168]
4.  Beckmann, C., Rattke, J., Oldham, N.J., Sperling, P., Heinz, E. and Boland, W. Characterization of a Δ8-sphingolipid desaturase from higher plants: a stereochemical and mechanistic study on the origin of E,Z isomers. Angew. Chem. Int. Ed. Engl. 41 (2002) 2298–2300. [DOI] [PMID: 12203571]
5.  Ryan, P.R., Liu, Q., Sperling, P., Dong, B., Franke, S. and Delhaize, E. A higher plant Δ8 sphingolipid desaturase with a preference for (Z)-isomer formation confers aluminum tolerance to yeast and plants. Plant Physiol. 144 (2007) 1968–1977. [DOI] [PMID: 17600137]
6.  Chen, M., Markham, J.E. and Cahoon, E.B. Sphingolipid Δ8 unsaturation is important for glucosylceramide biosynthesis and low-temperature performance in Arabidopsis. Plant J. 69 (2012) 769–781. [DOI] [PMID: 22023480]
[EC 1.14.19.29 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 2.3.1.24     
Accepted name: sphingosine N-acyltransferase
Reaction: acyl-CoA + sphingosine = CoA + a ceramide
Glossary: a ceramide = an N-acylsphingosine
Other name(s): ceramide synthetase; sphingosine acyltransferase
Systematic name: acyl-CoA:sphingosine N-acyltransferase
Comments: Acts on sphingosine or its 2-epimer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37257-09-3
References:
1.  Sribney, M. Enzymatic synthesis of ceramide. Biochim. Biophys. Acta 125 (1966) 542–547. [DOI] [PMID: 5973195]
[EC 2.3.1.24 created 1972]
 
 
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, PDB
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 2.3.1.296     
Accepted name: ω-hydroxyceramide transacylase
Reaction: a linoleate-containing triacyl-sn-glycerol + an ultra-long-chain ω-hydroxyceramide = a diacyl-sn-glycerol + a linoleate-esterified acylceramide
Glossary: an ultra-long-chain fatty acid = ULCFA = a fatty acid with aliphatic chain of 28 or more carbons
an ultra-long-chain ω-hydroxyceramide = a ceramide that contains an ultra-long-chain ω-hydroxyfatty acid moiety (C28-C36)
acylceramide = ω-O-acylceramide = a ceramide that contains an ultra-long-chain ω-hydroxyfatty acid moiety (C28-C36) that is further extended by ω-esterification with linoleic acid.
Other name(s): PNPLA1 (gene name)
Systematic name: triacyl-sn-glycerol:ultra-long-chain ω-hydroxyceramide ω-O-linoleoyltransferase
Comments: The enzyme participates in the production of acylceramides in the stratum corneum, the outermost layer of the epidermis. Acylceramides are crucial components of the skin permeability barrier.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohno, Y., Kamiyama, N., Nakamichi, S. and Kihara, A. PNPLA1 is a transacylase essential for the generation of the skin barrier lipid ω-O-acylceramide. Nat. Commun. 8:14610 (2017). [PMID: 28248318]
[EC 2.3.1.296 created 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 2.4.1.45      
Deleted entry: 2-hydroxyacylsphingosine 1-β-galactosyltransferase, now included with EC 2.4.1.47, N-acylsphingosine galactosyltransferase
[EC 2.4.1.45 created 1972, deleted 2016]
 
 
EC 2.4.1.47     
Accepted name: N-acylsphingosine galactosyltransferase
Reaction: UDP-α-D-galactose + a ceramide = UDP + a β-D-galactosylceramide
Glossary: a ceramide = an N-acylsphingosine
Other name(s): UGT8 (gene name); CGT (gene name); UDP galactose-N-acylsphingosine galactosyltransferase; uridine diphosphogalactose-acylsphingosine galactosyltransferase; UDP-galactose:N-acylsphingosine D-galactosyltransferase; UDP-α-D-galactose:N-acylsphingosine D-galactosyltransferase; 2-hydroxyacylsphingosine 1-β-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acylsphingosine β-D-galactosyltransferase (configuration-inverting)
Comments: This membrane-bound, endoplasmic reticulum-located enzyme catalyses the last step in the synthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. It has a strong preference for ceramides that contain hydroxylated fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-56-8
References:
1.  Fujino, Y. and Nakano, M. Enzymic synthesis of cerebroside from ceramide and uridine diphosphate galactose. Biochem. J. 113 (1969) 573–575. [PMID: 5807218]
2.  Morell, P. and Radin, N.S. Synthesis of cerebroside by brain from uridine diphosphate galactose and ceramide containing hydroxy fatty acid. Biochemistry 8 (1969) 506–512. [PMID: 5793706]
3.  Morell, P., Costantino-Ceccarini, E. and Radin, N.S. The biosynthesis by brain microsomes of cerebrosides containing nonhydroxy fatty acids. Arch. Biochem. Biophys. 141 (1970) 738–748. [DOI] [PMID: 5497154]
4.  Basu, S., Schultz, A., Basu, M. and Roseman, S. Enzymatic synthesis of galactocerebroside by a galactosyltransferase from embryonic chicken brain. J. Biol. Chem. 243 (1971) 4272–4279. [PMID: 5090043]
5.  Akanuma, H. and Kishimoto, Y. Synthesis of ceramides and cerebrosides containing both α-hydroxy and nonhydroxy fatty acids from lignoceroyl-CoA by rat brain microsomes. J. Biol. Chem. 254 (1979) 1050–1060. [PMID: 762114]
6.  Koul, O. and Jungalwala, F.B. UDP-galactose:ceramide galactosyltransferase of rat central-nervous-system myelin. Biochem. J. 194 (1981) 633–637. [PMID: 7306007]
7.  Schulte, S. and Stoffel, W. Ceramide UDP-galactosyltransferase from myelinating rat brain: purification, cloning, and expression. Proc. Natl. Acad. Sci. USA 90 (1993) 10265–10269. [DOI] [PMID: 7694285]
8.  Sprong, H., Kruithof, B., Leijendekker, R., Slot, J.W., van Meer, G. and van der Sluijs, P. UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum. J. Biol. Chem. 273 (1998) 25880–25888. [DOI] [PMID: 9748263]
9.  Fewou, S.N., Bussow, H., Schaeren-Wiemers, N., Vanier, M.T., Macklin, W.B., Gieselmann, V. and Eckhardt, M. Reversal of non-hydroxy:α-hydroxy galactosylceramide ratio and unstable myelin in transgenic mice overexpressing UDP-galactose:ceramide galactosyltransferase. J. Neurochem. 94 (2005) 469–481. [DOI] [PMID: 15998297]
[EC 2.4.1.47 created 1972]
 
