EC |
1.1.1.261 |
Accepted name: |
sn-glycerol-1-phosphate dehydrogenase |
Reaction: |
sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+ |
|
For diagram of archaetidylserine biosynthesis, click here and for diagram of archaetidylserine biosynthesis, click here |
Glossary: |
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate |
Other name(s): |
glycerol-1-phosphate dehydrogenase [NAD(P)+]; sn-glycerol-1-phosphate:NAD+ oxidoreductase; G-1-P dehydrogenase; Gro1PDH; AraM |
Systematic name: |
sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase |
Comments: |
This enzyme is found primarily as a Zn2+-dependent form in archaea but a Ni2+-dependent form has been found in Gram-positive bacteria [6]. The Zn2+-dependent metalloenzyme is responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea. It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase) and EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [4]. Activity of the enzyme is stimulated by K+ [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 204594-18-3 |
References: |
1. |
Nishihara, M. and Koga, Y. sn-Glycerol-1-phosphate dehydrogenase in Methanobacterium thermoautotrophicum: key enzyme in biosynthesis of the enantiomeric glycerophosphate backbone of ether phospholipids of archaebacteria. J. Biochem. 117 (1995) 933–935. [PMID: 8586635] |
2. |
Nishihara, M. and Koga, Y. Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of Archaea. J. Biochem. 122 (1997) 572–576. [PMID: 9348086] |
3. |
Koga, Y., Kyuragi, T., Nishihara, M. and Sone, N. Did archaeal and bacterial cells arise independently from noncellular precursors? A hypothesis stating that the advent of membrane phospholipid with enantiomeric glycerophosphate backbones caused the separation of the two lines of descent. J. Mol. Evol. 46 (1998) 54–63. [PMID: 9419225] |
4. |
Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [DOI] [PMID: 10960477] |
5. |
Han, J.S. and Ishikawa, K. Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1. Archaea 1 (2005) 311–317. [PMID: 15876564] |
6. |
Guldan, H., Sterner, R. and Babinger, P. Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis. Biochemistry 47 (2008) 7376–7384. [DOI] [PMID: 18558723] |
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[EC 1.1.1.261 created 2000, modified 2009] |
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EC
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1.14.13.45
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Transferred entry: | CMP-N-acetylneuraminate monooxygenase. Now EC 1.14.18.2, CMP-N-acetylneuraminate monooxygenase
|
[EC 1.14.13.45 created 1992, deleted 2003] |
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EC |
1.14.18.2 |
Accepted name: |
CMP-N-acetylneuraminate monooxygenase |
Reaction: |
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ = CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O |
Other name(s): |
CMP-N-acetylneuraminic acid hydroxylase; CMP-Neu5Ac hydroxylase; cytidine monophosphoacetylneuraminate monooxygenase; N-acetylneuraminic monooxygenase; cytidine-5′-monophosphate-N-acetylneuraminic acid hydroxylase |
Systematic name: |
CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating) |
Comments: |
This enzyme contains both a Rieske-type [2Fe-2S] cluster and a second iron site. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2). The enzyme can be activated by Fe2+ or Fe3+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 116036-67-0 |
References: |
1. |
Shaw, L. and Schauer, R. The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid. Biol. Chem. Hoppe-Seyler 369 (1988) 477–486. [PMID: 3202954] |
2. |
Kozutsumi, Y., Kawano, T., Yamakawa, T. and Suzuki, A. Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol. J. Biochem. (Tokyo) 109 (1990) 704–706. [PMID: 1964451] |
3. |
Schneckenburger, P., Shaw, L. and Schauer, R. Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver. Glycoconj. J. 11 (1994) 194–203. [PMID: 7841794] |
4. |
Kawano, T., Koyama, S., Takematsu, H., Kozutsumi, Y., Kawasaki, H., Kawashima, S., Kawasaki, T. and Suzuki, A. Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem. 270 (1995) 16458–16463. [DOI] [PMID: 7608218] |
5. |
Schlenzka, W., Shaw, L., Kelm, S., Schmidt, C.L., Bill, E., Trautwein, A.X., Lottspeich, F. and Schauer, R. CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya. FEBS Lett. 385 (1996) 197–200. [DOI] [PMID: 8647250] |
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[EC 1.14.18.2 created 1992 as EC 1.14.13.45, transferred 2003 to EC 1.14.18.2] |
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EC
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1.14.99.18
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Deleted entry: | CMP-N-acetylneuraminate monooxygenase |
[EC 1.14.99.18 created 1976, modified 1999, deleted 2003] |
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EC |
2.1.1.54 |
Accepted name: |
deoxycytidylate C-methyltransferase |
Reaction: |
5,10-methylenetetrahydrofolate + dCMP = dihydrofolate + deoxy-5-methylcytidylate |
Other name(s): |
deoxycytidylate methyltransferase; dCMP methyltransferase |
Systematic name: |
5,10-methylenetetrahydrofolate:dCMP C-methyltransferase |
Comments: |
dCMP is methylated by formaldehyde in the presence of tetrahydrofolate. CMP, dCTP and CTP can act as acceptors, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61970-01-2 |
References: |
1. |
Kuo, T.-T. and Tu, J. Enzymatic synthesis of deoxy-5-methyl-cytidylic acid replacing deoxycytidylic acid in Xanthomonas oryzae phage Xp12DNA. Nature 263 (1976) 615. [PMID: 980110] |
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[EC 2.1.1.54 created 1978] |
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EC |
2.1.1.351 |
Accepted name: |
nocamycin O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + nocamycin E = S-adenosyl-L-homocysteine + nocamycin I |
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For diagram of reaction, click here |
Glossary: |
nocamycin E = (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate
nocamycin I = methyl (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate |
Other name(s): |
ncmP (gene name) |
Systematic name: |
S-adenosyl-L-methionine:nocamycin E O-methyltransferase |
Comments: |
The enzyme, isolated from the bacterium Saccharothrix syringae, is involved in the biosynthesis of nocamycin I and nocamycin II. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mo, X., Gui, C. and Wang, Q. Elucidation of a carboxylate O-methyltransferase NcmP in nocamycin biosynthetic pathway. Bioorg. Med. Chem. Lett. 27 (2017) 4431–4435. [PMID: 28818448] |
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[EC 2.1.1.351 created 2018] |
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EC |
2.1.2.8 |
Accepted name: |
deoxycytidylate 5-hydroxymethyltransferase |
Reaction: |
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate |
Other name(s): |
dCMP hydroxymethylase; d-cytidine 5′-monophosphate hydroxymethylase; deoxyCMP hydroxymethylase; deoxycytidylate hydroxymethylase; deoxycytidylic hydroxymethylase |
Systematic name: |
5,10-methylenetetrahydrofolate:deoxycytidylate 5-hydroxymethyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-68-4 |
References: |
1. |
Mathews, C.K., Brown, F. and Cohen, S.S. Virus-induced acquisition of metabolic function. VII. Biosynthesis de novo of deoxycytidylate hydroxymethylase. J. Biol. Chem. 239 (1964) 2957–2963. [PMID: 14217882] |
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[EC 2.1.2.8 created 1972] |
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EC |
2.3.1.202 |
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] |
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[EC 2.3.1.202 created 2012] |
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EC |
2.4.2.57 |
Accepted name: |
AMP phosphorylase |
Reaction: |
(1) AMP + phosphate = adenine + α-D-ribose 1,5-bisphosphate (2) CMP + phosphate = cytosine + α-D-ribose 1,5-bisphosphate (3) UMP + phosphate = uracil + α-D-ribose 1,5-bisphosphate |
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For diagram of AMP catabolism, click here |
Other name(s): |
AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name) |
Systematic name: |
AMP:phosphate α-D-ribosyl 5′-phosphate-transferase |
Comments: |
The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The activity with CMP and UMP requires activation by cAMP [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Sato, T., Atomi, H. and Imanaka, T. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315 (2007) 1003–1006. [DOI] [PMID: 17303759] |
2. |
Aono, R., Sato, T., Yano, A., Yoshida, S., Nishitani, Y., Miki, K., Imanaka, T. and Atomi, H. Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway. J. Bacteriol. 194 (2012) 6847–6855. [DOI] [PMID: 23065974] |
3. |
Nishitani, Y., Aono, R., Nakamura, A., Sato, T., Atomi, H., Imanaka, T. and Miki, K. Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization. J. Mol. Biol. 425 (2013) 2709–2721. [DOI] [PMID: 23659790] |
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[EC 2.4.2.57 created 2014] |
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EC |
2.4.3.1 |
Accepted name: |
β-galactoside α-(2,6)-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + β-D-galactosyl-R = CMP + N-acetyl-α-neuraminyl-(2→6)-β-D-galactosyl-R |
Other name(s): |
ST6Gal-I; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; lactosylceramide α-2,6-N-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine α-(2→6)-N-acetylneuraminyltransferase; β-galactoside α-2,6-sialyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:β-D-galactoside α-(2→6)-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme acts on the terminal non-reducing β-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-81-4 |
References: |
1. |
Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase. J. Biol. Chem. 243 (1968) 6520–6528. [PMID: 5726897] |
2. |
Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H. Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin. J. Biol. Chem. 245 (1970) 759–766. [PMID: 4313609] |
3. |
Bartholomew, B.A., Jourdian, G.W. and Roseman, S. The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum. J. Biol. Chem. 248 (1973) 5751–5762. [PMID: 4723915] |
4. |
Paulson, J.C., Beranek, W.E. and Hill, R.L. Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. J. Biol. Chem. 252 (1977) 2356–2362. [PMID: 849932] |
5. |
Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476] |
6. |
Albarracin, I., Lassaga, F.E. and Caputto, R. Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biochem. J. 254 (1988) 559–565. [PMID: 2460092] |
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[EC 2.4.3.1 created 1972 as EC 2.4.99.1, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2016), modified 2017, transferred 2021 to EC 2.4.3.1] |
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EC |
2.4.3.2 |
Accepted name: |
β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R = CMP + an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R |
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For diagram of ganglioside biosynthesis, click here |
Glossary: |
a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GD1a |
Other name(s): |
CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide N-acetylneuraminyltransferase (ambiguous); monosialoganglioside sialyltransferase; CMP-N-acetylneuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide N-acetyl-β-neuraminyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R α-(2→3)-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme recognizes the sequence β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids [1]. When acting on gangloside GM1a, it forms gangloside GD1a [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-12-2 |
References: |
1. |
Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198] |
2. |
Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5′-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM1) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298–306. [DOI] [PMID: 4351506] |
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[EC 2.4.3.2 created 1976 as EC 2.4.99.2, modified 1986, modified 2017, transferred 2022 to EC 2.4.3.2] |
