Enzymes
| UniProtKB help_outline | 18 proteins |
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Reaction participants Show >> << Hide
- Name help_outline a β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl derivative Identifier CHEBI:133507 Charge 0 Formula C14H24NO11R SMILEShelp_outline [C@@H]1([C@@H]([C@H]([C@H]([C@H](O1)CO)O)O)O)O[C@H]2[C@@H]([C@H]([C@@H](O[C@@H]2CO)O*)NC(=O)C)O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CMP-N-acetyl-β-neuraminate Identifier CHEBI:57812 (Beilstein: 5899715) help_outline Charge -2 Formula C20H29N4O16P InChIKeyhelp_outline TXCIAUNLDRJGJZ-BILDWYJOSA-L SMILEShelp_outline [H][C@]1(O[C@](C[C@H](O)[C@H]1NC(C)=O)(OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1ccc(N)nc1=O)C([O-])=O)[C@H](O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 84 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl derivative Identifier CHEBI:136545 Charge -1 Formula C25H40N2O19R SMILEShelp_outline O([C@@H]1[C@H]([C@H](O[C@@H]2[C@H](O[C@@H](O*)[C@@H]([C@H]2O)NC(C)=O)CO)O[C@@H]([C@@H]1O)CO)O)[C@]3(O[C@@]([C@@H]([C@H](C3)O)NC(C)=O)([H])[C@@H]([C@@H](CO)O)O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CMP Identifier CHEBI:60377 Charge -2 Formula C9H12N3O8P InChIKeyhelp_outline IERHLVCPSMICTF-XVFCMESISA-L SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 166 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:52316 | RHEA:52317 | RHEA:52318 | RHEA:52319 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
- RHEA:80755
- RHEA:65432
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RHEA:56264
N4-{β-D-Gal-(1→4)-β-D-GlcNAc-(1→2)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→2)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] + CMP-N-acetyl-β-neuraminate = N4-{β-D-Gal-(1→4)-β-D-GlcNAc-(1→2)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[α-Neu5Ac-(2→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→2)-[β-D-Gal-(1→4)-β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] + CMP + H+
Publications
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Synthesis of bisubstrate and donor analogues of sialyltransferase and their inhibitory activities.
Izumi M., Wada K., Yuasa H., Hashimoto H.
[reaction: see text] Sialyltransferases (STs) are involved in the biosynthesis of glycoconjugates with important biological activities. Most STs utilize cytidine-5'-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac) as a common donor substrate. A bisubstrate analogue containing the donor substrate ( ... >> More
[reaction: see text] Sialyltransferases (STs) are involved in the biosynthesis of glycoconjugates with important biological activities. Most STs utilize cytidine-5'-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac) as a common donor substrate. A bisubstrate analogue containing the donor substrate (CMP-Neu5Ac mimic) and the acceptor substrate (galactose) was synthesized. Four donor analogues having the partial structure of the bisubstrate analogue were also synthesized to support study of the structure-activity relationship. Each analogue contains an ethylene group in place of the exocyclic anomeric oxygen of CMP-Neu5Ac. The bisubstrate analogue exhibited only weak inhibitory activity to rat recombinant alpha-2,3- and alpha-2,6-ST (IC(50) = 1.3, 2.4 mM). Conversion of the C-1 carboxylate of the Neu5Ac moiety to carboxyamide, hydroxymethyl, or methylene phosphate each resulted in a reduction in inhibitory activity. Among the synthesized analogues, cytidin-5'-yl sialylethylphosphonate (4) was the most potent inhibitor against rat recombinant alpha-2,3- and alpha-2,6-ST (IC(50) = 0.047, 0.34 mM). << Less
J Org Chem 70:8817-8824(2005) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Biosynthesis in vitro of sialyl(alpha 2-3)neolactotetraosylceramide by a sialyltransferase from embryonic chicken brain.
Basu M., Basu S., Stoffyn A., Stoffyn P.