 
EC 2.4.1.62     
Accepted name: ganglioside galactosyltransferase
Reaction: UDP-α-D-galactose + an N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis, click here
Glossary: N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = ganglioside GM2
a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
Other name(s): UDP-galactose—ceramide galactosyltransferase; uridine diphosphogalactose-ceramide galactosyltransferase; UDP galactose-LAC Tet-ceramide α-galactosyltransferase; UDP-galactose-GM2 galactosyltransferase; uridine diphosphogalactose-GM2 galactosyltransferase; uridine diphosphate D-galactose:glycolipid galactosyltransferase; UDP-galactose:N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosyl-glucosyl-ceramide galactosyltransferase; UDP-galactose-GM2 ganglioside galactosyltransferase; GM1-synthase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine β-1,3-D-galactosyltransferase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-(1→4)-β-D-glucosyl-N-acylsphingosine 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase
Comments: The substrate is also known as gangloside GM2, the product as gangloside GM1a
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37217-28-0
References:
1.  Basu, S., Kaufman, B. and Roseman, S. Conversion of Tay-Sachs ganglioside to monosialoganglioside by brain uridine diphosphate D-galactose: glycolipid galactosyltransferase. J. Biol. Chem. 240 (1965) 4115–4117. [PMID: 5842076]
2.  Yip, G.B. and Dain, J.A. The enzymic synthesis of ganglioside. II. UDP-galactose: N-acetylgalactosaminyl-(N-acetylneuraminyl)galactosyl-glucosyl-ceramide galactosyltransferase in rat brain. Biochim. Biophys. Acta 206 (1970) 252–260. [DOI] [PMID: 4987145]
3.  Yip, M.C.M. and Dain, J.A. Frog brain uridine diphosphate galactose-N-acetylgalactosaminyl-N-acetylneuraminylgalactosylglucosylceramide galactosyltransferase. Biochem. J. 118 (1970) 247–252. [PMID: 5484669]
[EC 2.4.1.62 created 1972, modified 2013]
 
 
EC 2.4.1.69     
Accepted name: type 1 galactoside α-(1,2)-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R
For diagram of lactotetraosylceramide biosynthesis, click here
Other name(s): galactoside 2-α-L-fucosyltransferase (ambiguous); blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase; α-(1→2)-L-fucosyltransferase (ambiguous); α-2-fucosyltransferase (ambiguous); α-2-L-fucosyltransferase (ambiguous); blood-group substance H-dependent fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase (ambiguous); guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase (ambiguous); secretor-type β-galactoside α1→2fucosyltransferase; β-galactoside α1→2fucosyltransferase (ambiguous); GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT2 (gene name); GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 2-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R α-(1,2)-L-fucosyltransferase (configuration-inverting)
Comments: The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 1 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen. In humans the main enzyme performing this reaction is encoded by the FUT2 gene (also known as the Secretor gene), which is also able to act on type 2 substrates (see EC 2.4.1.344). The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56093-23-3
References:
1.  Beyer, T.A. and Hill, R.L. Enzymatic properties of the β-galactoside α1→2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5373–5379. [PMID: 7372640]
2.  Beyer, T.A., Sadler, J.E. and Hill, R.L. Purification to homogeneity of H blood group β-galactoside α1→2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5364–5372. [PMID: 6246105]
3.  Kumazaki, T. and Yoshida, A. Biochemical evidence that secretor gene, Se, is a structural gene encoding a specific fucosyltransferase. Proc. Natl. Acad. Sci. USA 81 (1984) 4193–4197. [DOI] [PMID: 6588382]
4.  Koda, Y., Soejima, M., Wang, B. and Kimura, H. Structure and expression of the gene encoding secretor-type galactoside 2-α-L-fucosyltransferase (FUT2). Eur. J. Biochem. 246 (1997) 750–755. [DOI] [PMID: 9219535]
5.  Wang, G., Boulton, P.G., Chan, N.W., Palcic, M.M. and Taylor, D.E. Novel Helicobacter pylori α1,2-fucosyltransferase, a key enzyme in the synthesis of Lewis antigens. Microbiology 145 (1999) 3245–3253. [DOI] [PMID: 10589734]
[EC 2.4.1.69 created 1972 (EC 2.4.1.89 created 1976, incorporated 1984), modified 2002, modified 2017]
 