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EC |
2.4.3.3 |
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: |
N-acetyl-α-D-galactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, 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] |
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[EC 2.4.3.3 created 1984 as EC 2.4.99.3, modified 1986, transferred 2022 to EC 2.4.3.3] |
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EC |
2.4.3.4 |
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 2.4.3.2 β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, 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] |
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[EC 2.4.3.4 created 1984 as EC 2.4.99.4, modified 1986, transferred 2022 to EC 2.4.3.4] |
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EC |
2.4.3.5 |
Accepted name: |
galactosyldiacylglycerol α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + 1,2-diacyl-3-β-D-galactosyl-sn-glycerol = CMP + 1,2-diacyl-3-[3-(N-acetyl-α-D-neuraminyl)-β-D-galactosyl]-sn-glycerol |
Systematic name: |
CMP-N-acetyl-β-neuraminate: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, MetaCyc, 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] |
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[EC 2.4.3.5 created 1984 as EC 2.4.99.5, modified 1986, transferred 2022 to EC 2.4.3.5] |
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EC |
2.4.3.6 |
Accepted name: |
N-acetyllactosaminide α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R |
Other name(s): |
cytidine monophosphoacetylneuraminate-β-galactosyl(1→4)acetylglucosaminide α2→3-sialyltransferase; α2→3 sialyltransferase (ambiguous); SiaT (ambiguous); CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein α-2,3-N-acetylneuraminyltransferase; neolactotetraosylceramide α-2,3-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-glycoprotein α-(2→3)-N-acetylneuraminyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R (2→3)-N-acetyl-α-neuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme recognizes the sequence β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl (known as type 2 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids. The enzyme from chicken brain was shown to act on neolactotetraosylceramide, producing ganglioside LM1 [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77537-85-0 |
References: |
1. |
Van den Eijnden, D.H. and Schiphorst, W.E.C.M. Detection of β-galactosyl(1→4)N-acetylglucosaminide α(2→3)-sialyltransferase activity in fetal calf liver and other tissues. J. Biol. Chem. 256 (1981) 3159–3162. [PMID: 7204397] |
2. |
Basu, M., Basu, S., Stoffyn, A. and Stoffyn, P. Biosynthesis in vitro of sialyl(α2-3)neolactotetraosylceramide by a sialyltransferase from embryonic chicken brain. J. Biol. Chem. 257 (1982) 12765–12769. [PMID: 7130178] |
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[EC 2.4.3.6 created 1984 as EC 2.4.99.6, modified 1986 (EC 2.4.99.10 created 1986, incorporated 2017), transferred 2022 to EC 2.4.3.6] |
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EC |
2.4.3.7 |
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 |
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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] |
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[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] |
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EC |
2.4.3.8 |
Accepted name: |
α-N-acetylneuraminate α-2,8-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R = CMP + α-N-acetylneuraminyl-(2→8)-α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-R |
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For diagram of ganglioside biosynthesis (pathway to GD3), click here |
Other name(s): |
cytidine monophosphoacetylneuraminate-ganglioside GM3; α-2,8-sialyltransferase; ganglioside GD3 synthase; ganglioside GD3 synthetase sialyltransferase; CMP-NeuAc:LM1(α2-8) sialyltranferase; GD3 synthase; SAT-2 |
Systematic name: |
CMP-N-acetylneuraminate:α-N-acetylneuraminyl-(2→3)-β-D-galactoside α-(2→8)-N-acetylneuraminyltransferase |
Comments: |
Gangliosides act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67339-00-8 |
References: |
1. |
Eppler, M.C., Morré, J.D. and Keenan, T.W. Ganglioside biosynthesis in rat liver: alteration of sialyltransferase activities by nucleotides. Biochim. Biophys. Acta 619 (1980) 332–343. [DOI] [PMID: 7407217] |
2. |
Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824–828. [PMID: 3838172] |
3. |
McCoy, R.D., Vimr, E.R. and Troy, F.A. CMP-NeuNAc:poly-α-2,8-sialosyl sialyltransferase and the biosynthesis of polysialosyl units in neural cell adhesion molecules. J. Biol. Chem. 260 (1985) 12695–12699. [PMID: 4044605] |
4. |
Yohe, H.C. and Yu, R.K. In vitro biosynthesis of an isomer of brain trisialoganglioside, GT1a. J. Biol. Chem. 255 (1980) 608–613. [PMID: 6766128] |
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[EC 2.4.3.8 created 1984 as EC 2.4.99.8, modified 1986, transferred 2022 to EC 2.4.3.8] |
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EC |
2.4.3.9 |
Accepted name: |
lactosylceramide α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetylneuraminate + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = CMP + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
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For diagram of ganglioside biosynthesis (pathway to GM2), click here |
Glossary: |
lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
Other name(s): |
cytidine monophosphoacetylneuraminate-lactosylceramide α2,3- sialyltransferase; CMP-acetylneuraminate-lactosylceramide-sialyltransferase; CMP-acetylneuraminic acid:lactosylceramide sialyltransferase; CMP-sialic acid:lactosylceramide-sialyltransferase; cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase; ganglioside GM3 synthetase; GM3 synthase; GM3 synthetase; SAT 1; CMP-N-acetylneuraminate:lactosylceramide α-2,3-N-acetylneuraminyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide α-(2→3)-N-acetylneuraminyltransferase |
Systematic name: |
CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide α-(2→3)-N-acetylneuraminyltransferase |
Comments: |
Lactose cannot act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-90-1 |
References: |
1. |
Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388–1394. [PMID: 4631392] |
2. |
Fishman, P.H., Bradley, R.M. and Henneberry, R.C. Butyrate-induced glycolipid biosynthesis in HeLa cells: properties of the induced sialyltransferase. Arch. Biochem. Biophys. 172 (1976) 618–626. [DOI] [PMID: 4022] |
3. |
Higashi, H., Basu, M. and Basu, S. Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J. Biol. Chem. 260 (1985) 824–828. [PMID: 3838172] |
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[EC 2.4.3.9 created 1984 as EC 2.4.99.9, modified 1986, transferred 2022 to EC 2.4.3.9] |
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EC |
2.4.3.10 |
Accepted name: |
N-acetylglucosaminide α-(2,6)-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-β-D-glucosaminyl-R |
Other name(s): |
α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylglucosaminide 6-α-sialyltransferase; N-acetylglucosaminide (α 2→6)-sialyltransferase; ST6GlcNAc |
Systematic name: |
CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminide N-acetyl-β-D-glucosamine-6-α-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetyl-β-D-glucosamine. The enzyme from rat liver also acts on β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl residues, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Paulson, J.C., Weinstein, J. and de Souza-e-Silva, U. Biosynthesis of a disialylated sequence in N-linked oligosaccharides: identification of an N-acetylglucosaminide (α 2→6)-sialyltransferase in Golgi apparatus from rat liver. Eur. J. Biochem. 140 (1984) 523–530. [PMID: 6547092] |
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[EC 2.4.3.10 created 2020 as EC 2.4.99.22, transferred 2022 to EC 2.4.3.10] |
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EC
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2.4.99.1
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Transferred entry: | β-galactoside α-(2,6)-sialyltransferase. Now EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase
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[EC 2.4.99.1 created 1972, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2017), deleted 2022] |
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EC
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2.4.99.2
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Transferred entry: | β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase. Now EC 2.4.3.2, β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
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[EC 2.4.99.2 created 1976, modified 1986, deleted 2022] |
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EC
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2.4.99.3
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Transferred entry: | α-N-acetylgalactosaminide α-2,6-sialyltransferase. Now EC 2.4.3.3, α-N-acetylgalactosaminide α-2,6-sialyltransferase
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[EC 2.4.99.3 created 1984, modified 1986, deleted 2022] |
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EC
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2.4.99.4
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Transferred entry: | β-galactoside α-2,3-sialyltransferase. Now EC 2.4.3.4, β-galactoside α-2,3-sialyltransferase
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[EC 2.4.99.4 created 1984, modified 1986, deleted 2022] |
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EC
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2.4.99.5
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Transferred entry: | galactosyldiacylglycerol α-2,3-sialyltransferase. Now EC 2.4.3.5, galactosyldiacylglycerol α-2,3-sialyltransferase
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[EC 2.4.99.5 created 1984, modified 1986, deleted 2022] |
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EC
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2.4.99.6
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Transferred entry: | N-acetyllactosaminide α-2,3-sialyltransferase. Now EC 2.4.3.6, N-acetyllactosaminide α-2,3-sialyltransferase
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[EC 2.4.99.6 created 1984, modified 1986 (EC 2.4.99.10 created 1986, incorporated 2017), deleted 2022] |
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EC
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2.4.99.7
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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
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[EC 2.4.99.7 created 1984, modified 1986, modified 2004, deleted 2022] |
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EC
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2.4.99.8
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Transferred entry: | α-N-acetylneuraminate α-2,8-sialyltransferase. Now EC 2.4.3.8, α-N-acetylneuraminate α-2,8-sialyltransferase
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[EC 2.4.99.8 created 1984, modified 1986, deleted 2022] |
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EC
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2.4.99.9
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Transferred entry: | lactosylceramide α-2,3-sialyltransferase. Now EC 2.4.3.9, lactosylceramide α-2,3-sialyltransferase
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[EC 2.4.99.9 created 1984, modified 1986, deleted 2022] |
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EC
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2.4.99.10
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Transferred entry: | neolactotetraosylceramide α-2,3-sialyltransferase. Now included in
EC 2.4.3.6, N-acetyllactosaminide α-2,3-sialyltransferase
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[EC 2.4.99.10 created 1986, deleted 2017] |
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EC
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2.4.99.11
