The Enzyme Database

Displaying entries 101-150 of 1537.

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EC 2.4.1.229     Relevance: 100%
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 256531-81-4
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 11886837]
[EC 2.4.1.229 created 2003, modified 2013]
 
 
EC 2.3.1.276     Relevance: 99.8%
Accepted name: galactosamine-1-phosphate N-acetyltransferase
Reaction: acetyl-CoA + α-D-galactosamine 1-phosphate = CoA + N-acetyl-α-D-galactosamine 1-phosphate
Other name(s): ST0452 (locus name)
Systematic name: acetyl-CoA:α-D-galactosamine-1-phosphate N-acetyltransferase
Comments: The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward α-D-glucosamine 1-phosphate (cf. EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase). In addition, that enzyme contains a second domain that catalyses the activities of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase, and EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Zhang, Z., Tsujimura, M., Akutsu, J., Sasaki, M., Tajima, H. and Kawarabayasi, Y. Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7. J. Biol. Chem. 280 (2005) 9698–9705. [PMID: 15598657]
2.  Zhang, Z., Akutsu, J. and Kawarabayasi, Y. Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7. J. Bacteriol. 192 (2010) 3287–3293. [PMID: 20400541]
3.  Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091]
[EC 2.3.1.276 created 2018]
 
 
EC 3.5.99.6     Relevance: 99.5%
Accepted name: glucosamine-6-phosphate deaminase
Reaction: α-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
For diagram of UDP-N-acetylglucosamine biosynthesis, click here
Glossary: α-D-glucosamine 6-phosphate = 2-amino-2-deoxy-α-D-glucopyranose 6-phosphate
Other name(s): glucosaminephosphate isomerase (ambiguous); glucosamine-6-phosphate isomerase (ambiguous); phosphoglucosaminisomerase (ambiguous); glucosamine phosphate deaminase; aminodeoxyglucosephosphate isomerase (ambiguous); phosphoglucosamine isomerase (ambiguous); 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
Systematic name: 2-amino-2-deoxy-α-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
Comments: The enzyme uses ring opening and isomerization of the aldose-ketose type to convert the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-10-9
References:
1.  Wolfe, J.B., Britton, B.B., Nakada, H.I. Glucosamine degradation by Escherichia coli. III. Isolation and studies of "phosphoglucosaminisomerase". Arch. Biochem. Biophys. 66 (1957) 333–339. [DOI] [PMID: 13403679]
2.  Comb, D.G., Roseman, S. Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase. J. Biol. Chem. 232 (1958) 807–827. [PMID: 13549465]
3.  Pattabiraman, T.N., Bachhawat, B.K. Purification of glucosamine 6-phosphate deaminase from human brain. Biochim. Biophys. Acta 54 (1961) 273–283. [DOI] [PMID: 14484386]
4.  Liu, C., Li, D., Liang, Y.H., Li, L.F. and Su, X.D. Ring-opening mechanism revealed by crystal structures of NagB and its ES intermediate complex. J. Mol. Biol. 379 (2008) 73–81. [DOI] [PMID: 18436239]
[EC 3.5.99.6 created 1961 as EC 5.3.1.10, transferred 2000 to EC 3.5.99.6]
 
 
EC 2.4.1.182     Relevance: 99.5%
Accepted name: lipid-A-disaccharide synthase
Reaction: a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + a lipid X = UDP + a lipid A disaccharide
For diagram of lipid IVA biosynthesis, click here
Glossary: a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate =
2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine
a lipid A disaccharide = a 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
Other name(s): lpxB (gene name); UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine:2,3-bis-(3-hydroxytetradecanoyl)-β-D-glucosaminyl-1-phosphate 2,3-bis(3-hydroxytetradecanoyl)-glucosaminyltransferase (incorrect)
Systematic name: UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine:2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosaminyltransferase
Comments: Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC 2.7.1.130 (tetraacyldisaccharide 4′-kinase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-81-0
References:
1.  Ray, B.L., Painter, G. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. Formation of lipid A disaccharides from monosaccharide precursors in extracts of Escherichia coli. J. Biol. Chem. 259 (1984) 4852–4859. [PMID: 6370995]
2.  Crowell, D.N., Reznikoff, W.S. and Raetz, C.R.H. Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase. J. Bacteriol. 169 (1987) 5727–5734. [DOI] [PMID: 2824445]
3.  Metzger, L.E., 4th and Raetz, C.R. Purification and characterization of the lipid A disaccharide synthase (LpxB) from Escherichia coli, a peripheral membrane protein. Biochemistry 48 (2009) 11559–11571. [DOI] [PMID: 19883124]
4.  Bohl, T.E., Shi, K., Lee, J.K. and Aihara, H. Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. Nat. Commun. 9:377 (2018). [DOI] [PMID: 29371662]
[EC 2.4.1.182 created 1990, modified 2021]
 
 
EC 2.7.8.33     Relevance: 99.4%
Accepted name: UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate
Other name(s): UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase; UDP-GIcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase; GlcNAc-P-P-Und synthase; GPT (ambiguous); TagO; UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetylglucosaminephosphotransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-α-D-glucosaminephosphotransferase
Comments: This enzyme catalyses the synthesis of N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 [2] and of teichoic acid in certain Gram-positive bacteria [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Al-Dabbagh, B., Mengin-Lecreulx, D. and Bouhss, A. Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA. J. Bacteriol. 190 (2008) 7141–7146. [DOI] [PMID: 18723618]
2.  Lehrer, J., Vigeant, K.A., Tatar, L.D. and Valvano, M.A. Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide. J. Bacteriol. 189 (2007) 2618–2628. [DOI] [PMID: 17237164]
3.  Rush, J.S., Rick, P.D. and Waechter, C.J. Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli. Glycobiology 7 (1997) 315–322. [DOI] [PMID: 9134438]
4.  Soldo, B., Lazarevic, V. and Karamata, D. tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168. Microbiology 148 (2002) 2079–2087. [DOI] [PMID: 12101296]
[EC 2.7.8.33 created 2011]
 
 
EC 3.5.1.26     Relevance: 98.6%
Accepted name: N4-(β-N-acetylglucosaminyl)-L-asparaginase
Reaction: N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-β-D-glucosaminylamine + L-aspartate
Other name(s): aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Systematic name: N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Comments: Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free α-amino and α-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-24-5
References:
1.  Kohno, M. and Yamashina, I. Purification and properties of 4-L-aspartylglycosylamine amidohydrolase from hog kidney. Biochim. Biophys. Acta 258 (1972) 600–617. [DOI] [PMID: 5010303]
2.  Mahadevan, S. and Tappel, A.L. β-Aspartylglucosylamine amido hydrolase of rat liver and kidney. J. Biol. Chem. 242 (1967) 4568–4576. [PMID: 6061403]
3.  Tarentino, A.L. and Maley, F. The purification and properties of a β-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct. Arch. Biochem. Biophys. 130 (1969) 295–303. [PMID: 5778645]
[EC 3.5.1.26 created 1972 (EC 3.5.1.37 created 1972, incorporated 1976)]
 