 
EC 2.4.1.79     
Accepted name: globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of globotetraosylceramide biosynthesis, click here. For diagram of reaction, click here
Glossary: α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotriaosylceramide = Pk antigen
N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotetraosylceramide = globoside = P antigen
Other name(s): uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase; globoside synthetase; UDP-N-acetylgalactosamine:globotriaosylceramide β-3-N-acetylgalactosaminyltransferase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase; globoside synthase; gUDP-N-acetyl-D-galactosamine:D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide β-N-acetyl-D-galactosaminyltransferase; β3GalNAc-T1; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III3-β-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III3-β-N-acetyl-D-galactosaminyltransferase
Comments: Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity [4]. The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity [3]. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity [3]. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates [4]. For explanation of the superscripted ’3′ in the systematic name, see GL-5.3.4.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-46-1
References:
1.  Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778–1785. [PMID: 4632917]
2.  Ishibashi, T., Kijimoto, S. and Makita, A. Biosynthesis of globoside and Forssman hapten from trihexosylceramide and properties of β-N-acetyl-galactosaminyltransferase of guinea pig kidney. Biochim. Biophys. Acta 337 (1974) 92–106. [DOI] [PMID: 4433547]
3.  Taniguchi, N. and Makita, A. Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide β-3-N-acetylgalactosaminyltransferase, a synthase of human blood group P antigen, from canine spleen. J. Biol. Chem. 259 (1984) 5637–5642. [PMID: 6425294]
4.  Okajima, T., Nakamura, Y., Uchikawa, M., Haslam, D.B., Numata, S.I., Furukawa, K., Urano, T. and Furukawa, K. Expression cloning of human globoside synthase cDNAs. Identification of β3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase. J. Biol. Chem. 275 (2000) 40498–40503. [DOI] [PMID: 10993897]
[EC 2.4.1.79 created 1976, modified 2006]
 
 
EC 2.4.1.80     
Accepted name: ceramide glucosyltransferase
Reaction: UDP-α-D-glucose + an N-acylsphingosine = UDP + a β-D-glucosyl-N-acylsphingosine
For diagram of glycolipid biosynthesis, click here
Other name(s): UDP-glucose:ceramide glucosyltransferase; ceramide:UDP-Glc glucosyltransferase; uridine diphosphoglucose-ceramide glucosyltransferase; ceramide:UDP-glucose glucosyltransferase; glucosylceramide synthase; UDP-glucose:N-acylsphingosine D-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-acylsphingosine β-D-glucosyltransferase (configuration-inverting)
Comments: Sphingosine and dihydrosphingosine can also act as acceptors; CDP-glucose can act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37237-44-8
References:
1.  Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388–1394. [PMID: 4631392]
[EC 2.4.1.80 created 1976]
 
 
EC 2.4.1.86     
Accepted name: N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R
For diagram of lactotetraosylceramide biosynthesis, click here
Other name(s): B3GALT1 (gene name); uridine diphosphogalactose-acetyl-glucosaminylgalactosylglucosylceramide galactosyltransferase; GalT-4; UDP-galactose:N-acetyl-D-glucosaminyl-1,3-D-galactosyl-1,4-D-glucosylceramide β-D-galactosyltransferase; UDP-galactose:N-acetyl-D-glucosaminyl-(1→3)-D-galactosyl-(1→4)-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase; glucosaminylgalactosylglucosylceramide β-galactosyltransferase; UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-R 3-β-D-galactosyltransferase
Comments: The enzyme transfers galactose from UDP-α-D-galactose to the 3-position of substrates with a non-reducing terminal N-acetyl-β-D-glucosamine (β-GlcNAc) residue. It can act on both glycolipids and glycoproteins, generating a structure known as the type 1 histo-blood group antigen precursor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9073-46-5
References:
1.  Basu, M. and Basu, S. Enzymatic synthesis of a tetraglycosylceramide by a galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 247 (1972) 1489–1495. [PMID: 4335001]
2.  Basu, M., Presper, K.A., Basu, S., Hoffman, L.M. and Brooks, S.E. Differential activities of glycolipid glycosyltransferases in Tay-Sachs disease: studies in cultured cells from cerebrum. Proc. Natl. Acad. Sci. USA 76 (1979) 4270–4274. [DOI] [PMID: 291963]
3.  Amado, M., Almeida, R., Carneiro, F., Levery, S.B., Holmes, E.H., Nomoto, M., Hollingsworth, M.A., Hassan, H., Schwientek, T., Nielsen, P.A., Bennett, E.P. and Clausen, H. A family of human β3-galactosyltransferases. Characterization of four members of a UDP-galactose:β-N-acetyl-glucosamine/β-nacetyl-galactosamine β-1,3-galactosyltransferase family. J. Biol. Chem. 273 (1998) 12770–12778. [DOI] [PMID: 9582303]
4.  Amado, M., Almeida, R., Schwientek, T. and Clausen, H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta 1473 (1999) 35–53. [DOI] [PMID: 10580128]
5.  Bardoni, A., Valli, M. and Trinchera, M. Differential expression of β1,3galactosyltransferases in human colon cells derived from adenocarcinomas or normal mucosa. FEBS Lett. 451 (1999) 75–80. [DOI] [PMID: 10356986]
[EC 2.4.1.86 created 1976, modified 2017]
 
 
EC 2.4.1.87     
Accepted name: N-acetyllactosaminide 3-α-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R = UDP + α-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
Other name(s): α-galactosyltransferase; UDP-Gal:β-D-Gal(1,4)-D-GlcNAc α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α-1,3-D-galactosyltransferase; UDP-Gal:Galβ1→4GlcNAc-R α1→3-galactosyltransferase; UDP-galactose-acetyllactosamine α-D-galactosyltransferase; UDPgalactose:β-D-galactosyl-β-1,4-N-acetyl-D-glucosaminyl-glycopeptide α-1,3-D-galactosyltransferase; glucosaminylglycopeptide α-1,3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine α1→3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine galactosyltransferase; uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide galactosyltransferase; β-D-galactosyl-N-acetylglucosaminylglycopeptide α-1,3-galactosyltransferase; UDP-galactose:N-acetyllactosaminide 3-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-1,4-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein and N-acetyllactosamine (β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine), but not on 2′-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 128449-51-4
References:
1.  Basu, M. and Basu, S. Enzymatic synthesis of a blood group B-related pentaglycosylceramide by an α-galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 248 (1973) 1700–1706. [PMID: 4632915]
2.  Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927–12934. [PMID: 3932335]
3.  Blake, D.A. and Goldstein, I.J. An α-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (α-D-galactose-(1→3)-N-acetyllactosamine). J. Biol. Chem. 256 (1981) 5387–5393. [PMID: 6787040]
[EC 2.4.1.87 created 1976, modified 1989, modified 2002 (EC 2.4.1.124 created 1984, incorporated 2002, EC 2.4.1.151 created 1984, incorporated 2002)]
 