A sialyltransferase activity present in 7-to 12-day-old embryonic chicken brain catalyzes the transfer of sialic acid from CMP-sialic acid to the terminal galactose residue of [3H]nLcOse4Cer ([3H]Gal(beta 1-4).GlcNAc(beta 1-3)Gal(beta 1-4)Glc-Cer) to form NeuAc(alpha 2-3)-[3H]nLcOse4Cer (LM1 gangl ... >> More
A sialyltransferase activity present in 7-to 12-day-old embryonic chicken brain catalyzes the transfer of sialic acid from CMP-sialic acid to the terminal galactose residue of [3H]nLcOse4Cer ([3H]Gal(beta 1-4).GlcNAc(beta 1-3)Gal(beta 1-4)Glc-Cer) to form NeuAc(alpha 2-3)-[3H]nLcOse4Cer (LM1 ganglioside). The product is sialidase-labile (96%), and the NeuAc group is linked to O-3 of the terminal galactose residue. The (alpha 2-3) linkage between sialic acid and the terminal galactose was determined on the basis of identification of 2,4,6-tri-O-methyl[3H]galactose obtained after hydrolysis of the permethylated enzymatic product. The CMP-sialic acid:nLcOse4Cer (alpha 2-3)sialyltransferase activity sediments (90%) at the junction of 1.2 M and 1.5 M on a discontinuous sucrose density gradient when still membrane bound (insoluble in 0.2% Triton X-100). The enzyme preparation also catalyzes the transfer of sialic acid from CMP-sialic acid to O-3 of GgOse4Cer (Gal(beta 1-3)GalNAc(beta 1-4)Gal(beta 1-4)Glc-Cer) to form NeuAc (alpha 2-3)GgOse4Cer (GM1b). Substrate inhibition studies indicate that these two reactions are probably catalyzed by the same enzyme. << Less
J Biol Chem 257:12765-12769(1982) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Detection of beta-galactosyl(1 leads to 4)N-acetylglucosaminide alpha(2 leads to 3)-sialyltransferase activity in fetal calf liver and other tissues.
Van den Eijnden D.H., Schiphorst W.E.
Using a micromethodology based on methylation, the specificity of sialic acid transfer to asialo-alpha 1-acid [3H]-glycoprotein in various tissues was studied. CMP-N-acetylneuraminyl: beta-galactosyl(1 leads to 4)N-acetylglucosaminide alpha(2 leads to 3)-sialytransferase activity (an activity whic ... >> More
Using a micromethodology based on methylation, the specificity of sialic acid transfer to asialo-alpha 1-acid [3H]-glycoprotein in various tissues was studied. CMP-N-acetylneuraminyl: beta-galactosyl(1 leads to 4)N-acetylglucosaminide alpha(2 leads to 3)-sialytransferase activity (an activity which has not been demonstrated before) was detected in fetal calf liver, embryonic chicken brain, human placenta, and several other tissues. With the exception of the placenta all tissues investigated showed a considerable additional activity of CMP-N-acetylneuraminyl: beta-galactosyl(1 leads to 4)N-acetylglucosaminide alpha (2 leads to 6)-sialytransferase. Rat and porcine liver also contained the latter enzyme, but were essentially devoid of the alpha(2 leads to 3)-sialytransferase. Mixed enzyme experiments indicated that the alpha(2 leads to 3)-sialytransferase activity is due to a separate enzyme, which is clearly distinguishable from the CMP-N-acetylneuraminyl: beta-galactosyl(1 leads to 3)N-acetylgalactosaminide alpha(2 leads to 3)-sialytransferase of porcine liver and submaxillary gland. << Less
J Biol Chem 256:3159-3162(1981) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Mouse beta-galactoside alpha2,3-sialyltransferases: comparison of in vitro substrate specificities and tissue specific expression.
Kono M., Ohyama Y., Lee Y.-C., Hamamoto T., Kojima N., Tsuji S.