 
EC 2.8.2.23     Relevance: 98.3%
Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 1
Reaction: 3′-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3′,5′-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): heparin-glucosamine 3-O-sulfotransferase; 3′-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase; glucosaminyl 3-O-sulfotransferase; heparan sulfate D-glucosaminyl 3-O-sulfotransferase; isoform/isozyme 1 (3-OST-1, HS3ST1); 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
Comments: This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases [EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2) and EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3)] by being the most selective for a precursor of the antithrombin-binding site. It has a minimal acceptor sequence of: → GlcNAc6S→ GlcA→ GlcN2S*+/-6S→ IdoA2S→ GlcN2S→ , the asterisk marking the target (symbols as in 2-Carb-38) using +/- to mean the presence or absence of a substituent, and > to separate a predominant structure from a minor one. Thus Glc(N2S > NAc) means a residue of glucosamine where the N carries a sulfo group mainly but occasionally an acetyl group. [1-4]. It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites. These precursors are variants of the consensus sequence: → Glc(N2S > NAc)+/-6S→ GlcA→ GlcN2S*+/-6S→ GlcA > IdoA+/-2S→ Glc(N2S/NAc)+/-6S→ [5]. If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 183257-54-7
References:
1.  Kusche, M., Backström, G., Riesenfeld, J., Pepitou, M., Choay, J. and Lindahl, U. Biosynthesis of heparin. O-Sulfation of the antithrombin-binding region. J. Biol. Chem. 263 (1988) 15474–15484. [PMID: 3139669]
2.  Shworak, N.W., Fritze, L.M.S., Liu, J., Butler, L.D. and Rosenberg, R.D. Cell-free synthesis of anticoagulant heparan sulfate reveals a limiting activity which modifies a nonlimiting precursor pool. J. Biol. Chem. 271 (1996) 27063–27071. [DOI] [PMID: 8900197]
3.  Liu, J., Shworak, N.W., Fritze, L.M.S., Edelberg, J.M. and Rosenberg, R.D. Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 271 (1996) 27072–27082. [DOI] [PMID: 8900198]
4.  Shworak, N.W., Liu, J., Fritze, L.M.S., Schwartz, J.J., Zhang, L., Logeart, D. and Rosenberg, R.D. Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 272 (1997) 28008–28019. [DOI] [PMID: 9346953]
5.  Zhang, L., Yoshida, K., Liu, J. and Rosenberg, R.D. Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells. J. Biol. Chem. 274 (1999) 5681–5691. [DOI] [PMID: 10026187]
6.  Zhang, L., Lawrence, R., Schwartz, J.J., Bai, X. , Wei., G, Esko, J.D. and Rosenberg, R.D. The effect of precursor structures on the action of glucosaminyl 3-O-sulfotransferase-1 and the biosynthesis of anticoagulant heparan sulfate. J. Biol. Chem. 276 (2001) 28806–28813. [DOI] [PMID: 11375390]
[EC 2.8.2.23 created 1992, modified 2001]
 
 
EC 2.4.99.7      
Transferred entry: α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase. Now EC 2.4.3.7, α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase
[EC 2.4.99.7 created 1984, modified 1986, modified 2004, deleted 2022]
 
 
EC 2.4.1.313     Relevance: 96.8%
Accepted name: protein O-mannose β-1,3-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]
For diagram of glycoprotein biosynthesis, click here
Other name(s): B3GALNT2
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl-threonyl-[protein] 3-β-N-acetyl-D-galactosaminyltransferase
Comments: The human protein is specific for UDP-N-acetyl-α-D-galactosamine as donor [1]. The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hiruma, T., Togayachi, A., Okamura, K., Sato, T., Kikuchi, N., Kwon, Y.D., Nakamura, A., Fujimura, K., Gotoh, M., Tachibana, K., Ishizuka, Y., Noce, T., Nakanishi, H. and Narimatsu, H. A novel human β1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcβ1-3GlcNAc. J. Biol. Chem. 279 (2004) 14087–14095. [DOI] [PMID: 14724282]
2.  Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]
[EC 2.4.1.313 created 2013]
 
 
EC 2.3.1.202     Relevance: 96.6%
Accepted name: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase
Reaction: acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine = CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose
Other name(s): PseH
Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase
Comments: Isolated from Helicobacter pylori. The enzyme is involved in the biosynthesis of pseudaminic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schoenhofen, I.C., McNally, D.J., Brisson, J.R. and Logan, S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16 (2006) 8C–14C. [DOI] [PMID: 16751642]
[EC 2.3.1.202 created 2012]
 
 
EC 3.6.1.54     Relevance: 96.6%
Accepted name: UDP-2,3-diacylglucosamine diphosphatase
Reaction: a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + H2O = a lipid X + UMP
For diagram of lipid IVA biosynthesis, click here
Glossary: a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate =
2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine
Other name(s): lpxH (gene name); UDP-2,3-diacylglucosamine hydrolase; UDP-2,3-diacylglucosamine pyrophosphatase; ybbF (gene name); UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-α-D-glucosamine 2,3-bis[(3R)-3-hydroxymyristoyl]-β-D-glucosaminyl 1-phosphate phosphohydrolase (incorrect); UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosaminyl 1-phosphate phosphohydrolase
Systematic name: UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine-1-phosphate phosphohydrolase
Comments: The enzyme catalyses a step in the biosynthesis of lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Babinski, K.J., Ribeiro, A.A. and Raetz, C.R. The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis. J. Biol. Chem. 277 (2002) 25937–25946. [DOI] [PMID: 12000770]
2.  Babinski, K.J., Kanjilal, S.J. and Raetz, C.R. Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene. J. Biol. Chem. 277 (2002) 25947–25956. [DOI] [PMID: 12000771]
3.  Okada, C., Wakabayashi, H., Kobayashi, M., Shinoda, A., Tanaka, I. and Yao, M. Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa. Sci. Rep. 6:32822 (2016). [DOI] [PMID: 27609419]
4.  Cho, J., Lee, C.J., Zhao, J., Young, H.E. and Zhou, P. Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol 1:16154 (2016). [DOI] [PMID: 27780190]
5.  Arenas, J., Pupo, E., de Jonge, E., Perez-Ortega, J., Schaarschmidt, J., van der Ley, P. and Tommassen, J. Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A. J. Biol. Chem. 294 (2019) 7982–7989. [DOI] [PMID: 30926608]
[EC 3.6.1.54 created 2010, modified 2021]
 
 
EC 4.2.1.115     Relevance: 96.4%
Accepted name: UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)
Reaction: UDP-N-acetyl-α-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose + H2O
For diagram of UDP-N-acetyl-β-L-fucosamine biosynthesis, click here and for diagram of mechanism, click here
Glossary: pseudaminic acid = 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid
Other name(s): FlaA1; UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase; PseB; UDP-N-acetylglucosamine hydro-lyase (inverting; UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose-forming)
Systematic name: UDP-N-acetyl-α-D-glucosamine hydro-lyase (inverting; UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose-forming)
Comments: Contains NADP+ as a cofactor. This is the first enzyme in the biosynthetic pathway of pseudaminic acid [3], a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. This enzyme plays a critical role in H. pylori’s pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is completely inhibited by UDP-α-D-galactose. The reaction results in the chirality of the C-5 atom being inverted. It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ishiyama, N., Creuzenet, C., Miller, W.L., Demendi, M., Anderson, E.M., Harauz, G., Lam, J.S. and Berghuis, A.M. Structural studies of FlaA1 from Helicobacter pylori reveal the mechanism for inverting 4,6-dehydratase activity. J. Biol. Chem. 281 (2006) 24489–24495. [DOI] [PMID: 16651261]
2.  Schirm, M., Soo, E.C., Aubry, A.J., Austin, J., Thibault, P. and Logan, S.M. Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol. Microbiol. 48 (2003) 1579–1592. [DOI] [PMID: 12791140]
3.  Schoenhofen, I.C., McNally, D.J., Brisson, J.R. and Logan, S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16 (2006) 8C–14C. [DOI] [PMID: 16751642]
[EC 4.2.1.115 created 2009]
 