 
EC 2.4.1.88     
Accepted name: globoside α-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-α-D-galactosaminyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of globotetraosylceramide biosynthesis, click here
Other name(s): uridine diphosphoacetylgalactosamine-globoside α-acetylgalactosaminyltransferase; Forssman synthase; globoside acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide α-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-(1→3)-D-galactosyl-(1→4)-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide α-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide α-N-acetyl-D-galactosaminyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52037-97-5
References:
1.  Kijimoto, S., Ishibashi, T. and Makita, A. Biosynthesis of Forssman hapten from globoside by α-N-acetylgalactosaminyltransferase of guinea pig tissues. Biochem. Biophys. Res. Commun. 56 (1974) 177–184. [DOI] [PMID: 4823436]
[EC 2.4.1.88 created 1976]
 
 
EC 2.4.1.89      
Deleted entry: galactosylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase. Now included with EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase
[EC 2.4.1.89 created 1976, deleted 1984]
 
 
EC 2.4.1.92     
Accepted name: (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide = UDP + O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis, click here
Glossary: ganglioside GM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside GM3 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside GD3 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→8)-O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide ganglioside GD2 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→8)-O-(N-acetyl-α-neuraminyl)-(2→3)-O-[2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside SM3 = 1-O-[4-O-(3-O-sulfo-β-D-galactopyranosyl)-β-D-glucopyranosyl]-ceramideganglioside SM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-3-O-sulfo-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
Other name(s): uridine diphosphoacetylgalactosamine-ganglioside GM3 acetylgalactosaminyltransferase; ganglioside GM2 synthase; ganglioside GM3 acetylgalactosaminyltransferase; GM2 synthase; UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 1,4-β-N-acetyl-D-galactosaminyltransferase acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase; GM2/GD2-synthase; β-1,4N-acetylgalactosaminyltransferase; asialo-GM2 synthase; GalNAc-T; UDP-N-acetyl-D-galactosamine:(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 4-β-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide 4-β-N-acetyl-D-galactosaminyltransferase
Comments: This enzyme catalyses the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively. Asialo-GM3 [3] and lactosylceramide [2] are also substrates, but glycoproteins and oligosaccharides are not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67338-98-1
References:
1.  Dicesare, J.L. and Dain, J.A. The enzymic synthesis of ganglioside. IV. UDP-N-acetylgalactosamine: (N-acetylneuraminyl)-galactosylglucosyl ceramide N-acetylgalactosaminyltransferase in rat brain. Biochim. Biophys. Acta 231 (1971) 385–393. [DOI] [PMID: 5554906]
2.  Pohlentz, G., Klein, D., Schwarzmann, G., Schmitz, D. and Sandhoff, K. Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases are single enzymes in Golgi vesicles from rat liver. Proc. Natl. Acad. Sci. USA 85 (1988) 7044–7048. [DOI] [PMID: 3140234]
3.  Kazuya, I.-P., Hidari, J.K., Ichikawa, S., Furukawa, K., Yamasaki, M. and Hirabayashi, Y. β1-4N-Acetylgalactosaminyltransferase can synthesize both asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and in vivo: isolation and characterization of a β1-4N-acetylgalactosaminyltransferase cDNA clone from rat ascites hepatoma cell line AH7974F. Biochem. J. 303 (1994) 957–965. [PMID: 7980468]
4.  Hashimoto, Y., Sekine, M., Iwasaki, K. and Suzuki, A. Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 N-acetylgalactosaminyltransferase from mouse liver. J. Biol. Chem. 268 (1993) 25857–25864. [PMID: 8245020]
5.  Nagai, K. and Ishizuka, I. Biosynthesis of monosulfogangliotriaosylceramide and GM2 by N-acetylgalactosaminyltransferase from rat brain. J. Biochem. (Tokyo) 101 (1987) 1115–1127. [PMID: 3115968]
6.  Furukawa, K., Takamiya, K. and Furukawa, K. β1,4-N-Acetylgalactosaminyltransferase—GM2/GD2 synthase: a key enzyme to control the synthesis of brain-enriched complex gangliosides. Biochim. Biophys. Acta 1573 (2002) 356–362. [DOI] [PMID: 12417418]
7.  Yamashita, T., Wu, Y.P., Sandhoff, R., Werth, N., Mizukami, H., Ellis, J.M., Dupree, J.L., Geyer, R., Sandhoff, K. and Proia, R.L. Interruption of ganglioside synthesis produces central nervous system degeneration and altered axon-glial interactions. Proc. Natl. Acad. Sci. USA 102 (2005) 2725–2730. [DOI] [PMID: 15710896]
[EC 2.4.1.92 created 1976, modified 2006]
 