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Deleted entry: | lactosylceramide α-2,6-N-sialyltransferase. Now included with EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase |
[EC 2.4.99.11 created 1992, deleted 2017] |
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EC |
2.4.99.12 |
Accepted name: |
lipid IVA 3-deoxy-D-manno-octulosonic acid transferase |
Reaction: |
CMP-β-Kdo + a lipid IVA + CMP-β-Kdo = CMP + an α-Kdo-(2→6)-[lipid IVA] |
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For diagram of Kdo4-Lipid IVA biosynthesis, click here |
Glossary: |
CMP-β-Kdo = CMP-3-deoxy-β-D-manno-octulosonate = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate
a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-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): |
waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; lipid IVA KDO transferase; CMP-3-deoxy-D-manno-oct-2-ulosonate:lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase; KDO transferase |
Systematic name: |
CMP-3-deoxy-β-D-manno-oct-2-ulosonate:[lipid IVA] 3-deoxy-D-manno-oct-2-ulosonate transferase (configuration-inverting) |
Comments: |
The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.13 [(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The monofunctional enzymes from Bordetella pertusis, 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 IVA [2-4]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. |
Isobe, T., White, K.A., Allen, A.G., Peacock, M., Raetz, C.R. and Maskell, D.J. Bordetella pertussis waaA encodes a monofunctional 2-keto-3-deoxy-D-manno-octulosonic acid transferase that can complement an Escherichia coli waaA mutation. J. Bacteriol. 181 (1999) 2648–2651. [DOI] [PMID: 10198035] |
3. |
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. [DOI] [PMID: 19546212] |
4. |
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. [DOI] [PMID: 9195966] |
5. |
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. [DOI] [PMID: 8748024] |
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[EC 2.4.99.12 created 2010, modified 2011] |
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EC |
2.4.99.13 |
Accepted name: |
(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase |
Reaction: |
CMP-β-Kdo + an α-Kdo-(2→6)-[lipid IVA] = CMP + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] |
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For diagram of Kdo4-Lipid IVA biosynthesis, click here |
Glossary: |
CMP-β-Kdo = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate
a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-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): |
waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase; CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase; Kdo transferase (ambiguous) |
Systematic name: |
CMP-3-deoxy-β-D-manno-oct-2-ulosonate:α-Kdo-(2→6)-[lipid IVA] 3-deoxy-D-manno-oct-2-ulosonate transferase (configuration-inverting) |
Comments: |
The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.12 [lipid IVA 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 [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [PMID: 8748024] |
3. |
Schmidt, H., Hansen, G., Singh, S., Hanuszkiewicz, A., Lindner, B., Fukase, K., Woodard, R.W., Holst, O., Hilgenfeld, R., Mamat, U. and Mesters, J.R. Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis. Proc. Natl. Acad. Sci. USA 109 (2012) 6253–6258. [DOI] [PMID: 22474366] |
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[EC 2.4.99.13 created 2010, modified 2011, modified 2021] |
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EC |
2.4.99.14 |
Accepted name: |
(Kdo)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase |
Reaction: |
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP-β-Kdo = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP |
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For diagram of Kdo4-Lipid IVA biosynthesis, click here |
Glossary: |
(Kdo)2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (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 IVA = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (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-β-Kdo = CMP-3-deoxy-β-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; (KDO)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase |
Systematic name: |
CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)2-lipid IVA 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, MetaCyc |
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. [DOI] [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. [DOI] [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] |
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[EC 2.4.99.14 created 2010, modified 2011] |
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EC |
2.4.99.15 |
Accepted name: |
(Kdo)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase |
Reaction: |
α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP-β-Kdo = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP |
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For diagram of Kdo4-Lipid IVA biosynthesis, click here |
Glossary: |
(Kdo)3-lipid IVA = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (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 IVA = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (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-β-Kdo = CMP-3-deoxy-β-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; (KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase |
Systematic name: |
CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)3-lipid IVA 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 IVA 3-deoxy-D-manno-octulosonic acid transferase], EC 2.4.99.13 [(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase], and EC 2.4.99.14 [(Kdo)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase]). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [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. [DOI] [PMID: 7744029] |
|
[EC 2.4.99.15 created 2010, modified 2011] |
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EC
|
2.4.99.22