 
EC 2.4.1.88     Relevance: 96.3%
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 2.4.1.68     Relevance: 96.2%
Accepted name: glycoprotein 6-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] = GDP + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-[α-L-Fuc-(1→6)]-β-D-GlcNAc}-L-asparaginyl-[protein]
For diagram of mannosyl-glycoprotein fucosyl and xylosyl transferases, click here
Other name(s): GDP-fucose—glycoprotein fucosyltransferase; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase; GDP-L-fucose-glycoprotein fucosyltransferase; glycoprotein fucosyltransferase; guanosine diphosphofucose-glycoprotein fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of 4-N-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 6-α-L-fucosyltransferase; FucT; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 6-α-L-fucosyltransferase; GDP-β-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 6-α-L-fucosyltransferase
Systematic name: GDP-β-L-fucose:N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] 6-α-L-fucosyltransferase (configuration-inverting)
Comments: This enzyme catalyses a reaction similar to that of EC 2.4.1.214, glycoprotein 3-α-L-fucosyltransferase, but transfers the L-fucosyl group from GDP-β-L-fucose to form an α1,6-linkage rather than an α1,3-linkage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-08-3
References:
1.  Longmore, G.D. and Schachter, H. Product-identification and substrate-specificity studies of the GDP-L-fucose:2-acetamido-2-deoxy-β-D-glucoside (Fuc → Asn-linked GlcNAc) 6-α-L-fucosyltransferase in a Golgi-rich fraction from porcine liver. Carbohydr. Res. 100 (1982) 365–392. [DOI] [PMID: 7083256]
2.  Voynow, J.A., Scanlin, T.F. and Glick, M.C. A quantitative method for GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase activity with lectin affinity chromatography. Anal. Biochem. 168 (1988) 367–373. [DOI] [PMID: 3364733]
3.  Uozumi, N., Yanagidani, S., Miyoshi, E., Ihara, Y., Sakuma, T., Gao, C.-X., Teshima, T., Fujii, S., Shiba, T. and Taniguchi, N. Purification and cDNA cloning of porcine brain GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase. J. Biol. Chem. 271 (1996) 27810–27817. [DOI] [PMID: 8910378]
[EC 2.4.1.68 created 1972, modified 2002]
 
 
EC 2.4.2.38     Relevance: 96.1%
Accepted name: glycoprotein 2-β-D-xylosyltransferase
Reaction: UDP-α-D-xylose + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] = UDP + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-[β-D-Xyl-(1→2)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein]
For diagram of mannosyl-glycoprotein fucosyl and xylosyl transferases, click here
Other name(s): β1,2-xylosyltransferase; UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of 4-N-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase; UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase
Systematic name: UDP-α-D-xylose:N4-{β-D-GlcNAc-(1→2)-α-D-mannosyl-(1→3)-[β-D-GlcNAc-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] 2-β-D-xylosyltransferase (configuration-inverting)
Comments: Specific for N-linked oligosaccharides (N-glycans).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 141256-56-6
References:
1.  Zeng, Y., Bannon, G., Thomas, V.H., Rice, K., Drake, R. and Elbein, A. Purification and specificity of β1,2-xylosyltransferase, an enzyme that contributes to the allergenicity of some plant proteins. J. Biol. Chem. 272 (1997) 31340–31347. [DOI] [PMID: 9395463]
2.  Strasser, R., Mucha, J., Mach, L., Altmann, F., Wilson, I.B., Glössl, J. and Steinkellner, H. Molecular cloning and functional expression of β1,2-xylosyltransferase cDNA from Arabidopsis thaliana. FEBS Lett. 472 (2000) 105–108. [DOI] [PMID: 10781814]
[EC 2.4.2.38 created 2001]
 
 
EC 3.1.6.14     Relevance: 95.9%
Accepted name: N-acetylglucosamine-6-sulfatase
Reaction: Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate
Other name(s): chondroitinsulfatase; O,N-disulfate O-sulfohydrolase; acetylglucosamine 6-sulfatase; N-acetylglucosamine 6-sulfate sulfatase; acetylglucosamine 6-sulfatase; 2-acetamido-2-deoxy-D-glucose 6-sulfate sulfatase
Systematic name: N-acetyl-D-glucosamine-6-sulfate 6-sulfohydrolase
Comments: May be identical with EC 3.1.6.11 disulfoglucosamine-6-sulfatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65666-34-4
References:
1.  Basner, R., Kresse, H. and von Figura, K. N-Acetylglucosamine-6-sulfate sulfatase from human urine. J. Biol. Chem. 254 (1979) 1151–1158. [PMID: 762121]
2.  Kresse, H., Fuchs, W., Glössl, J., Holtfrerich, D. and Gilberg, W. Liberation of N-acetylglucosamine-6-sulfate by human β-N-acetylhexosaminidase A. J. Biol. Chem. 256 (1981) 12926–12932. [PMID: 6458607]
3.  Weissmann, B., Chao, H. and Chow, P. A glucosamine O,N-disulfate O-sulfohydrolase with a probable role in mammalian catabolism of heparan sulfate. Biochem. Biophys. Res. Commun. 97 (1980) 827–833. [DOI] [PMID: 6451222]
[EC 3.1.6.14 created 1984]
 
 
EC 2.4.3.7     Relevance: 95.9%
Accepted name: α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase
Reaction: CMP-N-acetylneuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-D-galactosaminyl-R
For diagram of reaction, click here
Other name(s): sialyltransferase; cytidine monophosphoacetylneuraminate-(α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetylgalactosaminide-α-2,6-sialyltransferase; α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetyl-galactosaminide α-2,6-sialyltransferase; SIAT7; ST6GALNAC; (α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetyl-galactosaminide 6-α-sialyltransferase; CMP-N-acetylneuraminate:(α-N-acetylneuraminyl-2,3-β-D-galactosyl-1,3)-N-acetyl-D-galactosaminide α-2,6-N-acetylneuraminyl-transferase
Systematic name: CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)- N-acetyl-D-galactosaminide galactosamine-6-α-N-acetylneuraminyltransferase
Comments: Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetylgalactosamine only when present in the structure of α-N-acetylneuraminyl-(2→3)-β-galactosyl-(1→3)-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.3.3 α-N-acetylgalactosaminide α-2,6-sialyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129924-24-9
References:
1.  Bergh, M.L.E., Hooghwinkel, G.J.M. and Van den Eijnden, D.H. Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin. Indications for an α-N-acetylgalactosaminide α2→6 sialyltransferase with a narrow acceptor specificity in fetal calf liver. J. Biol. Chem. 258 (1983) 7430–7436. [PMID: 6190802]
[EC 2.4.3.7 created 1984 as EC 2.4.99.7, modified 1986, modified 2004, transferred 2022 to EC 2.4.3.7]
 
 
EC 2.4.1.142     Relevance: 95.7%
Accepted name: chitobiosyldiphosphodolichol β-mannosyltransferase
Reaction: GDP-α-D-mannose + N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = GDP + β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Glossary: N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = N,N′-diacetylchitobiosyl-diphosphodolichol
Other name(s): guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose:chitobiosyldiphosphodolichol β-D-mannosyltransferase
Systematic name: GDP-α-D-mannose:N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol 4-β-D-mannosyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83380-85-2
References:
1.  Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [DOI] [PMID: 6215245]
2.  Takahashi, T., Honda, R. and Nishikawa, Y. Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1. Glycobiology 10 (2000) 321–327. [DOI] [PMID: 10704531]
[EC 2.4.1.142 created 1984, modified 2001]
 