 
EC 2.4.1.149     
Accepted name: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): uridine diphosphoacetylglucosamine-acetyllactosaminide β1→3-acetylglucosaminyltransferase; poly-N-acetyllactosamine extension enzyme; Galβ1→4GlcNAc-R β1→3 N-acetylglucosaminyltransferase; UDP-GlcNAc:GalR β-D-3-N-acetylglucosaminyltransferase; N-acetyllactosamine β(1-3)N-acetylglucosaminyltransferase; UDP-GlcNAc:Galβ1→4GlcNAcβ-Rβ1→3-N-acetylglucosaminyltransferase; GnTE; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosamine β-1,3-acetyl-D-glucosaminyltransferase; β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine 3-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R 3-β N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on glycoproteins, glycolipids, and oligosaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85638-39-7
References:
1.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
2.  Basu, M. and Basu, S. Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by β 1-3- and β 1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma. J. Biol. Chem. 259 (1984) 12557–12562. [PMID: 6238026]
3.  Takeya, A., Hosomi, O. and Kogure, T. The presence of N-acetyllactosamine and lactose: β (1-3)N-acetylglucosaminyltransferase activity in human urine. Jpn. J. Med. Sci. Biol. 38 (1985) 1–8. [PMID: 3160874]
[EC 2.4.1.149 created 1984 (EC 2.4.1.163 created 1989, incorporated 2016), modified 2016]
 
 
EC 2.4.1.150     
Accepted name: N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Glossary: β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = type 2 precursor disaccharide
Other name(s): GCNT2 (gene name); GCNT3 (gene name); IGnT; I-branching β1,6-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-acetyllactosaminide β1→6-acetylglucosaminyltransferase; Galβ1→4GlcNAc-R β1→6 N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: The enzyme acts on poly-N-acetyllactosamine [glycan chains of β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine units connected by β(1,3) linkages] attached to proteins or lipids. It transfers a GlcNAc residue by β(1,6)-linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0
References:
1.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
2.  Basu, M. and Basu, S. Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by β 1-3- and β 1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma. J. Biol. Chem. 259 (1984) 12557–12562. [PMID: 6238026]
3.  Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385–13390. [PMID: 6490658]
4.  Bierhuizen, M.F., Maemura, K., Kudo, S. and Fukuda, M. Genomic organization of core 2 and I branching β-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the β-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology 5 (1995) 417–425. [DOI] [PMID: 7579796]
5.  Ujita, M., McAuliffe, J., Suzuki, M., Hindsgaul, O., Clausen, H., Fukuda, M.N. and Fukuda, M. Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I. J. Biol. Chem. 274 (1999) 9296–9304. [DOI] [PMID: 10092606]
6.  Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215–3221. [DOI] [PMID: 9915862]
[EC 2.4.1.150 created 1984 (EC 2.4.1.164 created 1989, incorporated 2016), modified 2017]
 
 
EC 2.4.1.152     
Accepted name: 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = GDP + β-D-galactosyl-(1→4)-[α-L-fucosyl-(1→3)]-N-acetyl-D-glucosaminyl-R
For diagram of fucosylneolactotetraosylceramide biosynthesis, click here
Other name(s): Lewis-negative α-3-fucosyltransferase; plasma α-3-fucosyltransferase; guanosine diphosphofucose-glucoside α1→3-fucosyltransferase; galactoside 3-fucosyltransferase; GDP-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase; GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase; GDP-β-L-fucose:(1→4)-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R 3-α-L-fucosyltransferase (configuration-inverting)
Comments: Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39279-34-0
References:
1.  Johnson, P.H., Yates, A.D. and Watkins, W.M. Human salivary fucosyltransferase: evidence for two distinct α-3-L-fucosyltransferase activities one of which is associated with the Lewis blood Le gene. Biochem. Biophys. Res. Commun. 100 (1981) 1611–1618. [DOI] [PMID: 7295318]
2.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
3.  Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. C-terminal amino acids of Helicobacter pylori α1,3/4 fucosyltransferases determine type I and type II transfer. J. Biol. Chem. 278 (2003) 21893–21900. [DOI] [PMID: 12676935]
[EC 2.4.1.152 created 1984, modified 2002, modified 2019]
 
 
EC 2.4.1.154      
Deleted entry: globotriosylceramide β-1,6-N-acetylgalactosaminyl-transferase. The enzyme is identical to EC 2.4.1.79, globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase. The reference cited referred to a 1→3 linkage and not to a 1→6 linkage, as indicated in the enzyme entry
[EC 2.4.1.154 created 1986, deleted 2006]
 
 
EC 2.4.1.163      
Transferred entry: β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase, now included in EC 2.4.1.149, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
[EC 2.4.1.163 created 1989, deleted 2016]
 
 
EC 2.4.1.164      
Transferred entry: galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,6-N-acetylglucosaminyltransferase, now included with EC 2.4.1.150, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
[EC 2.4.1.164 created 1989, deleted 2016]
 
 
EC 2.4.1.165     
Accepted name: N-acetylneuraminylgalactosylglucosylceramide β-1,4-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis, click here
Other name(s): uridine diphosphoacetylgalactosamine-acetylneuraminyl(α2→3)galactosyl(β1→4)glucosyl β1→4-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-2,3-α-D-galactosyl-1,4-β-D-glucosylceramide β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2→3)-α-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 4-β-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2→3)-α-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-N-acetylgalactosaminyltransferase
Comments: Requires Mn2+. Only substances containing sialic acid residues can act as acceptors; bovine fetuin is the best acceptor tested.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 109136-50-7
References:
1.  Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778–1785. [PMID: 4632917]
2.  Piller, F., Blanchard, D., Huet, M. and Cartron, J.-P. Identification of a α-NeuAc-(2-3)-β-D-galactopyranosyl N-acetyl-β-D-galactosaminyltransferase in human kidney. Carbohydr. Res. 149 (1986) 171–184. [DOI] [PMID: 2425965]
3.  Takeya, A., Hosomi, O. and Kogure, T. Identification and characterization of UDP-GalNAc: NeuAc α2-3Gal β1-4Glc(NAc) β1-4(GalNAc to Gal)N-acetylgalactosaminyltransferase in human blood plasma. J. Biochem. (Tokyo) 101 (1987) 251–259. [PMID: 3106337]
[EC 2.4.1.165 created 1989]
 
