ExplorEnz: EC 2.4.99.*

Your query returned 15 entries. Printable version

2.4.99.1

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

Other name(s):

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

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, IUBMB, 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 2.4.99.1 created 1972, modified 1976, modified 1986]

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

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, IUBMB, 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 α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198]
2.	Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5′-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM1) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298–306. [PMID: 4351506]

[EC 2.4.99.2 created 1976, modified 1986]

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, IUBMB, 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 α2→6 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 5934–5941. [PMID: 447688]

[EC 2.4.99.3 created 1984, modified 1986]

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, IUBMB, 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 α2→3 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 α2→3 sialyltransferase and partial purification of an α-N-acetylgalactosaminide α2→6 sialyltransferase from porcine submaxillary glands. J. Biol. Chem. 254 (1979) 4434–4442. [PMID: 438196]

[EC 2.4.99.4 created 1984, modified 1986]

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, IUBMB, 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 β1→4GlcNAc α2→6 sialyltransferase and a Gal β1→3(4)GlcNAc α2→3 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 β1→3(4)GlcNAc α2→3 sialyltransferase and a Gal β1→4GlcNAc α2→6 sialyltransferase from rat liver. J. Biol. Chem. 257 (1982) 13845–13853. [PMID: 7142180]

[EC 2.4.99.5 created 1984, modified 1986]

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(1→4)acetylglucosaminide α2→3-sialyltransferase; α2→3 sialyltransferase; SiaT; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein α-2,3-N-acetylneuraminyltransferase

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, IUBMB, KEGG, CAS registry number: 77537-85-0

References:

1.	Van den Eijnden, D.H. and Schiphorst, W.E.C.M. Detection of β-galactosyl(1→4)N-acetylglucosaminide α(2→3)-sialyltransferase activity in fetal calf liver and other tissues. J. Biol. Chem. 256 (1981) 3159–3162. [PMID: 7204397]

[EC 2.4.99.6 created 1984, modified 1986]

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 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-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, IUBMB, KEGG, CAS registry number: 129924-24-9

References:

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 2.4.99.7 created 1984, modified 1986, modified 2004]

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

Other name(s):

cytidine monophosphoacetylneuraminate-ganglioside G_M3; α-2,8-sialyltransferase; ganglioside G_D3 synthase; ganglioside G_D3 synthetase sialyltransferase; CMP-NeuAc:LM1(α2-8) sialyltranferase; G_D3 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, IUBMB, 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, GT 1a. J. Biol. Chem. 255 (1980) 608–613. [PMID: 6766128]

[EC 2.4.99.8 created 1984, modified 1986]

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

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, IUBMB, 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 2.4.99.9 created 1984, modified 1986]

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; CMP-N-acetylneuraminate:neolactotetraosylceramide α-2,3-sialyltransferase; 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 α-(2→3)-sialyltransferase

Systematic name:

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 α-(2→3)-sialyltransferase

Links to other databases:

BRENDA, EXPASY, IUBMB, 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 2.4.99.10 created 1986]

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

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; cytidine monophosphoacetylneuraminate-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, IUBMB, 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 2.4.99.11 created 1992]

2.4.99.12

Accepted name:

lipid IV_A 3-deoxy-D-manno-octulosonic acid transferase

Reaction:

2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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-3-deoxy-D-manno-octulosonate = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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

Glossary:

lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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 = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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

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-octulosonate:lipid IV_A 3-deoxy-D-manno-octulosonate transferase

Comments:

The bifunctional enzyme from Escherichia coli transfers two 3-deoxy-D-manno-octulosonate 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-octulosonate residue from CMP-3-deoxy-D-manno-octulosonate to lipid IV_A [2,3]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-octulosonate residues and generate genus-specific epitopes [4].

Links to other databases:

BRENDA, EXPASY, IUBMB, KEGG

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 2.4.99.12 created 2010]

2.4.99.13

Accepted name:

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

Reaction:

3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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-3-deoxy-D-manno-octulosonate = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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

Glossary:

(KDO)-lipid IV_A = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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 = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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

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-octulosonate:(KDO)-lipid IV_A 3-deoxy-D-manno-octulosonate transferase

Comments:

The bifunctional enzyme from Escherichia coli transfers two 3-deoxy-D-manno-octulosonate 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-octulosonate residues and generate genus-specific epitopes [4].

Links to other databases:

BRENDA, EXPASY, IUBMB, KEGG

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 2.4.99.13 created 2010]

2.4.99.14

Accepted name:

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

Reaction:

3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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-3-deoxy-D-manno-octulosonate = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→8)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosy[l-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyrano]syl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanoyl]amino-1-O-phosphono-α-D-glucopyranose + CMP

Glossary:

(KDO)₂-lipid IV_A = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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 = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→8)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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

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-octulosonate:(KDO)₂-lipid IV_A 3-deoxy-D-manno-octulosonate transferase ((2→8) glycosidic bond-forming)

Comments:

The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-octulosonate residues and generate genus-specific epitopes.

Links to other databases:

BRENDA, EXPASY, IUBMB, KEGG

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 2.4.99.14 created 2010]

2.4.99.15

Accepted name:

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

Reaction:

3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→8)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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-3-deoxy-D-manno-octulosonate = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→8)-[3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)]-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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

Glossary:

(KDO)₃-lipid IV_A = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→8)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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 = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→8)-[3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-hydroxypentadecanoyl]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

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-octulosonate:(KDO)₃-lipid IV_A 3-deoxy-D-manno-octulosonate 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, IUBMB, KEGG

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]

[EC 2.4.99.15 created 2010]