EC 2.4.99

Contents

EC 2.4.99.12 lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase
EC 2.4.99.13 (KDO)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase
EC 2.4.99.14 (KDO)₂-lipid IV_A (2-8) 3-deoxy-D-manno-octulosonic acid transferase
EC 2.4.99.15 (KDO)₃-lipid IV_A (2-4) 3-deoxy-D-manno-octulosonic acid transferase

Entries

Accepted name: β-galactoside α-2,6-sialyltransferase

Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine = CMP + α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine

Systematic name: CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase

Comments: The terminal β-D-galactosyl residue of the oligosaccharide of glycoproteins, as well as lactose, can act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9075-81-4

References:

1. Bartholomew, B.A., Jourdian, G.W. and Roseman, S. The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum. J. Biol. Chem. 248 (1973) 5751-5762. [PMID: 4723915]

2. Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H.Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-¹⁴C-labeled ceruloplasmin. J. Biol. Chem. 245 (1970) 759-766. [PMID: 4313609]

3. Paulson, J.C., Beranek, W.E. and Hill, R.L. Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. J. Biol. Chem. 252 (1977) 2356-2362. [PMID: 849932]

4. 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]

5. Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase. J. Biol. Chem. 243 (1968) 6520-6528. [PMID: 5726897]

EC 2.4.99.2

Accepted name: monosialoganglioside sialyltransferase

Reaction: CMP-N-acetylneuraminate + D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide = CMP + N-acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide

For diagram of reaction click here.

Other name(s): CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide N-acetylneuraminyltransferase; CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl(1↔1)ceramide N-acetylneuraminyltransferase

Systematic name: CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide N-acetylneuraminyltransferase

Comments: May be identical with EC 2.4.99.4 β-galactoside α-2,3-sialyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 60202-12-2

References:

1. Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α23 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444-4451. [PMID: 438198]

2. Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5'-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM₁) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298-306. [PMID: 4351506]

EC 2.4.99.3

Accepted name: α-N-acetylgalactosaminide α-2,6-sialyltransferase

Reaction: CMP-N-acetylneuraminate + glycano-(1→3)-(N-acetyl-α-D-galactosaminyl)-glycoprotein = CMP + glycano-[(2→6)-α-N-acetylneuraminyl]-(N-acetyl-D-galactosaminyl)-glycoprotein

Systematic name: CMP-N-acetylneuraminate:glycano-1,3-(N-acetyl-α-D-galactosaminyl)-glycoprotein α-2,6-N-acetylneuraminyltransferase

Comments: α-N-Acetylgalactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 71124-50-0

References:

1. Sadler, J.E., Rearick, J.I. and Hill, R.L. Purification to homogeneity and enzymatic characterization of an α-N-acetylgalactosaminide α26 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 5934-5941. [PMID: 447688]

EC 2.4.99.4

Accepted name: β-galactoside α-2,3-sialyltransferase

Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R

Other name(s): CMP-N-acetylneuraminate:β-D-galactoside α-2,3-N-acetylneuraminyl-transferase

Systematic name: CMP-N-acetylneuraminate:β-D-galactoside α-(2→3)-N-acetylneuraminyl-transferase

Comments: The acceptor is Galβ1,3GalNAc-R, where R is H, a threonine or serine residue in a glycoprotein, or a glycolipid. Lactose can also act as acceptor. May be identical with EC 2.4.99.2 monosialoganglioside sialyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 71124-51-1

References:

1. Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α23 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444-4451. [PMID: 438198]

2. Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Purification to homogeneity of a β-galactoside α23 sialyltransferase and partial purification of an α-N-acetylgalactosaminide α26 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 4434-4442. [PMID: 438196]

EC 2.4.99.5

Accepted name: galactosyldiacylglycerol α-2,3-sialyltransferase

Reaction: CMP-N-acetylneuraminate + 1,2-diacyl-3-β-D-galactosyl-sn-glycerol = CMP + 1,2-diacyl-3-[3-(α-D-N-acetylneuraminyl)-β-D-galactosyl]-sn-glycerol

Systematic name: CMP-N-acetylneuraminate:1,2-diacyl-3-β-D-galactosyl-sn-glycerol N-acetylneuraminyltransferase

Comments: The β-D-galactosyl residue of the oligosaccharide of glycoproteins may also act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 80237-98-5

References:

1. Pieringer, J., Keech, S. and Pieringer, R.A. Biosynthesis in vitro of sialosylgalactosyldiacylglycerol by mouse brain microsomes. J. Biol. Chem. 256 (1981) 12306-12309. [PMID: 7298658]

2. Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. Purification of a Gal β14GlcNAc α26 sialyltransferase and a Gal β13(4)GlcNAc α23 sialyltransferase to homogeneity from rat liver. J. Biol. Chem. 257 (1982) 13835-13844. [PMID: 7142179]

3. Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal β13(4)GlcNAc α23 sialyltransferase and a Gal β14GlcNAc α26 sialyltransferase from rat liver. J. Biol. Chem. 257 (1982) 13845-13853. [PMID: 7142180]

EC 2.4.99.6

Accepted name: N-acetyllactosaminide α-2,3-sialyltransferase

Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-glycoprotein = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-glycoprotein

Other name(s): sialyltransferase; cytidine monophosphoacetylneuraminate-β-galactosyl(14)acetylglucosaminide α23-sialyltransferase; α23 sialyltransferase

Systematic name: CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein α-2,3-N-acetylneuraminyltransferase

Comments: Acts on β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoprotein.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 77537-85-0

References:

1. Van den Eijnden, D.H. and Schiphorst, W.E.C.M. Detection of β-galactosyl(14)N-acetylglucosaminide α(23)-sialyltransferase activity in fetal calf liver and other tissues. J. Biol. Chem. 256 (1981) 3159-3162. [PMID: 7204397]

EC 2.4.99.7

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 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:(α-N-acetylneuraminyl-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-acetyl-galactosamine only when present in the structure of α-N-acetyl-neuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.99.3 α-N-acetylgalactosaminide α-2,6-sialyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, 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 α26 sialyltransferase with a narrow acceptor specificity in fetal calf liver. J. Biol. Chem. 258 (1983) 7430-7436. [PMID: 6190802]

EC 2.4.99.8

Accepted name: α-N-acetylneuraminate α-2,8-sialyltransferase

Reaction: CMP-N-acetylneuraminate + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R = CMP + α-N-acetylneuraminyl-(2→8)-α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R

For diagram of reaction click here.

Other name(s): cytidine monophosphoacetylneuraminate-ganglioside GM3; α-2,8-sialyltransferase; ganglioside GD3 synthase; ganglioside GD3 synthetase sialyltransferase; CMP-NeuAc:LM1(α2-8) sialyltranferase; GD3 synthase; SAT-2

Systematic name: CMP-N-acetylneuraminate:α-N-acetylneuraminyl-2,3-β-D-galactoside α-2,8-N-acetylneuraminyltransferase

Comments: Gangliosides act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 67339-00-8

References:

1. Eppler, M.C., Morré, J.D. and Keenan, T.W. Ganglioside biosynthesis in rat liver: alteration of sialyltransferase activities by nucleotides. Biochim. Biophys. Acta 619 (1980) 332-343. [PMID: 7407217]

2. Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824-828. [PMID: 3838172]

3. McCoy, R.D., Vimr, E.R. and Troy, F.A. CMP-NeuNAc:poly-α-2,8-sialosyl sialyltransferase and the biosynthesis of polysialosyl units in neural cell adhesion molecules. J. Biol. Chem. 260 (1985) 12695-12699. [PMID: 4044605]

4. Yohe, H.C. and Yu, R.K. In vitro biosynthesis of an isomer of brain trisialoganglioside, GT1a. J. Biol. Chem. 255 (1980) 608-613. [PMID: 6766128]

EC 2.4.99.9

Accepted name: lactosylceramide α-2,3-sialyltransferase

Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of reaction click here.

Glossary: lactosylceramide = β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide

Other name(s): cytidine monophosphoacetylneuraminate-lactosylceramide α2,3- sialyltransferase; CMP-acetylneuraminate-lactosylceramide-sialyltransferase; CMP-acetylneuraminic acid:lactosylceramide sialyltransferase; CMP-sialic acid:lactosylceramide-sialyltransferase; cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase; ganglioside G_M3 synthetase; G_M3 synthase; G_M3 synthetase; SAT 1; CMP-N-acetylneuraminate:lactosylceramide α-2,3-N-acetylneuraminyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide α-(2→3)-N-acetylneuraminyltransferase

Systematic name: CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide α-(2→3)-N-acetylneuraminyltransferase