 
EC 2.4.1.179     
Accepted name: lactosylceramide β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-D-glucosyl-R = UDP + β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-R
For diagram of glycolipid biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): uridine diphosphogalactose-lactosylceramide β1→3-galactosyltransferase; UDP-galactose:D-galactosyl-1,4-β-D-glucosyl-R β-1,3-galactosyltransferase; UDP-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase; UDP-α-D-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase
Comments: R may be an oligosaccharide or a glycolipid; lactose can also act as acceptor, but more slowly. Involved in the elongation of oligosaccharide chains, especially in glycolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 106769-64-6
References:
1.  Bailly, P., Piller, F. and Cartron, J.-P. Characterization and specific assay for a galactoside β-3-galactosyltransferase of human kidney. Eur. J. Biochem. 173 (1988) 417–422. [DOI] [PMID: 3129295]
[EC 2.4.1.179 created 1989]
 
 
EC 2.4.1.206     
Accepted name: lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of lactotetraosylceramide biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
lactotriosylceramide = N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): LA2 synthase; β1→3-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lactosylceramide β-acetylglucosaminyltransferase; lactosylceramide β-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-β-D-glucosylceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-80-8
References:
1.  Gottfries, J., Percy, A.K., Maansson, J.-E., Fredman, P., Wilkstrand, C.J., Friedman, H.S., Bigner, D.D. and Svennerholm, L. Glycolipids and glycosyltransferases in permanent cell lines established from human medulloblastomas. Biochim. Biophys. Acta 1081 (1991) 253–261. [DOI] [PMID: 1825612]
2.  Holmes, E.H., Hakomori, S. and Ostrander, G.K. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1→3N-acetylglucosaminyltransferase. J. Biol. Chem. 262 (1987) 15649–15658. [PMID: 2960671]
3.  Percy, A.K., Gottfries, J., Vilbergsson, G., Maansson, J.E. and Svennerholm, J. Glycosphingolipid glycosyltransferases in human fetal brain. J. Neurochem. 56 (1991) 1461–1465. [DOI] [PMID: 1901591]
[EC 2.4.1.206 created 1992]
 
 
EC 2.4.1.228     
Accepted name: lactosylceramide 4-α-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of globotetraosylceramide biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase; globotriaosylceramide/CD77 synthase; histo-blood group Pk UDP-galactose; UDP-galactose:lactosylceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl(1↔1)ceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide 4II-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide 4II-α-D-galactosyltransferase
Comments: For explanation of superscript II in systematic name, see 2-carb.37.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52725-57-2
References:
1.  Bailly, P., Piller, F., Cartron, J.P., Leroy, Y. and Fournet, B. Identification of UDP-galactose: lactose (lactosylceramide) α-4 and β-3 galactosyltransferases in human kidney. Biochem. Biophys. Res. Commun. 141 (1986) 84–91. [DOI] [PMID: 3099784]
2.  Steffensen, R., Carlier, K., Wiels, J., Levery, S.B., Stroud, M., Cedergren, B., Nilsson Sojka, B., Bennett, E.P., Jersild, C. and Clausen, H. Cloning and expression of the histo-blood group Pk UDP-galactose: Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase. Molecular genetic basis of the p phenotype. J. Biol. Chem. 275 (2000) 16723–16729. [DOI] [PMID: 10747952]
3.  Kojima, Y., Fukumoto, S., Furukawa, K., Okajima, T., Wiels, J., Yokoyama, K., Suzuki, Y., Urano, T., Ohta, M. and Furukawa, K. Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J. Biol. Chem. 275 (2000) 15152–15156. [DOI] [PMID: 10748143]
[EC 2.4.1.228 created 2002]
 
 
EC 2.4.1.274     
Accepted name: glucosylceramide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of glycolipid biosynthesis, click here
Other name(s): lactosylceramide synthase; uridine diphosphate-galactose:glucosyl ceramide β 1-4 galactosyltransferase; UDP-Gal:glucosylceramide β1→4galactosyltransferase; GalT-2 (misleading); UDP-galactose:β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase
Comments: Involved in the synthesis of several different major classes of glycosphingolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chatterjee, S. and Castiglione, E. UDPgalactose:glucosylceramide β1→4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes. Biochim. Biophys. Acta 923 (1987) 136–142. [DOI] [PMID: 3099851]
2.  Trinchera, M., Fiorilli, A. and Ghidoni, R. Localization in the Golgi apparatus of rat liver UDP-Gal:glucosylceramide β1→4galactosyltransferase. Biochemistry 30 (1991) 2719–2724. [PMID: 1900430]
3.  Chatterjee, S., Ghosh, N. and Khurana, S. Purification of uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase from human kidney. J. Biol. Chem. 267 (1992) 7148–7153. [PMID: 1551920]
4.  Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Wakisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M. and Matsuo, N. Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide β-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273 (1998) 13570–13577. [DOI] [PMID: 9593693]
5.  Takizawa, M., Nomura, T., Wakisaka, E., Yoshizuka, N., Aoki, J., Arai, H., Inoue, K., Hattori, M. and Matsuo, N. cDNA cloning and expression of human lactosylceramide synthase. Biochim. Biophys. Acta 1438 (1999) 301–304. [DOI] [PMID: 10320813]
[EC 2.4.1.274 created 2011]
 
 
EC 2.4.1.275     
Accepted name: neolactotriaosylceramide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of neolactotetraosylceramide biosynthesis, click here
Glossary: N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = neolactotriaosylceramide
Other name(s): β4Gal-T4; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase; lactotriaosylceramide β-1,4-galactosyltransferase (incorrect)
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331–29340. [DOI] [PMID: 9792633]
[EC 2.4.1.275 created 2011, modified 2013]
 