 
EC 2.4.1.378     Relevance: 95.2%
Accepted name: GDP-mannose:α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,4-mannosyltransferase
Reaction: GDP-α-D-mannose + α-L-Rha-(1→3)-α-D-Gal-PP-Und = GDP + α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaU (gene name); rfbU (gene name)
Systematic name: GDP-α-D-mannose:α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 4II-α-rhamnosyltransferase (configuration-retaining)
Comments: The enzyme from Salmonella participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B, and D1 groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408–3413. [DOI] [PMID: 7684736]
[EC 2.4.1.378 created 2021]
 
 
EC 2.3.1.129     Relevance: 95.1%
Accepted name: acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-N-acetyl-α-D-glucosamine = an [acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine
For diagram of lipid IVA biosynthesis, click here
Other name(s): lpxA (gene name); UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-N-acetyl-α-D-glucosamine 3-O-(3-hydroxyacyl)transferase
Comments: Involved with EC 2.4.1.182, lipid-A-disaccharide synthase, and EC 2.7.1.130, tetraacyldisaccharide 4′-kinase, in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-69-4
References:
1.  Anderson, M.S., Bulawa, C.E. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. Formation of lipid A precursors from UDP-GlcNAc in extracts of Escherichia coli. J. Biol. Chem. 260 (1985) 15536–15541. [PMID: 3905795]
2.  Anderson, M.S., Bull, H.G., Galloway, S.M., Kelly, T.M., Mohan, S., Radika, K. and Raetz, C.R. UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable. J. Biol. Chem. 268 (1993) 19858–19865. [PMID: 8366124]
3.  Raetz, C.R. and Roderick, S.L. A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270 (1995) 997–1000. [DOI] [PMID: 7481807]
4.  Williams, A.H. and Raetz, C.R. Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase. Proc. Natl. Acad. Sci. USA 104 (2007) 13543–13550. [DOI] [PMID: 17698807]
5.  Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J. Bacteriol. 190 (2008) 4549–4558. [DOI] [PMID: 18456814]
[EC 2.3.1.129 created 1990, modified 2021]
 
 
EC 2.4.1.165     Relevance: 95%
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 1.1.1.426     Relevance: 95%
Accepted name: UDP-N-acetyl-α-D-quinovosamine dehydrogenase
Reaction: UDP-N-acetyl-α-D-quinovosamine + NAD(P)+ = UDP-2-acetamido-2,6-dideoxy-α-D-xylohex-4-ulose + NAD(P)H + H+
Glossary: UDP-N-acetyl-α-D-quinovosamine = UDP-N-acetyl-6-deoxy-α-D-glucosamine
Other name(s): wbpV (gene name); wreQ (gene name)
Systematic name: UDP-N-acetyl-α-D-quinovosamine:NAD(P)+ 4-dehydrogenase
Comments: The enzyme participates in the biosynthesis of N-acetyl-α-D-quinovosamine, a 6-deoxy sugar that is present in the O antigens of many Gram-negative bacteria, including Pseudomonas aeruginosa serotypes O6 and O10, Rhizobium etli, and Brucella abortus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Belanger, M., Burrows, L.L. and Lam, J.S. Functional analysis of genes responsible for the synthesis of the B-band O antigen of Pseudomonas aeruginosa serotype O6 lipopolysaccharide. Microbiology (Reading) 145 (1999) 3505–3521. [DOI] [PMID: 10627048]
2.  Forsberg, L.S., Noel, K.D., Box, J. and Carlson, R.W. Genetic locus and structural characterization of the biochemical defect in the O-antigenic polysaccharide of the symbiotically deficient Rhizobium etli mutant, CE166. Replacement of N-acetylquinovosamine with its hexosyl-4-ulose precursor. J. Biol. Chem. 278 (2003) 51347–51359. [DOI] [PMID: 14551189]
3.  Li, T., Simonds, L., Kovrigin, E.L. and Noel, K.D. In vitro biosynthesis and chemical identification of UDP-N-acetyl-D-quinovosamine (UDP-D-QuiNAc). J. Biol. Chem. 289 (2014) 18110–18120. [DOI] [PMID: 24817117]
[EC 1.1.1.426 created 2021]
 
 
EC 3.2.1.81     Relevance: 94.9%
Accepted name: β-agarase
Reaction: Hydrolysis of (1→4)-β-D-galactosidic linkages in agarose, giving the tetramer as the predominant product
Glossary: agarose = a linear polysaccharide produced by some members of the Rhodophyta (red algae) made up from alternating D-galactose and 3,6-anhydro-α-L-galactopyranose residues joined by α-(1→3)- and β-(1→4)-linkages. In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not.
For example:
neoagarobiose = 3,6-anhydro-α-L-galactopyranosyl-(1→3)-D-galactose
agarobiose = β-D-galactopyranosyl-(1→4)-3,6-anhydro-L-galactose
Other name(s): agarase (ambiguous); AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase (incorrect)
Systematic name: agarose 4-glycanohydrolase
Comments: Also acts on porphyran, but more slowly [1]. This enzyme cleaves the β-(1→4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing β-anomers that give rise progressively to α-anomers when mutarotation takes place [6]. The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-57-6
References:
1.  Duckworth, M. and Turvey, J.R. The action of a bacterial agarase on agarose, porphyran and alkali-treated porphyran. Biochem. J. 113 (1969) 687–692. [PMID: 5386190]
2.  Allouch, J., Jam, M., Helbert, W., Barbeyron, T., Kloareg, B., Henrissat, B. and Czjzek, M. The three-dimensional structures of two β-agarases. J. Biol. Chem. 278 (2003) 47171–47180. [DOI] [PMID: 12970344]
3.  Ohta, Y., Nogi, Y., Miyazaki, M., Li, Z., Hatada, Y., Ito, S. and Horikoshi, K. Enzymatic properties and nucleotide and amino acid sequences of a thermostable β-agarase from the novel marine isolate, JAMB-A94. Biosci. Biotechnol. Biochem. 68 (2004) 1073–1081. [DOI] [PMID: 15170112]
4.  Ohta, Y., Hatada, Y., Nogi, Y., Miyazaki, M., Li, Z., Akita, M., Hidaka, Y., Goda, S., Ito, S. and Horikoshi, K. Enzymatic properties and nucleotide and amino acid sequences of a thermostable β-agarase from a novel species of deep-sea Microbulbifer. Appl. Microbiol. Biotechnol. 64 (2004) 505–514. [DOI] [PMID: 15088129]
5.  Sugano, Y., Terada, I., Arita, M., Noma, M. and Matsumoto, T. Purification and characterization of a new agarase from a marine bacterium, Vibrio sp. strain JT0107. Appl. Environ. Microbiol. 59 (1993) 1549–1554. [PMID: 8517750]
6.  Jam, M., Flament, D., Allouch, J., Potin, P., Thion, L., Kloareg, B., Czjzek, M., Helbert, W., Michel, G. and Barbeyron, T. The endo-β-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours. Biochem. J. 385 (2005) 703–713. [DOI] [PMID: 15456406]
[EC 3.2.1.81 created 1972, modified 2006]
 