|
Transferred entry: | N-acetylglucosaminide α-(2,6)-sialyltransferase. Now EC 2.4.3.10, N-acetylglucosaminide α-(2,6)-sialyltransferase
|
[EC 2.4.99.22 created 2020, deleted 2022] |
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|
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EC |
2.5.1.41 |
Accepted name: |
phosphoglycerol geranylgeranyltransferase |
Reaction: |
geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate |
|
For diagram of archaetidylserine biosynthesis, click here |
Glossary: |
sn-glycerol 1-phosphate = sn-glyceryl phosphate = (S)-2,3-dihydroxypropyl dihydrogen phosphate |
Other name(s): |
glycerol phosphate geranylgeranyltransferase; geranylgeranyl-transferase (ambiguous); prenyltransferase (ambiguous); (S)-3-O-geranylgeranylglyceryl phosphate synthase; (S)-geranylgeranylglyceryl phosphate synthase; GGGP synthase; (S)-GGGP synthase; GGGPS; geranylgeranyl diphosphate:sn-glyceryl phosphate geranylgeranyltransferase; geranylgeranyl diphosphate:sn-glycerol-1-phosphate geranylgeranyltransferase |
Systematic name: |
geranylgeranyl-diphosphate:sn-glycerol-1-phosphate geranylgeranyltransferase |
Comments: |
This cytosolic enzyme catalyses the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria [2]. Requires Mg2+ for maximal activity [2]. It catalyses the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase) and EC 2.7.7.67 (CDP-archaeol synthase), which lead to the formation of CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 124650-69-7 |
References: |
1. |
Zhang, D.-L., Daniels, L. and Poulter, C.D. Biosynthesis of archaebacterial membranes. Formation of isoprene ethers by a prenyl transfer reaction. J. Am. Chem. Soc. 112 (1990) 1264–1265. |
2. |
Chen, A., Zhang, D. and Poulter, C.D. (S)-Geranylgeranylglyceryl phosphate synthase. Purification and characterization of the first pathway-specific enzyme in archaebacterial membrane lipid biosynthesis. J. Biol. Chem. 268 (1993) 21701–21705. [PMID: 8408023] |
3. |
Nemoto, N., Oshima, T. and Yamagishi, A. Purification and characterization of geranylgeranylglyceryl phosphate synthase from a thermoacidophilic archaeon, Thermoplasma acidophilum. J. Biochem. 133 (2003) 651–657. [PMID: 12801917] |
4. |
Payandeh, J., Fujihashi, M., Gillon, W. and Pai, E.F. The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme. J. Biol. Chem. 281 (2006) 6070–6078. [DOI] [PMID: 16377641] |
5. |
Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [DOI] [PMID: 10960477] |
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[EC 2.5.1.41 created 1992, modified 2009] |
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EC |
2.5.1.42 |
Accepted name: |
geranylgeranylglycerol-phosphate geranylgeranyltransferase |
Reaction: |
geranylgeranyl diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate |
|
For diagram of archaetidylserine biosynthesis, click here |
Other name(s): |
geranylgeranyloxyglycerol phosphate geranylgeranyltransferase; geranylgeranyltransferase II; (S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; DGGGP synthase; DGGGPS; geranylgeranyl diphosphate:sn-3-O-(geranylgeranyl)glycerol 1-phosphate geranylgeranyltransferase |
Systematic name: |
geranylgeranyl-diphosphate:3-(O-geranylgeranyl)-sn-glycerol 1-phosphate geranylgeranyltransferase |
Comments: |
This enzyme is an integral-membrane protein that carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in Archaea. Requires a divalent metal cation, such as Mg2+ or Mn2+, for activity [2]. 4-Hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate and α-glycerophosphate cannot act as prenyl-acceptor substrates [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase), which, together with this enzyme, alkylates the hydroxy groups of glycerol 1-phosphate to yield unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 [CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase] to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [3]. Belongs in the UbiA prenyltransferase family [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 124650-68-6 |
References: |
1. |
Zhang, D.-L., Daniels, L. and Poulter, C.D. Biosynthesis of archaebacterial membranes. Formation of isoprene ethers by a prenyl transfer reaction. J. Am. Chem. Soc. 112 (1990) 1264–1265. |
2. |
Hemmi, H., Shibuya, K., Takahashi, Y., Nakayama, T. and Nishino, T. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids. J. Biol. Chem. 279 (2004) 50197–50203. [DOI] [PMID: 15356000] |
3. |
Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [DOI] [PMID: 10960477] |
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[EC 2.5.1.42 created 1992, modified 2009] |
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EC |
2.5.1.101 |
Accepted name: |
N,N′-diacetyllegionaminate synthase |
Reaction: |
2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose + phosphoenolpyruvate + H2O = N,N′-diacetyllegionaminate + phosphate |
|
For diagram of legionaminic acid biosynthesis, click here |
Glossary: |
legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate |
Other name(s): |
neuB (gene name); legI (gene name) |
Systematic name: |
phosphoenolpyruvate:2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose 1-(2-carboxy-2-oxoethyl)transferase |
Comments: |
Requires a divalent metal such as Mn2+. Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni, where it is involved in the biosynthesis of legionaminic acid, a virulence-associated, cell surface sialic acid-like derivative. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N′-diacetyllegionaminic acid from UDP-N,N′-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272–3282. [DOI] [PMID: 18275154] |
2. |
Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715–725. [DOI] [PMID: 19282391] |
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[EC 2.5.1.101 created 2012] |
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EC |
2.7.1.48 |
Accepted name: |
uridine/cytidine kinase |
Reaction: |
(1) ATP + uridine = ADP + UMP (2) ATP + cytidine = ADP + CMP |
Other name(s): |
UCK (gene name); URK1 (gene name); pyrimidine ribonucleoside kinase; uridine-cytidine kinase; uridine kinase (phosphorylating); uridine phosphokinase; ATP:uridine 5′-phosphotransferase; uridine kinase |
