EC 2.4.1.22     
Accepted name: lactose synthase
Reaction: UDP-α-D-galactose + D-glucose = UDP + lactose
Other name(s): UDP-galactose—glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:D-glucose 4-β-D-galactosyltransferase
Comments: The enzyme is a complex of two proteins, A and B. In the absence of the B protein (α-lactalbumin), the enzyme catalyses the transfer of galactose from UDP-α-D-galactose to N-acetylglucosamine (EC 2.4.1.90 N-acetyllactosamine synthase).
References:
1.  Fitzgerald, D.K., Brodbeck, U., Kiyosawa, I., Mawal, R., Colvin, B. and Ebner, K.E. α-Lactalbumin and the lactose synthetase reaction. J. Biol. Chem. 245 (1970) 2103–2108. [PMID: 5440844]
2.  Hill, R.L. and Brew, K. Lactose synthetase. Adv. Enzymol. Relat. Areas Mol. Biol. 43 (1975) 411–490. [PMID: 812340]
3.  Watkins, W.M. and Hassid, W.Z. The synthesis of lactose by particulate enzyme preparations from guinea pig and bovine mammary glands. J. Biol. Chem. 237 (1962) 1432–1440. [PMID: 14005251]
[EC 2.4.1.22 created 1965]
 
 
EC 2.4.1.220     
Accepted name: indoxyl-UDPG glucosyltransferase
Reaction: UDP-glucose + indoxyl = UDP + indican
Glossary: indoxyl = indole-3-ol
Other name(s): indoxyl-UDPG-glucosyltransferase
Systematic name: UDP-glucose:indoxyl 3-O-β-D-glucosyltransferase
Comments: Also acts to a limited extent on 4-, 5-, 6- and 7-hydroxyindole. After enzymic or chemical hydrolysis, indican forms indoxyl, which, in turn, is converted in the presence of oxygen to the dye indigo.
References:
1.  Marcinek, H., Weyler, W., Deus-Neumann, B. and Zenk, M.H. Indoxyl-UDPG-glucosyltransferase from Baphicacanthus cusia. Phytochemistry 53 (2000) 201–207. [PMID: 10680172]
[EC 2.4.1.220 created 2002]
 
 
EC 2.4.1.221     
Accepted name: peptide-O-fucosyltransferase
Reaction: transfers an α-L-fucosyl residue from GDP-β-L-fucose to the serine hydroxy group of a protein acceptor
Other name(s): GDP-L-fucose:polypeptide fucosyltransferase; GDP-fucose protein O-fucosyltransferase; GDP-fucose:polypeptide fucosyltransferase
Systematic name: GDP-β-L-fucose:polypeptide O-α-L-fucosyltransferase
Comments: Involved in the biosynthesis of O-fucosylated epidermal growth factor (EGF) and thrombospondin type 1 repeats. The attachment of O-linked fucose to serine or threonine occurs on EGF domains within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.
References:
1.  Wang, Y. and Spellman, M.W. Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells. J. Biol. Chem. 273 (1998) 8112–8118. [PMID: 9525914]
2.  Wang, Y., Shao, L., Shi, S., Harris, R.J., Spellman, M.W., Stanley, P. and Haltiwanger, R.S. Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase. J. Biol. Chem. 276 (2001) 40338–40345. [PMID: 11524432]
3.  Wang, Y., Lee, G.F., Kelley, R.F. and Spellman, M.W. Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains. Glycobiology 6 (1996) 837–842. [PMID: 9023546]
4.  Hofsteenge, J., Huwiler, K.G., Macek, B., Hess, D., Lawler, J., Mosher, D.F. and Peter-Katalinic, J. C-mannosylation and O-fucosylation of the thrombospondin type 1 module. J. Biol. Chem. 276 (2001) 6485–6498. [PMID: 11067851]
[EC 2.4.1.221 created 2002]
 
 
EC 2.4.1.222     
Accepted name: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase
Reaction: transfers a β-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
Other name(s): O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase; fringe (ambiguous)
Systematic name: UDP-D-GlcNAc:O-L-fucosylpeptide 3-β-N-acetyl-D-glucosaminyltransferase
Comments: O-Fucosylpeptide 3-β-N-acetylglucosaminyltransferases are the products of fringe genes. O-linked fucose is an unusual form of glycosylation where the fucose is attached directly to proteins through the hydroxy groups of Ser or Thr residues.
References:
1.  Moloney, D.J., Panin, V.M., Johnston, S.H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K.D., Haltiwanger, R.S. and Vogt, T.F. Fringe is a glycosyltransferase that modifies Notch. Nature 406 (2000) 369–375. [PMID: 10935626]
[EC 2.4.1.222 created 2002]
 