Four types of beta-galactoside alpha 2,3-sialyltransferase (ST3Gal I-IV) have been cloned from several animals, but some contradictory observations regarding their substrate specificities and expression have been reported. Therefore, it is necessary to concurrently analyze the substrate specificit ... >> More
Four types of beta-galactoside alpha 2,3-sialyltransferase (ST3Gal I-IV) have been cloned from several animals, but some contradictory observations regarding their substrate specificities and expression have been reported. Therefore, it is necessary to concurrently analyze the substrate specificities of the four enzymes, of which the source should be one animal. Accordingly, the acceptor substrate specificities and gene expression of mST3Gal I-IV were analyzed. Since we had already cloned ST3Gal I and II, as previously reported (Lee, Y.-C. et al., Eur. J. Biochem., 216, 377-385 (1993); J. Biol. Chem., 269, 10028-10033 (1994)), the cDNAs of ST3Gal III and IV were cloned from mouse cDNA libraries. Each of the four enzymes was expressed in COS-7 cells as a recombinant enzyme fused with protein A, and applied on an IgG-Sepharose gel to eliminate endogenous sialyltransferase activity. ST3Gal I and II showed the highest activity toward Gal beta 1, 3 GalNAc (type III), very low activity toward Gal beta 1,3GlcNAc (type I), but none toward Gal beta 1,4GlcNAc (type II). ST3Gal III and IV exhibited high activity toward the type I and II disaccharides, but very low activity toward the type III one. On the other hand, asialo-GM1 (Gg4Cer) was as good a substrate for ST3Gal I and II as the type III disaccharide, though ST3Gal III and IV hardly utilized glycolipids as substrates, as indicated by in vitro experiments. Northern blot analysis revealed that enzymes of the ST3Gal-family are expressed mainly in a tissue-specific manner. The ST3Gal I gene was strongly expressed in spleen and salivary gland, and weakly in brain, liver, heart, kidney, and thymus. The ST3Gal II gene was strongly expressed in brain, and weakly in colon, thymus, salivary gland, and testis, and developmentally expressed in liver, heart, kidney, and spleen. The ST3Gal III and IV genes were expressed in a wide variety of tissues. These differences in tissue specific expression suggest the expression of each ST3Gal influences the distribution of sialyl-glycoconjugates in vivo. << Less
Glycobiology 7:469-479(1997) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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A systematic analysis of acceptor specificity and reaction kinetics of five human alpha(2,3)sialyltransferases: Product inhibition studies illustrate reaction mechanism for ST3Gal-I.
Gupta R., Matta K.L., Neelamegham S.
Sialyltransferases (STs) catalyze the addition of sialic acids to the non-reducing ends of glycoproteins and glycolipids. In this work, we examined the acceptor specificity of five human α(2,3)sialyltransferases, namely ST3Gal -I, -II, -III, -IV and -VI. KM values for each of these enzymes is pres ... >> More
Sialyltransferases (STs) catalyze the addition of sialic acids to the non-reducing ends of glycoproteins and glycolipids. In this work, we examined the acceptor specificity of five human α(2,3)sialyltransferases, namely ST3Gal -I, -II, -III, -IV and -VI. KM values for each of these enzymes is presented using radioactivity for acceptors containing Type-I (Galβ1,3GlcNAc), Type-II (Galβ1,4GlcNAc), Type-III (Galβ1,3GalNAc) and Core-2 (Galβ1,3(GlcNAcβ1,6)GalNAc) reactive groups. Several variants of acceptors inhibited ST3Gal activity emphasizing structural role of acceptor in enzyme-catalyzed reactions. In some cases, mass spectrometry was performed for structural verification. The results demonstrate human ST3Gal-I catalysis towards Type-III and Core-2 acceptors with KM = 5-50 μM and high VMax values. The KM for ST3Gal-I and ST3Gal-II was 100 and 30-fold lower, respectively, for Type-III compared to Type-I acceptors. Variants of Type-I and Type-II structures characterized ST3Gal-III, -IV and -VI for their catalytic specificity. This manuscript also estimates KM for human ST3Gal-VI using Type-I and Type-II substrates. Together, these findings built a platform for designing inhibitors of STs having therapeutic potential. << Less
Biochem. Biophys. Res. Commun. 469:606-612(2016) [PubMed] [EuropePMC]