 
EC 2.4.1.275     Relevance: 94.9%
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 2.6.1.122     Relevance: 94.6%
Accepted name: UDP-N-acetyl-3-dehydro-α-D-glucosamine 3-aminotranferase
Reaction: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose + 2-oxoglutarate = UDP-N-acetyl-3-dehydro-α-D-glucosamine + L-glutamate
Other name(s): gnnB (gene name)
Systematic name: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucopyranose:2-oxoglutarate aminotransferase
Comments: This bacterial enzyme participates, together with EC 1.1.1.374, UDP-N-acetylglucosamine 3-dehydrogenase, in the synthesis of 2,3-diamino-2,3-dideoxy-D-glucopyranose, a component of lipid A in some species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sweet, C.R., Ribeiro, A.A. and Raetz, C.R. Oxidation and transamination of the 3"-position of UDP-N-acetylglucosamine by enzymes from Acidithiobacillus ferrooxidans. Role in the formation of lipid a molecules with four amide-linked acyl chains. J. Biol. Chem. 279 (2004) 25400–25410. [DOI] [PMID: 15044494]
[EC 2.6.1.122 created 2021]
 
 
EC 2.4.1.60     Relevance: 94.5%
Accepted name: CDP-abequose:α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase
Reaction: CDP-α-D-abequose + α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = CDP + α-D-Abe-(1→3)-α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und
Glossary: D-abequose = 3,6-deoxy-D-xylo-hexose = 3,6-deoxy-D-galactose = 3-deoxy-D-fucose
α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Abe-(1→3)-α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-D-abequopyranosyl-(1→3)-α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaV (gene name); rfbV (gene name); trihexose diphospholipid abequosyltransferase; abequosyltransferase (ambiguous); CDP-α-D-abequose:Man(α1→4)Rha(α1→3)Gal(β-1)-diphospholipid D-abequosyltransferase
Systematic name: CDP-α-D-abequose:α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 3III-α-abequosyltransferase (configuration retaining)
Comments: The enzyme from Salmonella participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B and D1-D3 groups. The enzyme is able to transfer abequose, paratose, or tyvelose, depending on the availability of the specific dideoxyhexose in a particular strain.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-67-1
References:
1.  Osborn, M.J. and Weiner, I.M. Biosynthesis of a bacterial lipopolysaccharide. VI. Mechanism of incorporation of abequose into the O-antigen of Salmonella typhimurium. J. Biol. Chem. 243 (1968) 2631–2639. [PMID: 4297268]
2.  Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084–4088. [DOI] [PMID: 7541787]
[EC 2.4.1.60 created 1972, modified 2012, modified 2021]
 
 
EC 2.4.1.152     Relevance: 94.3%
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 3.2.1.157     Relevance: 94.3%
Accepted name: ι-carrageenase
Reaction: Endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in ι-carrageenans
For diagram of reaction, click here
Glossary: In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not.
For example:
ι-neocarrabiose = 3,6-anhydro-2-O-sulfo-α-D-galactopyranosyl-(1→3)-4-O-sulfo-D-galactose
ι-carrabiose = 4-O-sulfo-β-D-galactopyranosyl-(1→4)-3,6-anhydro-2-O-sulfo-D-galactose
Systematic name: ι-carrageenan 4-β-D-glycanohydrolase (configuration-inverting)
Comments: The main products of hydrolysis are ι-neocarratetraose sulfate and ι-neocarrahexaose sulfate. ι-Neocarraoctaose is the shortest substrate oligomer that can be cleaved. Unlike EC 3.2.1.81, β-agarase and EC 3.2.1.83, κ-carrageenase, this enzyme proceeds with inversion of the anomeric configuration. ι-Carrageenan differs from κ-carrageenan by possessing a sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in addition to that present in the κ-compound on O-4 of the D-galactose residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50936-37-3
References:
1.  Barbeyron, T., Michel, G., Potin, P., Henrissat, B. and Kloareg, B. ι-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of κ-carrageenases. J. Biol. Chem. 275 (2000) 35499–35505. [DOI] [PMID: 10934194]
2.  Michel, G., Chantalat, L., Fanchon, E., Henrissat, B., Kloareg, B. and Dideberg, O. The ι-carrageenase of Alteromonas fortis. A β-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide. J. Biol. Chem. 276 (2001) 40202–40209. [DOI] [PMID: 11493601]
3.  Michel, G., Helbert, W., Kahn, R., Dideberg, O. and Kloareg, B. The structural bases of the processive degradation of ι-carrageenan, a main cell wall polysaccharide of red algae. J. Mol. Biol. 334 (2003) 421–433. [DOI] [PMID: 14623184]
[EC 3.2.1.157 created 2006]
 
 
EC 2.4.1.174     Relevance: 94.2%
Accepted name: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + [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-(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
For diagram of chondroitin biosynthesis (later stages), click here
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): N-acetylgalactosaminyltransferase I; glucuronylgalactosylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I; UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-β-D-galactosyl-proteoglycan β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1→3)-β-D-galactosyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting)
Comments: Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96189-39-8
References:
1.  Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754]
2.  Uyama, T., Kitagawa, H., Tamura, J.-i. and Sugahara, K. Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: the key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate. J. Biol. Chem. 277 (2002) 8841–8846. [DOI] [PMID: 11788602]
[EC 2.4.1.174 created 1989, modified 2002]
 
 
EC 2.4.1.39     Relevance: 94.1%
Accepted name: steroid N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + estradiol-17α 3-D-glucuronoside = UDP + 17α-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside
Other name(s): hydroxy steroid acetylglucosaminyltransferase; steroid acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-steroid acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:estradiol-17α-3-D-glucuronoside 17α-N-acetylglucosaminyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-56-1
References:
1.  Collins, D.C., Jirku, H. and Layne, D.S. Steroid N-acetylglucosaminyl transferase. Localization and some properties of the enzyme in rabbit tissues. J. Biol. Chem. 243 (1968) 2928–2933. [PMID: 5660254]
[EC 2.4.1.39 created 1972]
 
 
EC 3.2.1.36     Relevance: 93.7%
Accepted name: hyaluronoglucuronidase
Reaction: Random hydrolysis of (1→3)-linkages between β-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate
Other name(s): hyaluronidase; glucuronoglucosaminoglycan hyaluronate lyase; orgelase
Systematic name: hyaluronate 3-glycanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-34-9
References:
1.  Linker, A., Meyer, K. and Hoffman, P. The production of hyaluronate oligosaccharides by leech hyaluronidase and alkali. J. Biol. Chem. 235 (1960) 924–927. [PMID: 14417285]
2.  Meyer, K., Hoffman, P. and Linker, A. Hyaluronidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 447–460.
[EC 3.2.1.36 created 1965, modified 1980]
 