 
EC 2.4.1.223     
Accepted name: glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(α-D-GlcNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
Glossary: [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
Other name(s): α-N-acetylglucosaminyltransferase I; α1,4-N-acetylglucosaminyltransferase; glucuronosylgalactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl-proteoglycan 4IV-α-N-acetyl-D-glucosaminyltransferase; glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4IV-α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)
Comments: Enzyme involved in the initiation of heparin and heparan sulfate synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core. Apparently products of both the human EXTL2 and EXTL3 genes can catalyse this reaction. In Caenorhabditis elegans, the product of the rib-2 gene displays this activity as well as that of EC 2.4.1.224, glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase. For explanation of the use of a superscript in the systematic name, see 2-Carb-37.2.
References:
1.  Kitagawa, H., Shimakawa, H. and Sugahara, K. The tumor suppressor EXT-like gene EXTL2 encodes an α1,4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J. Biol. Chem. 274 (1999) 13933–13937. [PMID: 10318803]
2.  Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834–4838. [PMID: 11121397]
[EC 2.4.1.223 created 2002, modified 2016]
 
 
EC 2.4.1.224     
Accepted name: glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan = UDP + N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan
Other name(s): α-N-acetylglucosaminyltransferase II glucuronyl-N-acetylglucosaminylproteoglycan α-1,4-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the enzyme from human (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the 4-β-glucuronosyltransferase (EC 2.4.1.225, N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase) activity required for the synthesis of the heparan sulfate disaccharide repeats. Other human forms of this enzyme (e.g. the product of the EXTL1 gene) have only the 4-α-N-acetylglucosaminyltransferase activity. In Caenorhabditis elegans, the product of the rib-2 gene displays the activities of this enzyme as well as EC 2.4.1.223, glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase.
References:
1.  Kim, B.T., Kitagawa, H., Tamura, J., Saito, T., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode α1,4-N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/heparin biosynthesis. Proc. Natl. Acad. Sci. USA 98 (2001) 7176–7181. [PMID: 11390981]
2.  Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834–4838. [PMID: 11121397]
3.  Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282–286. [PMID: 11256613]
4.  Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265–26268. [PMID: 9756849]
[EC 2.4.1.224 created 2002]
 
 
EC 2.4.1.225     
Accepted name: N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan = UDP + β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan
Other name(s): N-acetylglucosaminylproteoglycan β-1,4-glucuronyltransferase; heparan glucuronyltransferase II
Systematic name: UDP-α-D-glucuronate:N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 4-β-glucuronosyltransferase
Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity required for the synthesis of the heparan sulfate disaccharide repeats.
References:
1.  Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282–286. [PMID: 11256613]
2.  Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265–26268. [PMID: 9756849]
[EC 2.4.1.225 created 2002]
 
 
EC 2.4.1.226     
Accepted name: N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase
Reaction: (1) UDP-α-D-glucuronate + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
(2) UDP-α-D-glucuronate + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
Other name(s): chondroitin glucuronyltransferase II; α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase; UDP-α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase
Systematic name: UDP-α-D-glucuronate:[protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 3-β-glucuronosyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of chondroitin and dermatan sulfate. The human chondroitin synthetase is a bifunctional glycosyltransferase, which has the 3-β-glucuronosyltransferase and 4-β-N-acetylgalactosaminyltransferase (EC 2.4.1.175) activities required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli. There is also another human protein with apparently only the 3-β-glucuronosyltransferase activity.
References:
1.  Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721–38726. [PMID: 11514575]
2.  DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124–24129. [PMID: 10818104]
3.  Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567–21575. [PMID: 11943778]
4.  Gotoh, M., Yada, T., Sato, T., Akashima, T., Iwasaki, H., Mochizuki, H., Inaba, N., Togayachi, A., Kudo, T., Watanabe, H., Kimata, K. and Narimatsu, H. Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase which transfers glucuronic acid to N-acetylgalactosamine. J. Biol. Chem. 277 (2002) 38179–38188. [PMID: 12145278]
[EC 2.4.1.226 created 2002, modified 2018]
 
 
EC 2.4.1.227     
Accepted name: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Other name(s): MurG transferase; UDP-N-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol β-1,4-N-acetylglucosaminlytransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase (configuration-inverting)
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
References:
1.  van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]
[EC 2.4.1.227 created 2002]
 
 
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
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.
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. [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. [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. [PMID: 10748143]
[EC 2.4.1.228 created 2002]
 
 
EC 2.4.1.229     
Accepted name: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-α-D-glucosaminyl)-trans-4-hydroxy-L-proline
Other name(s): Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[Skp1-protein]-trans-4-hydroxy-L-proline N-acetyl-α-D-glucosaminyl-transferase
Comments: Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity.
References:
1.  van der Wel, H., Morris, H.R., Panico, M., Paxton, T., Dell, A., Kaplan, L. and West, C.M. Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of Dictyostelium. J. Biol. Chem. 277 (2002) 46328–46337. [PMID: 12244115]
2.  Teng-umnuay, P., van der Wel, H. and West, C.M. Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium. J. Biol. Chem. 274 (1999) 36392–36402. [PMID: 10593934]
3.  West, C.M., van der Wel, H. and Gaucher, E.A. Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins. Glycobiology 12 (2002) 17. [PMID: 11886837]
[EC 2.4.1.229 created 2003, modified 2013]
 
 


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