Systematic name: |
ATP:uridine/cytidine 5′-phosphotransferase |
Comments: |
The enzyme, found in prokaryotes and eukaryotes, phosphorylates both uridine and cytidine to their monophosphate forms. The enzyme from Escherichia coli prefers GTP to ATP. The human enzyme also catalyses the phosphorylation of several cytotoxic ribonucleoside analogs. cf. EC 2.7.1.213, cytidine kinase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-39-5 |
References: |
1. |
Sköld, O. Uridine kinase from Erlich ascites tumor: purification and properties. J. Biol. Chem. 235 (1960) 3273–3279. |
2. |
Orengo, A. Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor. J. Biol. Chem. 244 (1969) 2204–2209. [PMID: 5782006] |
3. |
Valentin-Hansen, P. Uridine-cytidine kinase from Escherichia coli. Methods Enzymol. 51 (1978) 308–314. [PMID: 211379] |
4. |
Kern, L. The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase. Nucleic Acids Res. 18:5279 (1990). [PMID: 2169608] |
5. |
Van Rompay, A.R., Norda, A., Linden, K., Johansson, M. and Karlsson, A. Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol. Pharmacol. 59 (2001) 1181–1186. [PMID: 11306702] |
6. |
Ohler, L., Niopek-Witz, S., Mainguet, S.E. and Mohlmann, T. Pyrimidine salvage: physiological functions and interaction with chloroplast biogenesis. Plant Physiol. 180 (2019) 1816–1828. [PMID: 31101721] |
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[EC 2.7.1.48 created 1965, modified 2020] |
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EC |
2.7.1.74 |
Accepted name: |
deoxycytidine kinase |
Reaction: |
NTP + deoxycytidine = NDP + dCMP |
Other name(s): |
deoxycytidine kinase (phosphorylating); 2′-deoxycytidine kinase; Ara-C kinase; arabinofuranosylcytosine kinase; deoxycytidine-cytidine kinase |
Systematic name: |
NTP:deoxycytidine 5′-phosphotransferase |
Comments: |
Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9039-45-6 |
References: |
1. |
Durham, J.P. and Ives, D.H. Deoxycytidine kinase. II. Purification and general properties of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2276–2284. [PMID: 5442271] |
2. |
Ives, D.H. and Durham, J.P. Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2285–2294. [PMID: 5462538] |
3. |
Kessel, D. Properties of deoxycytidine kinase partially purified from L1210 cells. J. Biol. Chem. 243 (1968) 4739–4744. [PMID: 5687717] |
4. |
Momparler, R.L. and Fischer, G.A. Mammalian deoxynucleoside kinase. I. Deoxycytidine kinase: purification, properties, and kinetic studies with cytosine arabinoside. J. Biol. Chem. 243 (1968) 4298–4304. [PMID: 5684726] |
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[EC 2.7.1.74 created 1972] |
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EC |
2.7.1.213 |
Accepted name: |
cytidine kinase |
Reaction: |
ATP + cytidine = ADP + CMP |
Systematic name: |
ATP:cytidine 5′-phosphotransferase |
Comments: |
The enzyme, characterized from the archaeon Thermococcus kodakarensis, participates in a pathway for nucleoside degradation. The enzyme can also act on deoxycytidine and uridine, but unlike EC 2.7.1.48, uridine kinase, it is most active with cytidine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Aono, R., Sato, T., Imanaka, T. and Atomi, H. A pentose bisphosphate pathway for nucleoside degradation in Archaea. Nat. Chem. Biol. 11 (2015) 355–360. [DOI] [PMID: 25822915] |
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[EC 2.7.1.213 created 2016] |
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EC |
2.7.4.14 |
Accepted name: |
UMP/CMP kinase |
Reaction: |
(1) ATP + (d)CMP = ADP + (d)CDP (2) ATP + UMP = ADP + UDP |
Other name(s): |
cytidylate kinase (misleading); deoxycytidylate kinase (misleading); CTP:CMP phosphotransferase (misleading); dCMP kinase (misleading); deoxycytidine monophosphokinase (misleading); UMP-CMP kinase; ATP:UMP-CMP phosphotransferase; pyrimidine nucleoside monophosphate kinase; uridine monophosphate-cytidine monophosphate phosphotransferase |
Systematic name: |
ATP:(d)CMP/UMP phosphotransferase |
Comments: |
This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, (d)CMP kinase and EC 2.7.4.22, UMP kinase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37278-21-0 |
References: |
1. |
Hurwitz, J. The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material. J. Biol. Chem. 234 (1959) 2351–2358. [PMID: 14405566] |
2. |
Ruffner, B.W., Jr. and Anderson, E.P. Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis. J. Biol. Chem. 244 (1969) 5994–6002. [PMID: 5350952] |
3. |
Scheffzek, K., Kliche, W., Wiesmuller, L. and Reinstein, J. Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5′-adenosyl) P5-(5′-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 Å: implications for water-mediated specificity. Biochemistry 35 (1996) 9716–9727. [DOI] [PMID: 8703943] |
4. |
Zhou, L., Lacroute, F. and Thornburg, R. Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase. Plant Physiol. 117 (1998) 245–254. [PMID: 9576794] |
5. |
Van Rompay, A.R., Johansson, M. and Karlsson, A. Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme. Mol. Pharmacol. 56 (1999) 562–569. [PMID: 10462544] |
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[EC 2.7.4.14 created 1961 as EC 2.7.4.5, transferred 1972 to EC 2.7.4.14, modified 1980, modified 2011] |
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EC |
2.7.4.19 |
Accepted name: |
5-methyldeoxycytidine-5′-phosphate kinase |
Reaction: |
ATP + 5-methyldeoxycytidine 5′-phosphate = ADP + 5-methyldeoxycytidine diphosphate |
Systematic name: |
ATP:5-methyldeoxycytidine-5′-phosphate phosphotransferase |
Comments: |
The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts m5dCMP into m5dCDP and then into m5dCTP. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81032-53-3 |
References: |
1. |
Wang, R.Y.-H., Huang, L.-H. and Ehrlich, M. A bacteriophage-induced 5-methyldeoxycytidine 5′-monophosphate kinase. Biochim. Biophys. Acta 696 (1982) 31–36. [DOI] [PMID: 7082669] |
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[EC 2.7.4.19 created 1984] |