 
EC 2.4.1.344     
Accepted name: type 2 galactoside α-(1,2)-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase (ambiguous); α-(1→2)-L-fucosyltransferase (ambiguous); α-2-fucosyltransferase (ambiguous); α-2-L-fucosyltransferase (ambiguous); blood-group substance H-dependent fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase (ambiguous); guanosine diphosphofucose-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase (ambiguous); H-gene-encoded β-galactoside α(1→2)fucosyltransferase; β-galactoside α(1→2)fucosyltransferase (ambiguous); GDP-L-fucose:lactose fucosyltransferase; GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT1 (gene name); FUT2 (gene name)
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R α-(1,2)-L-fucosyltransferase (configuration-inverting)
Comments: The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956–2962. [PMID: 804484]
2.  Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351–353.
3.  Ernst, L.K., Rajan, V.P., Larsen, R.D., Ruff, M.M. and Lowe, J.B. Stable expression of blood group H determinants and GDP-L-fucose: β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264 (1989) 3436–3447. [PMID: 2464598]
4.  Larsen, R.D., Ernst, L.K., Nair, R.P. and Lowe, J.B. Molecular cloning, sequence, and expression of a human GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc. Natl. Acad. Sci. USA 87 (1990) 6674–6678. [DOI] [PMID: 2118655]
[EC 2.4.1.344 created 2017]
 
 
EC 2.4.1.370     
Accepted name: inositol phosphorylceramide mannosyltransferase
Reaction: GDP-α-D-mannose + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine = 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 + GDP
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
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
Other name(s): SUR1 (gene name); CSH1 (gene name)
Systematic name: GDP-α-D-mannose:(4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine mannosyltransferase (configuration-retaining)
Comments: The simplest complex sphingolipid of yeast, inositol-phospho-α-hydroxyphytoceramide (IPC), is usually mannosylated to yield mannosyl-inositol-phospho-α hydroxyphytoceramide (MIPC). The enzyme is located in the Golgi apparatus, and utilizes GDP-mannose as the mannosyl group donor. It consists of a catalytic subunit (SUR1 or CSH1) and a regulatory subunit (CSG2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Beeler, T.J., Fu, D., Rivera, J., Monaghan, E., Gable, K. and Dunn, T.M. SUR1 (CSG1/BCL21), a gene necessary for growth of Saccharomyces cerevisiae in the presence of high Ca2+ concentrations at 37 degrees C, is required for mannosylation of inositolphosphorylceramide. Mol. Gen. Genet. 255 (1997) 570–579. [DOI] [PMID: 9323360]
2.  Dean, N., Zhang, Y.B. and Poster, J.B. The VRG4 gene is required for GDP-mannose transport into the lumen of the Golgi in the yeast, Saccharomyces cerevisiae. J. Biol. Chem. 272 (1997) 31908–31914. [DOI] [PMID: 9395539]
3.  Uemura, S., Kihara, A., Inokuchi, J. and Igarashi, Y. Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p. J. Biol. Chem. 278 (2003) 45049–45055. [DOI] [PMID: 12954640]
[EC 2.4.1.370 created 2019]
 
 
EC 2.4.3.1     
Accepted name: β-galactoside α-(2,6)-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + β-D-galactosyl-R = CMP + N-acetyl-α-neuraminyl-(2→6)-β-D-galactosyl-R
Other name(s): ST6Gal-I; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; lactosylceramide α-2,6-N-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine α-(2→6)-N-acetylneuraminyltransferase; β-galactoside α-2,6-sialyltransferase
Systematic name: CMP-N-acetyl-β-neuraminate:β-D-galactoside α-(2→6)-N-acetylneuraminyltransferase (configuration-inverting)
Comments: The enzyme acts on the terminal non-reducing β-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-81-4
References:
1.  Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase. J. Biol. Chem. 243 (1968) 6520–6528. [PMID: 5726897]
2.  Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H. Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin. J. Biol. Chem. 245 (1970) 759–766. [PMID: 4313609]
3.  Bartholomew, B.A., Jourdian, G.W. and Roseman, S. The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum. J. Biol. Chem. 248 (1973) 5751–5762. [PMID: 4723915]
4.  Paulson, J.C., Beranek, W.E. and Hill, R.L. Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. J. Biol. Chem. 252 (1977) 2356–2362. [PMID: 849932]
5.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
6.  Albarracin, I., Lassaga, F.E. and Caputto, R. Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biochem. J. 254 (1988) 559–565. [PMID: 2460092]
[EC 2.4.3.1 created 1972 as EC 2.4.99.1, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2016), modified 2017, transferred 2021 to EC 2.4.3.1]
 
 
EC 2.4.3.2     
Accepted name: β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R = CMP + an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R
For diagram of ganglioside biosynthesis, click here
Glossary: a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GD1a
Other name(s): CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide N-acetylneuraminyltransferase (ambiguous); monosialoganglioside sialyltransferase; CMP-N-acetylneuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide N-acetyl-β-neuraminyltransferase
Systematic name: CMP-N-acetyl-β-neuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R α-(2→3)-N-acetylneuraminyltransferase (configuration-inverting)
Comments: The enzyme recognizes the sequence β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids [1]. When acting on gangloside GM1a, it forms gangloside GD1a [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-12-2
References:
1.  Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198]
2.  Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5′-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM1) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298–306. [DOI] [PMID: 4351506]
[EC 2.4.3.2 created 1976 as EC 2.4.99.2, modified 1986, modified 2017, transferred 2022 to EC 2.4.3.2]
 