Comments: Lactose cannot act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 125752-90-1

References:

1. Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388-1394. [PMID: 4631392]

2. Fishman, P.H., Bradley, R.M. and Henneberry, R.C. Butyrate-induced glycolipid biosynthesis in HeLa cells: properties of the induced sialyltransferase. Arch. Biochem. Biophys. 172 (1976) 618-626. [PMID: 4022]

3. Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824-828. [PMID: 3838172]

EC 2.4.99.10

Accepted name: neolactotetraosylceramide α-2,3-sialyltransferase

Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide

Glossary: neolactotetraosylceramide = β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide

Other name(s): sialyltransferase; cytidine monophosphoacetylneuraminate-neolactotetraosylceramide sialyltransferase; sialyltransferase 3; SAT-3

Systematic name: CMP-N-acetylneuraminate:neolactotetraosylceramide α-2,3-sialyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 83745-06-6

References:

1. Basu, M., Basu, S., Stoffyn, A. and Stoffyn, P. Biosynthesis in vitro of sialyl(α2-3)neolactotetraosylceramide by a sialyltransferase from embryonic chicken brain. J. Biol. Chem. 257 (1982) 12765-12769. [PMID: 7130178]

EC 2.4.99.11

Accepted name: lactosylceramide α-2,6-N-sialyltransferase

Reaction: CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = CMP + α-N-acetylneuraminyl-(2→6)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of reaction click here.

Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

Other name(s): cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase; CMP-acetylneuraminate-lactosylceramide-sialyltransferase; CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase; CMP-sialic acid:lactosylceramide sialyltransferase; CMP-N-acetylneuraminate:lactosylceramide α-2,6-N-acetylneuraminyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide α-(2→6)-N-acetylneuraminyltransferase

Systematic name: CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide α-(2→6)-N-acetylneuraminyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 55071-95-9

References:

1. Albarracin, I., Lassaga, F.E. and Caputto, R. Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biochem. J. 254 (1988) 559-565. [PMID: 2460092]

2. Landa, C.A., Maccioni, H.J.F., Arce, A. and Caputto, R. The biosynthesis of brain gangliosides. Separation of membranes with different ratios of ganglioside sialylating activity to gangliosides. Biochem. J. 168 (1977) 325-332. [PMID: 606237]

EC 2.4.99.12

Accepted name: lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase

Reaction: lipid IV_A + CMP-α-Kdo = α-Kdo-(2→6)-lipid IV_A + CMP

Glossary: lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(KDO)-lipid IV_A = α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
CMP-α-Kdo = CMP-3-deoxy-α-D-manno-oct-2-ulopyranosylonate

Other name(s): KDO transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; lipid IV_A KDO transferase

Systematic name: CMP-3-deoxy-D-manno-oct-2-ulosonate:lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase

Comments: The bifunctional enzyme from Escherichia coli transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IV_A (cf. EC 2.4.99.13 [(KDO)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The monofunctional enzymes from Aquifex aeolicus and Haemophilus influenzae catalyse the transfer of a single 3-deoxy-D-manno-oct-2-ulosonate residue from CMP-3-deoxy-D-manno-oct-2-ulosonate to lipid IV_A [2,3]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [4].

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:

References:

1. Belunis, C.J. and Raetz, C.R. Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli. J. Biol. Chem. 267 (1992) 9988-9997. [PMID: 1577828]

2. Mamat, U., Schmidt, H., Munoz, E., Lindner, B., Fukase, K., Hanuszkiewicz, A., Wu, J., Meredith, T.C., Woodard, R.W., Hilgenfeld, R., Mesters, J.R. and Holst, O. WaaA of the hyperthermophilic bacterium Aquifex aeolicus is a monofunctional 3-deoxy-D-manno-oct-2-ulosonic acid transferase involved in lipopolysaccharide biosynthesis. J. Biol. Chem. 284 (2009) 22248-22262. [PMID: 19546212]

3. White, K.A., Kaltashov, I.A., Cotter, R.J. and Raetz, C.R. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae. J. Biol. Chem. 272 (1997) 16555-16563. [PMID: 9195966]

4. Lobau, S., Mamat, U., Brabetz, W. and Brade, H. Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-α-D-manno-octulosonic acid transferase of Chlamydia pneumoniae strain TW-183. Mol. Microbiol. 18 (1995) 391-399. [PMID: 8748024]