 
EC 4.2.2.1     Relevance: 93.4%
Accepted name: hyaluronate lyase
Reaction: Cleaves hyaluronate chains at a β-D-GlcNAc-(1→4)-β-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.
Other name(s): hyaluronidase (ambiguous); glucuronoglycosaminoglycan lyase (ambiguous); spreading factor; mucinase (ambiguous)
Systematic name: hyaluronate lyase
Comments: The enzyme catalyses the degradation of hyaluronan by a β-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37259-53-3
References:
1.  Linker, A., Hoffman, P., Meyer, K., Sampson, P. and Korn, E.D. The formation of unsaturated disacharides from mucopoly-saccharides and their cleavage to α-keto acid by bacterial enzymes. J. Biol. Chem. 235 (1960) 3061. [PMID: 13762462]
2.  Meyer, K. and Rapport, M.M. Hyaluronidases. Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 199–236. [PMID: 14943668]
3.  Moran, F., Nasuno, S. and Starr, M.P. Extracellular and intracellular polygalacturonic acid trans-eliminases of Erwinia carotovora. Arch. Biochem. Biophys. 123 (1968) 298–306. [DOI] [PMID: 5642600]
[EC 4.2.2.1 created 1961 as EC 4.2.99.1, transferred 1972 to EC 4.2.2.1, modified 2001]
 
 
EC 2.4.1.214     Relevance: 93.4%
Accepted name: glycoprotein 3-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] = GDP + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-[α-L-Fuc-(1→3)]-β-D-GlcNAc}-L-asparaginyl-[protein]
For diagram of mannosyl-glycoprotein fucosyl and xylosyl transferases, click here
Other name(s): GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1,3-fucosyltransferase; GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase; GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1→6GlcNAc)-Asn-peptide) α1→3-fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of 4-N-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 3-α-L-fucosyl-transferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 3-α-L-fucosyl-transferase; GDP-β-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 3-α-L-fucosyl-transferase
Systematic name: GDP-β-L-fucose:N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] 3-α-L-fucosyltransferase (configuration-retaining)
Comments: Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-α-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-β-L-fucose to form an α1,3-linkage rather than an α1,6-linkage. The N-glycan products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 68247-53-0
References:
1.  Wilson, I.B.H., Rendic, D., Freilinger, A., Dumic, J., Altmann, F., Mucha, J., Müller, S. and Hauser, M.-T. Cloning and expression of α1,3-fucosyltransferase homologues from Arabidopsis thaliana. Biochim. Biophys. Acta 1527 (2001) 88–96. [DOI] [PMID: 11420147]
2.  Fabini, G., Freilinger, A., Altmann, F. and Wilson, I.B.H. Identification of core α1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope. J. Biol. Chem. 276 (2001) 28058–28067. [DOI] [PMID: 11382750]
3.  Leiter, H., Mucha, J., Staudacher, E., Grimm, R., Glössl, J. and Altmann, F. Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase from mung beans. J. Biol. Chem. 274 (1999) 21830–21839. [DOI] [PMID: 10419500]
4.  van Tetering, A., Schiphorst, W.E.C.M., van den Eijnden, D.H. and van Die, I. Characterization of core α1→3-fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex type N-glycans. FEBS Lett. 461 (1999) 311–314. [DOI] [PMID: 10567717]
5.  Staudacher, E., Altmann, F., Glössl, J., März, L., Schachter, H., Kamerling, J.P., Haard, K. and Vliegenthart, J.F.G. GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1→6GlcNAc)-Asn-peptide) α1→3-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine. Eur. J. Biochem. 199 (1991) 745–751. [DOI] [PMID: 1868856]
[EC 2.4.1.214 created 2001]
 
 
EC 2.4.1.79     Relevance: 93.3%
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 1.1.1.136     Relevance: 93.1%
Accepted name: UDP-N-acetylglucosamine 6-dehydrogenase
Reaction: UDP-N-acetyl-α-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-α-D-glucuronate + 2 NADH + 2 H+
For diagram of UDP-N-acetylgalactosamine and UDP-N-acetylmannosamine biosynthesis, click here
Other name(s): uridine diphosphoacetylglucosamine dehydrogenase; UDP-acetylglucosamine dehydrogenase; UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase; UDP-GlcNAc dehydrogenase; WbpA; WbpO
Systematic name: UDP-N-acetyl-α-D-glucosamine:NAD+ 6-oxidoreductase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-83-5
References:
1.  Fan, D.-F., John, C.E., Zalitis, J. and Feingold, D.S. UDPacetylglucosamine dehydrogenase from Achromobacter georgiopolitanum. Arch. Biochem. Biophys. 135 (1969) 45–49. [DOI] [PMID: 4312076]
2.  Miller, W.L., Wenzel, C.Q., Daniels, C., Larocque, S., Brisson, J.R. and Lam, J.S. Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 279 (2004) 37551–37558. [DOI] [PMID: 15226302]
[EC 1.1.1.136 created 1972, modified 2012]
 
 
EC 5.1.3.28     Relevance: 93%
Accepted name: UDP-N-acetyl-L-fucosamine synthase
Reaction: UDP-2-acetamido-2,6-dideoxy-β-L-talose = UDP-N-acetyl-β-L-fucosamine
For diagram of UDP-N-acetyl-β-L-fucosamine biosynthesis, click here
Glossary: UDP-2-acetamido-2,6-dideoxy-β-L-talose = UDP-N-acetyl-β-L-pneumosamine
Other name(s): WbjD; Cap5G
Systematic name: UDP-2-acetamido-2,6-dideoxy-β-L-talose 2-epimerase
Comments: Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus. Involved in bacterial polysaccharide biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kneidinger, B., O'Riordan, K., Li, J., Brisson, J.R., Lee, J.C. and Lam, J.S. Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas aeruginosa O11 and capsule in Staphylococcus aureus type 5. Implications for the UDP-N-acetyl-L-fucosamine biosynthetic pathway. J. Biol. Chem. 278 (2003) 3615–3627. [DOI] [PMID: 12464616]
2.  Mulrooney, E.F., Poon, K.K., McNally, D.J., Brisson, J.R. and Lam, J.S. Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis of lipopolysaccharide in Pseudomonas aeruginosa serotype O11. J. Biol. Chem. 280 (2005) 19535–19542. [DOI] [PMID: 15778500]
[EC 5.1.3.28 created 2014]
 
 
EC 2.4.1.380     Relevance: 92.4%
Accepted name: GDP-Man:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-mannosyltransferase
Reaction: GDP-α-D-mannose + α-D-Man-(1→3)-α-D-Gal-PP-Und = GDP + α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und
Glossary: α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaW (gene name); rfbW (gene name)
Systematic name: GDP-α-D-mannose:α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 2II-α-mannosyltransferase (configuration-retaining)
Comments: The enzyme, present in Salmonella strains that belong to group C2, participates in the biosynthesis of the repeat unit of O antigens produced by these strains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brown, P.K., Romana, L.K. and Reeves, P.R. Cloning of the rfb gene cluster of a group C2 Salmonella strain: comparison with the rfb regions of groups B and D. Mol. Microbiol. 5 (1991) 1873–1881. [DOI] [PMID: 1722557]
2.  Brown, P.K., Romana, L.K. and Reeves, P.R. Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen (strain M67): the genetic basis of the polymorphism between groups C2 and B. Mol. Microbiol. 6 (1992) 1385–1394. [DOI] [PMID: 1379320]
3.  Liu, D., Haase, A.M., Lindqvist, L., Lindberg, A.A. and Reeves, P.R. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175 (1993) 3408–3413. [DOI] [PMID: 7684736]
4.  Zhao, X., Dai, Q., Jia, R., Zhu, D., Liu, M., Wang, M., Chen, S., Sun, K., Yang, Q., Wu, Y. and Cheng, A. two novel Salmonella bivalent vaccines confer dual protection against two Salmonella serovars in mice. Front Cell Infect Microbiol 7:391 (2017). [DOI] [PMID: 28929089]
[EC 2.4.1.380 created 2021]
 