 
EC 2.4.3.6     
Accepted name: N-acetyllactosaminide α-2,3-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): cytidine monophosphoacetylneuraminate-β-galactosyl(1→4)acetylglucosaminide α2→3-sialyltransferase; α2→3 sialyltransferase (ambiguous); SiaT (ambiguous); CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein α-2,3-N-acetylneuraminyltransferase; neolactotetraosylceramide α-2,3-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-glycoprotein α-(2→3)-N-acetylneuraminyltransferase
Systematic name: CMP-N-acetyl-β-neuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R (2→3)-N-acetyl-α-neuraminyltransferase (configuration-inverting)
Comments: The enzyme recognizes the sequence β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl (known as type 2 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids. The enzyme from chicken brain was shown to act on neolactotetraosylceramide, producing ganglioside LM1 [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77537-85-0
References:
1.  Van den Eijnden, D.H. and Schiphorst, W.E.C.M. Detection of β-galactosyl(1→4)N-acetylglucosaminide α(2→3)-sialyltransferase activity in fetal calf liver and other tissues. J. Biol. Chem. 256 (1981) 3159–3162. [PMID: 7204397]
2.  Basu, M., Basu, S., Stoffyn, A. and Stoffyn, P. Biosynthesis in vitro of sialyl(α2-3)neolactotetraosylceramide by a sialyltransferase from embryonic chicken brain. J. Biol. Chem. 257 (1982) 12765–12769. [PMID: 7130178]
[EC 2.4.3.6 created 1984 as EC 2.4.99.6, modified 1986 (EC 2.4.99.10 created 1986, incorporated 2017), transferred 2022 to EC 2.4.3.6]
 
 
EC 2.4.3.8     
Accepted name: α-N-acetylneuraminate α-2,8-sialyltransferase
Reaction: CMP-N-acetylneuraminate + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R = CMP + α-N-acetylneuraminyl-(2→8)-α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R
For diagram of ganglioside biosynthesis (pathway to GD3), click here
Other name(s): cytidine monophosphoacetylneuraminate-ganglioside GM3; α-2,8-sialyltransferase; ganglioside GD3 synthase; ganglioside GD3 synthetase sialyltransferase; CMP-NeuAc:LM1(α2-8) sialyltranferase; GD3 synthase; SAT-2
Systematic name: CMP-N-acetylneuraminate:α-N-acetylneuraminyl-(2→3)-β-D-galactoside α-(2→8)-N-acetylneuraminyltransferase
Comments: Gangliosides act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67339-00-8
References:
1.  Eppler, M.C., Morré, J.D. and Keenan, T.W. Ganglioside biosynthesis in rat liver: alteration of sialyltransferase activities by nucleotides. Biochim. Biophys. Acta 619 (1980) 332–343. [DOI] [PMID: 7407217]
2.  Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824–828. [PMID: 3838172]
3.  McCoy, R.D., Vimr, E.R. and Troy, F.A. CMP-NeuNAc:poly-α-2,8-sialosyl sialyltransferase and the biosynthesis of polysialosyl units in neural cell adhesion molecules. J. Biol. Chem. 260 (1985) 12695–12699. [PMID: 4044605]
4.  Yohe, H.C. and Yu, R.K. In vitro biosynthesis of an isomer of brain trisialoganglioside, GT1a. J. Biol. Chem. 255 (1980) 608–613. [PMID: 6766128]
[EC 2.4.3.8 created 1984 as EC 2.4.99.8, modified 1986, transferred 2022 to EC 2.4.3.8]
 
 
EC 2.4.3.9     
Accepted name: lactosylceramide α-2,3-sialyltransferase
Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis (pathway to GM2), click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): cytidine monophosphoacetylneuraminate-lactosylceramide α2,3- sialyltransferase; CMP-acetylneuraminate-lactosylceramide-sialyltransferase; CMP-acetylneuraminic acid:lactosylceramide sialyltransferase; CMP-sialic acid:lactosylceramide-sialyltransferase; cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase; ganglioside GM3 synthetase; GM3 synthase; GM3 synthetase; SAT 1; CMP-N-acetylneuraminate:lactosylceramide α-2,3-N-acetylneuraminyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide α-(2→3)-N-acetylneuraminyltransferase
Systematic name: CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide α-(2→3)-N-acetylneuraminyltransferase
Comments: Lactose cannot act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-90-1
References:
1.  Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388–1394. [PMID: 4631392]
2.  Fishman, P.H., Bradley, R.M. and Henneberry, R.C. Butyrate-induced glycolipid biosynthesis in HeLa cells: properties of the induced sialyltransferase. Arch. Biochem. Biophys. 172 (1976) 618–626. [DOI] [PMID: 4022]
3.  Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824–828. [PMID: 3838172]
[EC 2.4.3.9 created 1984 as EC 2.4.99.9, modified 1986, transferred 2022 to EC 2.4.3.9]
 
 
EC 2.4.99.1      
Transferred entry: β-galactoside α-(2,6)-sialyltransferase. Now EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase
[EC 2.4.99.1 created 1972, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2017), deleted 2022]
 
 
EC 2.4.99.2      
Transferred entry: β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase. Now EC 2.4.3.2, β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
[EC 2.4.99.2 created 1976, modified 1986, deleted 2022]
 
 
EC 2.4.99.6      
Transferred entry: N-acetyllactosaminide α-2,3-sialyltransferase. Now EC 2.4.3.6, N-acetyllactosaminide α-2,3-sialyltransferase
[EC 2.4.99.6 created 1984, modified 1986 (EC 2.4.99.10 created 1986, incorporated 2017), deleted 2022]
 
 
EC 2.4.99.8      
Transferred entry: α-N-acetylneuraminate α-2,8-sialyltransferase. Now EC 2.4.3.8, α-N-acetylneuraminate α-2,8-sialyltransferase
[EC 2.4.99.8 created 1984, modified 1986, deleted 2022]
 
 


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