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|
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EC |
2.7.4.22 |
Accepted name: |
UMP kinase |
Reaction: |
ATP + UMP = ADP + UDP |
Other name(s): |
uridylate kinase; UMPK; uridine monophosphate kinase; PyrH; UMP-kinase; SmbA |
Systematic name: |
ATP:UMP phosphotransferase |
Comments: |
This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9036-23-1 |
References: |
1. |
Serina, L., Blondin, C., Krin, E., Sismeiro, O., Danchin, A., Sakamoto, H., Gilles, A.M. and Bârzu, O. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a
hexamer regulated by guanine nucleotides and UTP. Biochemistry 34 (1995) 5066–5074. [PMID: 7711027] |
2. |
Marco-Marín, C., Gil-Ortiz, F. and Rubio, V. The crystal structure of Pyrococcus furiosus UMP kinase provides insight
into catalysis and regulation in microbial pyrimidine nucleotide
biosynthesis. J. Mol. Biol. 352 (2005) 438–454. [DOI] [PMID: 16095620] |
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[EC 2.7.4.22 created 2006] |
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EC |
2.7.4.25 |
Accepted name: |
(d)CMP kinase |
Reaction: |
ATP + (d)CMP = ADP + (d)CDP |
Glossary: |
CMP = cytidine monophosphate
dCMP = deoxycytidine monophosphate
CDP = cytidine diphosphate
dCDP = deoxycytidine diphosphate
UMP = uridine monophosphate
UDP = uridine diphosphate |
Other name(s): |
cmk (gene name); prokaryotic cytidylate kinase; deoxycytidylate kinase (misleading); dCMP kinase (misleading); deoxycytidine monophosphokinase (misleading) |
Systematic name: |
ATP:(d)CMP phosphotransferase |
Comments: |
The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Bertrand, T., Briozzo, P., Assairi, L., Ofiteru, A., Bucurenci, N., Munier-Lehmann, H., Golinelli-Pimpaneau, B., Barzu, O. and Gilles, A.M. Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. J. Mol. Biol. 315 (2002) 1099–1110. [DOI] [PMID: 11827479] |
2. |
Thum, C., Schneider, C.Z., Palma, M.S., Santos, D.S. and Basso, L.A. The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP. J. Bacteriol. 191 (2009) 2884–2887. [DOI] [PMID: 19181797] |
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[EC 2.7.4.25 created 2011] |
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EC
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2.7.7.21
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Transferred entry: | tRNA cytidylyltransferase. Now EC 2.7.7.72, CCA tRNA nucleotidyltransferase
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[EC 2.7.7.21 created 1965, deleted 2010] |
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EC
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2.7.7.25
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Transferred entry: | tRNA adenylyltransferase. Now EC 2.7.7.72, CCA tRNA nucleotidyltransferase
|
[EC 2.7.7.25 created 1965, deleted 2010] |
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|
|
EC |
2.7.7.38 |
Accepted name: |
3-deoxy-manno-octulosonate cytidylyltransferase |
Reaction: |
CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate |
Other name(s): |
CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase; 2-keto-3-deoxyoctonate cytidylyltransferase; 3-Deoxy-D-manno-octulosonate cytidylyltransferase; CMP-3-deoxy-D-manno-octulosonate synthetase; CMP-KDO synthetase; CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase; cytidine monophospho-3-deoxy-D-manno-octulosonate pyrophosphorylase |
Systematic name: |
CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-28-7 |
References: |
1. |
Ghalambor, M.A. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. IV. Purification and properties of cytidine monophosphate 3-deoxy-D-manno-octulosonate synthetase. J. Biol. Chem. 241 (1966) 3216–3221. [PMID: 5330266] |
|
[EC 2.7.7.38 created 1972] |
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|
|
|
EC |
2.7.7.43 |
Accepted name: |
N-acylneuraminate cytidylyltransferase |
Reaction: |
CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate |
|
For diagram of N-Acetylneuraminic acid biosynthesis, click here |
Other name(s): |
CMP-sialate pyrophosphorylase; CMP-sialate synthase; cytidine 5′-monophosphosialic acid synthetase; CMP-Neu5Ac synthetase; CMP-NeuAc synthetase; acylneuraminate cytidyltransferase; CMP-N-acetylneuraminate synthetase; CMP-N-acetylneuraminate synthase; CMP-N-acetylneuraminic acid synthase; CMP-NANA synthetase; CMP-sialate synthetase; CMP-sialic synthetase; cytidine 5′-monophospho-N-acetylneuraminic acid synthetase; cytidine 5-monophosphate N-acetylneuraminic acid synthetase; cytidine monophosphosialic acid synthetase; cytidine monophosphoacetylneuraminic synthetase; cytidine monophosphosialate pyrophosphorylase; cytidine monophosphosialate synthetase; acetylneuraminate cytidylyltransferase |
Systematic name: |
CTP:N-acylneuraminate cytidylyltransferase |
Comments: |
Acts on N-acetyl- and N-glycolyl- derivatives. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-82-7 |
References: |
1. |
Kean, E.L. and Roseman, S. The sialic acids. X. Purification and properties of cytidine 5′-monophosphosialic acid synthetase. J. Biol. Chem. 241 (1966) 5643–5650. [PMID: 4288894] |
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[EC 2.7.7.43 created 1972] |
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EC |
2.7.7.81 |
Accepted name: |
pseudaminic acid cytidylyltransferase |
Reaction: |
CTP + 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid = diphosphate + CMP-5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid
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Glossary: |
5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid = pseudaminic acid
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Other name(s): |
PseF |
Systematic name: |
CTP:5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-nonulosonic acid cytidylyltransferase |
Comments: |
Mg2+ is required for activity. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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] |
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[EC 2.7.7.81 created 2012] |
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