 
EC 2.7.7.83     Relevance: 91.3%
Accepted name: UDP-N-acetylgalactosamine diphosphorylase
Reaction: UTP + N-acetyl-α-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-α-D-galactosamine
Systematic name: UTP:N-acetyl-α-D-galactosamine-1-phosphate uridylyltransferase
Comments: The enzyme from plants and animals also has activity toward N-acetyl-α-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Wang-Gillam, A., Pastuszak, I. and Elbein, A.D. A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J. Biol. Chem. 273 (1998) 27055–27057. [DOI] [PMID: 9765219]
2.  Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F. and Bourne, Y. Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 20 (2001) 6191–6202. [DOI] [PMID: 11707391]
[EC 2.7.7.83 created 2012]
 
 
EC 3.5.1.21     Relevance: 91.1%
Accepted name: N-acetyl-β-alanine deacetylase
Reaction: N-acetyl-β-alanine + H2O = acetate + β-alanine
Systematic name: N-acetyl-β-alanine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-04-6
References:
1.  Fujimoto, D., Koyama, T. and Tamiya, N. N-Acetyl-β-alanine deacetylase in hog kidney. Biochim. Biophys. Acta 167 (1968) 407–413.
[EC 3.5.1.21 created 1972]
 
 
EC 2.6.1.34     Relevance: 91%
Accepted name: UDP-N-acetylbacillosamine transaminase
Reaction: UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose + L-glutamate
For diagram of legionaminic acid biosynthesis, click here
Glossary: UDP-N-acetylbacillosamine = UDP-2-acetamido-4-amino-2,4,6-trideoxy-α-D-glucose = UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine
Other name(s): uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase; UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase; UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase; pglE (gene name); UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase
Systematic name: UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N′-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-89-7
References:
1.  Distler, J., Kaufman, B. and Roseman, S. Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae. Arch. Biochem. Biophys. 116 (1966) 466–478. [DOI] [PMID: 4381351]
2.  Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659–13669. [DOI] [PMID: 17087520]
3.  Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281 (2006) 723–732. [DOI] [PMID: 16286454]
4.  Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47 (2008) 1827–1836. [DOI] [PMID: 18198901]
5.  Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N′-diacetylbacillosamine. Biochemistry 50 (2011) 4936–4948. [DOI] [PMID: 21542610]
[EC 2.6.1.34 created 1972, modified 2013]
 
 
EC 3.1.6.15     Relevance: 90.6%
Accepted name: N-sulfoglucosamine-3-sulfatase
Reaction: Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin
Other name(s): chondroitinsulfatase
Systematic name: N-sulfo-3-sulfoglucosamine 3-sulfohydrolase
Comments: The enzyme from Flavobacterium heparinum also hydrolyses N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bruce, J.S., McLean, M.W., Long, W.F. and Williamson, F.B. Flavobacterium heparinum 3-O-sulphatase for N-substituted glucosamine 3-O-sulphate. Eur. J. Biochem. 148 (1985) 359–365. [DOI] [PMID: 3987694]
2.  Leder, I.G. A novel 3-O sulfatase from human urine acting on methyl-2-deoxy-2-sulfamino-α-D-glucopyranoside 3-sulfate. Biochem. Biophys. Res. Commun. 94 (1980) 1183–1189. [DOI] [PMID: 7396957]
[EC 3.1.6.15 created 1984, modified 1989]
 
 
EC 3.2.1.159     Relevance: 90.5%
Accepted name: α-neoagaro-oligosaccharide hydrolase
Reaction: Hydrolysis of the (1→3)-α-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose
Glossary: In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not.
For example:
neoagarobiose = 3,6-anhydro-α-L-galactopyranosyl-(1→3)-D-galactose
agarobiose = β-D-galactopyranosyl-(1→4)-3,6-anhydro-L-galactose
Other name(s): α-neoagarooligosaccharide hydrolase; α-NAOS hydrolase
Systematic name: α-neoagaro-oligosaccharide 3-glycohydrolase
Comments: When neoagarohexaose is used as a substrate, the oligosaccharide is cleaved at the non-reducing end to produce 3,6-anhydro-L-galactose and agaropentaose, which is further hydrolysed to agarobiose and agarotriose. With neoagarotetraose as substrate, the products are predominantly agarotriose and 3,6-anhydro-L-galactose. In Vibrio sp. the actions of EC 3.2.1.81, β-agarase and EC 3.2.1.159 can be used to degrade agarose to 3,6-anhydro-L-galactose and D-galactose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-77-6
References:
1.  Sugano, Y., Kodama, H., Terada, I., Yamazaki, Y. and Noma, M. Purification and characterization of a novel enzyme, α-neoagarooligosaccharide hydrolase (α-NAOS hydrolase), from a marine bacterium, Vibrio sp. strain JT0107. J. Bacteriol. 176 (1994) 6812–6818. [DOI] [PMID: 7961439]
[EC 3.2.1.159 created 2006]
 
 
EC 4.2.1.126     Relevance: 90.3%
Accepted name: N-acetylmuramic acid 6-phosphate etherase
Reaction: (R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O
Other name(s): MurNAc-6-P etherase; MurQ
Systematic name: (R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming)
Comments: This enzyme, along with EC 2.7.1.170, anhydro-N-acetylmuramic acid kinase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium’s own cell wall murein during cell wall recycling.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Jaeger, T., Arsic, M. and Mayer, C. Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase". J. Biol. Chem. 280 (2005) 30100–30106. [DOI] [PMID: 15983044]
2.  Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M. and Park, J.T. Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J. Bacteriol. 187 (2005) 3643–3649. [DOI] [PMID: 15901686]
3.  Uehara, T., Suefuji, K., Jaeger, T., Mayer, C. and Park, J.T. MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall. J. Bacteriol. 188 (2006) 1660–1662. [DOI] [PMID: 16452451]
4.  Hadi, T., Dahl, U., Mayer, C. and Tanner, M.E. Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling. Biochemistry 47 (2008) 11547–11558. [DOI] [PMID: 18837509]
5.  Jaeger, T. and Mayer, C. N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism. Cell. Mol. Life Sci. 65 (2008) 928–939. [DOI] [PMID: 18049859]
[EC 4.2.1.126 created 2011]
 
 
EC 2.4.1.180     Relevance: 89.5%
Accepted name: lipopolysaccharide N-acetylmannosaminouronosyltransferase
Reaction: UDP-N-acetyl-α-D-mannosaminouronate + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate
Other name(s): ManNAcA transferase; uridine diphosphoacetylmannosaminuronate-acetylglucosaminylpyrophosphorylundecaprenol acetylmannosaminuronosyltransferase; UDP-N-acetyl-β-D-mannosaminouronate:lipid I N-acetyl-β-D-mannosaminouronosyltransferase (incorrect)
Systematic name: UDP-N-acetyl-α-D-mannosaminouronate:lipid I N-acetyl-α-D-mannosaminouronosyltransferase
Comments: Involved in the biosynthesis of common antigen in Enterobacteriaceae.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113478-30-1
References:
1.  Barr, K., Ward, S., Meier-Dieter, U., Mayer, H. and Rick, P.D. Characterization of an Escherichia coli rff mutant defective in transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA to a lipid-linked intermediate involved in enterobacterial common antigen synthesis. J. Bacteriol. 170 (1988) 228–233. [DOI] [PMID: 3275612]
[EC 2.4.1.180 created 1990, modified 2011]
 