EC 2.4.99.13

Accepted name: (KDO)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase

Reaction: α-Kdo-(2→6)-lipid IV_A + CMP-α-Kdo = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP

Glossary: (KDO)-lipid IV_A = α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(KDO)₂-lipid IV_A = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
CMP-α-Kdo = CMP-3-deoxy-α-D-manno-oct-2-ulopyranosylonate

Other name(s): KDO transferase; waaA (gene name); kdtA (gene name); Kdo transferase; 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase

Systematic name: CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)-lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase

Comments: The bifunctional enzyme from Escherichia coli transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IV_A (cf. EC 2.4.99.12 [lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [4].

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:

References:

1. Belunis, C.J. and Raetz, C.R. Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli. J. Biol. Chem. 267 (1992) 9988-9997. [PMID: 1577828]

2. Lobau, S., Mamat, U., Brabetz, W. and Brade, H. Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-α-D-manno-octulosonic acid transferase of Chlamydia pneumoniae strain TW-183. Mol. Microbiol. 18 (1995) 391-399. [PMID: 8748024]

EC 2.4.99.14

Accepted name: (KDO)₂-lipid IV_A (2-8) 3-deoxy-D-manno-octulosonic acid transferase

Reaction: α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP-α-Kdo = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP

Glossary: (KDO)₂-lipid IV_A = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(KDO)₃-lipid IV_A = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
CMP-α-Kdo = CMP-3-deoxy-α-D-manno-oct-2-ulopyranosylonate

Other name(s): KDO transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase

Systematic name: CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)₂-lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase [(2→8) glycosidic bond-forming]

Comments: The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes.

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:

References:

1. Lobau, S., Mamat, U., Brabetz, W. and Brade, H. Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-α-D-manno-octulosonic acid transferase of Chlamydia pneumoniae strain TW-183. Mol. Microbiol. 18 (1995) 391-399. [PMID: 8748024]

2. Mamat, U., Baumann, M., Schmidt, G. and Brade, H. The genus-specific lipopolysaccharide epitope of Chlamydia is assembled in C. psittaci and C. trachomatis by glycosyltransferases of low homology. Mol. Microbiol. 10 (1993) 935-941. [PMID: 7523826]

3. Belunis, C.J., Mdluli, K.E., Raetz, C.R. and Nano, F.E. A novel 3-deoxy-D-manno-octulosonic acid transferase from Chlamydia trachomatis required for expression of the genus-specific epitope. J. Biol. Chem. 267 (1992) 18702-18707. [PMID: 1382060]

EC 2.4.99.15

Accepted name: (KDO)₃-lipid IV_A (2-4) 3-deoxy-D-manno-octulosonic acid transferase

Reaction: α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP-α-Kdo = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A + CMP

Glossary: (KDO)₃-lipid IV_A = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(KDO)₄-lipid IV_A = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IV_A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-[(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
CMP-α-Kdo = CMP-3-deoxy-α-D-manno-oct-2-ulopyranosylonate

Other name(s): KDO transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase

Systematic name: CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)₃-lipid IV_A 3-deoxy-D-manno-oct-2-ulosonate transferase [(2→4) glycosidic bond-forming]

Comments: The enzyme from Chlamydia psittaci transfers four KDO residues to lipid A, forming a branched tetrasaccharide with the structure α-KDO-(2,8)-[α-KDO-(2,4)]-α-KDO-(2,4)-α-KDO (cf. EC 2.4.99.12 [lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase], EC 2.4.99.13 [(KDO)-lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase], and EC 2.4.99.14 [(KDO)₂-lipid IV_A (2-8) 3-deoxy-D-manno-octulosonic acid transferase]).

Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:

References:

1. Brabetz, W., Lindner, B. and Brade, H. Comparative analyses of secondary gene products of 3-deoxy-D-manno-oct-2-ulosonic acid transferases from Chlamydiaceae in Escherichia coli K-12. Eur. J. Biochem. 267 (2000) 5458-5465. [PMID: 10951204]

2. Holst, O., Bock, K., Brade, L. and Brade, H. The structures of oligosaccharide bisphosphates isolated from the lipopolysaccharide of a recombinant Escherichia coli strain expressing the gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] of Chlamydia psittaci 6BC. Eur. J. Biochem. 229 (1995) 194-200. [PMID: 7744029]