 
EC 2.7.1.183     Relevance: 89.1%
Accepted name: glycoprotein-mannosyl O6-kinase
Reaction: ATP + O3-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl/L-seryl-[protein] = ADP + O3-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-(6-phospho)mannosyl]-L-threonyl/L-seryl-[protein]
For diagram of glycoprotein biosynthesis, click here
Other name(s): SGK196; protein O-mannose kinase
Systematic name: ATP:O3-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl/L-seryl-[protein] 6-phosphotransferase
Comments: In humans this phosphorylated trisaccharide is attached to an L-threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains, and is important for its activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]
[EC 2.7.1.183 created 2014]
 
 
EC 3.2.1.183     Relevance: 88.6%
Accepted name: UDP-N-acetylglucosamine 2-epimerase (hydrolysing)
Reaction: UDP-N-acetyl-α-D-glucosamine + H2O = N-acetyl-D-mannosamine + UDP
For diagram of N-acetylneuraminic acid biosynthesis, click here, and for mechanism, click here
Other name(s): UDP-N-acetylglucosamine 2-epimerase (ambiguous); GNE (gene name); siaA (gene name); neuC (gene name)
Systematic name: UDP-N-acetyl-α-D-glucosamine hydrolase (2-epimerising)
Comments: The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus. It catalyses the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The initial product formed is the α anomer, which rapidly mutarotates to a mixture of anomers [2]. The mammalian enzyme is bifunctional and also catalyses EC 2.7.1.60, N-acetylmannosamine kinase. cf. EC 5.1.3.14, UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Stasche, R., Hinderlich, S., Weise, C., Effertz, K., Lucka, L., Moormann, P. and Reutter, W. A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase. J. Biol. Chem. 272 (1997) 24319–24324. [DOI] [PMID: 9305888]
2.  Chou, W.K., Hinderlich, S., Reutter, W. and Tanner, M.E. Sialic acid biosynthesis: stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase. J. Am. Chem. Soc. 125 (2003) 2455–2461. [DOI] [PMID: 12603133]
3.  Blume, A., Ghaderi, D., Liebich, V., Hinderlich, S., Donner, P., Reutter, W. and Lucka, L. UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, functionally expressed in and purified from Escherichia coli, yeast, and insect cells. Protein Expr. Purif. 35 (2004) 387–396. [DOI] [PMID: 15135418]
4.  Murkin, A.S., Chou, W.K., Wakarchuk, W.W. and Tanner, M.E. Identification and mechanism of a bacterial hydrolyzing UDP-N-acetylglucosamine 2-epimerase. Biochemistry 43 (2004) 14290–14298. [DOI] [PMID: 15518580]
[EC 3.2.1.183 created 2012]
 
 
EC 2.7.8.35     Relevance: 88.6%
Accepted name: UDP-N-acetylglucosamine—decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + trans,octacis-decaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol
For diagram of galactofuranan biosynthesis, click here
Other name(s): GlcNAc-1-phosphate transferase; UDP-GlcNAc:undecaprenyl phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Comments: Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis. This enzyme catalyses the synthesis of monotrans,octacis-decaprenyl-N-acetyl-α-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. cf. EC 2.7.8.33, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jin, Y., Xin, Y., Zhang, W. and Ma, Y. Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 have WecA function and MSMEG_4947 is required for the growth of M. smegmatis. FEMS Microbiol. Lett. 310 (2010) 54–61. [DOI] [PMID: 20637039]
[EC 2.7.8.35 created 2012]
 
 
EC 2.3.1.72     Relevance: 88.5%
Accepted name: indoleacetylglucose—inositol O-acyltransferase
Reaction: 1-O-(indol-3-yl)acetyl-β-D-glucose + myo-inositol = D-glucose + O-(indol-3-yl)acetyl-myo-inositol
Other name(s): indole-3-acetyl-β-1-D-glucoside:myo-inositol indoleacetyltransferase; 1-O-(indol-3-ylacetyl)-β-D-glucose:myo-inositol indole-3-ylacetyltransferase
Systematic name: 1-O-(indol-3-yl)acetyl-β-D-glucose:myo-inositol (indol-3-yl)acetyltransferase
Comments: The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74082-57-8
References:
1.  Michalczuk, L. and Bandurski, R.S. Enzymic synthesis of 1-O-indol-3-ylacetyl-β-D-glucose and indol-3-ylacetyl-myo-inositol. Biochem. J. 207 (1982) 273–281. [PMID: 6218801]
2.  Michalczuk, L. and Bandurski, R.S. UDP-glucose: indoleacetic acid glucosyl transferase and indoleacetyl-glucose: myo-inositol indoleacetyl transferase. Biochem. Biophys. Res. Commun. 93 (1980) 588–592. [DOI] [PMID: 6446303]
[EC 2.3.1.72 created 1984, modified 2003]
 
 
EC 2.4.1.272     Relevance: 88.5%
Accepted name: soyasapogenol B glucuronide galactosyltransferase
Reaction: UDP-α-D-galactose + soyasapogenol B 3-O-β-D-glucuronide = UDP + soyasaponin III
For diagram of soyasapogenol biosynthesis, click here
Glossary: soyasaponin III = 3β-(2-O-β-D-galactopyranosyl-β-D-glucopyranosyloxyuronic acid)olean-12-ene-22β,24-diol
Other name(s): UDP-galactose:SBMG-galactosyltransferase; UGT73P2; GmSGT2 (gene name); UDP-galactose:soyasapogenol B 3-O-glucuronide β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:soyasapogenol B 3-O-glucuronide β-D-galactosyltransferase
Comments: Part of the biosynthetic pathway for soyasaponins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Nishimura, K., Yasuyama, N. and Ebizuka, Y. Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584 (2010) 2258–2264. [DOI] [PMID: 20350545]
[EC 2.4.1.272 created 2011]
 
 
EC 3.2.1.158     Relevance: 88.2%
Accepted name: α-agarase
Reaction: Endohydrolysis of (1→3)-α-L-galactosidic linkages in agarose, yielding agarotetraose as the major product
Glossary: agarose = a linear polysaccharide produced by some members of the Rhodophyta (red algae) made up from alternating D-galactose and 3,6-anhydro-α-L-galactopyranose residues joined by α-(1→3)- and β-(1→4)-linkages. In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not.
For example:
neoagarobiose = 3,6-anhydro-α-L-galactopyranosyl-(1→3)-D-galactose
agarobiose = β-D-galactopyranosyl-(1→4)-3,6-anhydro-L-galactose
Other name(s): agarase (ambiguous); agaraseA33
Systematic name: agarose 3-glycanohydrolase
Comments: Requires Ca2+. The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate. The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer. While the enzyme can also hydrolyse the highly sulfated agarose porphyran very efficiently, it cannot hydrolyse the related compounds κ-carrageenan (see EC 3.2.1.83) and ι-carrageenan (see EC 3.2.1.157) [2]. See also EC 3.2.1.81, β-agarase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63952-00-1
References:
1.  Potin, P., Richard, C., Rochas, C. and Kloareg, B. Purification and characterization of the α-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B. Eur. J. Biochem. 214 (1993) 599–607. [DOI] [PMID: 8513809]
2.  Ohta, Y., Hatada, Y., Miyazaki, M., Nogi, Y., Ito, S. and Horikoshi, K. Purification and characterization of a novel α-agarase from a Thalassomonas sp. Curr. Microbiol. 50 (2005) 212–216. [DOI] [PMID: 15902469]
[EC 3.2.1.158 created 2006]
 
 


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