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- Name help_outline a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl derivative Identifier CHEBI:136588 Charge 0 Formula C14H24NO11R SMILEShelp_outline O([C@H]1[C@@H]([C@H]([C@H]([C@H](O1)CO)O)O[C@H]2[C@@H]([C@H]([C@H]([C@H](O2)CO)O)O)O)NC(C)=O)* 2D coordinates Mol file for the small molecule Search links Involved in 1 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 81 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→3)-N-acetyl-β-D-galactosaminyl derivative Identifier CHEBI:136589 Charge -1 Formula C25H40N2O19R SMILEShelp_outline O([C@H]1[C@@H]([C@H]([C@@H](O)[C@H](O1)CO)O[C@@H]2O[C@@H]([C@@H]([C@@H]([C@H]2O)O[C@]3(O[C@]([C@@H]([C@H](C3)O)NC(C)=O)([C@@H]([C@@H](CO)O)O)[H])C([O-])=O)O)CO)NC(C)=O)* 2D coordinates Mol file for the small molecule Search links Involved in 3 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 164 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:52380 | RHEA:52381 | RHEA:52382 | RHEA:52383 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Enzymatic characterization of beta D-galactoside alpha2 leads to 3 sialyltransferase from porcine submaxillary gland.
Rearick J.I., Sadler J.E., Paulson J.C., Hill R.L.
The substrate requirements, linkage specificity, and kinetic mechanism of a pure sialyltransferase from porcine submaxillary glands have been examined. The enzyme transfers sialic acid from the donor nucleotide, CMP-NeuAc, into the sequence NeuAcalpha2 leads to 3Galbeta1 leads to 3GalNAc, which is ... >> More
The substrate requirements, linkage specificity, and kinetic mechanism of a pure sialyltransferase from porcine submaxillary glands have been examined. The enzyme transfers sialic acid from the donor nucleotide, CMP-NeuAc, into the sequence NeuAcalpha2 leads to 3Galbeta1 leads to 3GalNAc, which is found in both glycoproteins and gangliosides. It forms only the alpha2 leads to 3 linkage with the disaccharide Gal/beta1 leads to 3GalNAc or antifreeze glycoprotein, which, along with asialoglycoproteins containing the sequence Gal/beta1 leads to 3GalNAcalpha1 leads to O-Thr/Ser, are the best acceptor substrates. Low molecular weight galactosides linked beta1 leads to 3 to glycose residues other than N-acetylgalactosamine are poor acceptors with relatively high Km values, while those in beta1 leads to 4 or beta1 leads to 6 linkages have both high Km and low Vmax. With glycoprotein and ganglioside acceptors this substrate specificity appears to be even more strict, with the sequence Gal/beta1 leads to 3GalNAc serving as the exclusive acceptor. Thus the present enzyme is not responsible either for the sequence, NeuAcalpha2 leads to 3Galbeta1 leads to 4GlcNAc, found in the asparagine-linked chains of certain glycoproteins, or for the synthesis of hematoside, NeuAcalpha2 leads to 3Galbeta1 leads to 4Glcbeta1 leads to 1Cer. Initial rate kinetic studies, with and without inhibitors, suggest that the transferase has an equilibrium random order mechanism. << Less
J Biol Chem 254:4444-4451(1979) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Kinetic properties and acceptor substrate preferences of two kinds of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase from mouse brain.
Kojima N., Lee Y.C., Hamamoto T., Kurosawa N., Tsuji S.
The cDNAs encoding two kinds of Gal beta 1,3GalNAc alpha 2,3-sialytransferases (ST3GalA.1 and ST3GalA.2) have been cloned from mouse brain, both of which could synthesize the NeuAc alpha 2,3Gal beta 1,-3GalNAc sequence of gangliosides as well as O-glycosidically linked oligosaccharides of glycopro ... >> More
The cDNAs encoding two kinds of Gal beta 1,3GalNAc alpha 2,3-sialytransferases (ST3GalA.1 and ST3GalA.2) have been cloned from mouse brain, both of which could synthesize the NeuAc alpha 2,3Gal beta 1,-3GalNAc sequence of gangliosides as well as O-glycosidically linked oligosaccharides of glycoproteins [Lee et al. (1993) Eur. J. Biochem. 216, 377-385; Lee et al. (1994) J. Biol. Chem. (in press)]. Kinetic analysis of the two sialyltransferases using Gal beta 1,3GalNAc, asialoGM1, or asialofetuin revealed that ST3GalA.1 exhibits the highest Km value for asialoGM1 (Km = 1.25 mM) and the lowest one for asialofetuin (Km = 0.10 mM), whereas the Km values of ST3GalA.2 for the substrates are very similar (Km approximately 0.5 mM). The synthesis of GM1b from asialoGM1 by ST3GalA.1 was clearly inhibited in the presence of Gal beta 1,3GalNAc or asialofetuin, but that by ST3GalA.2 was not at all. On the other hand, the activity of ST3GalA.2 toward Gal beta 1,3GalNAc or asialofetuin was inhibited by asialoGM1 or GM1. The results of acceptor competition experiments involving asialoGM1, Gal beta 1,3GalNAc, and asialofetuin indicated that ST3GalA.2 exhibits noncompetitive inhibition between asialoGM1 and Gal beta 1,3GalNAc or between asialoGM1 and asialofetuin, whereas ST3GalA.1 exhibits competitive inhibition between all kinds of acceptors. These results strongly indicate that acceptor preference of ST3GalA.1 is different from that of ST3GalA.2, although their acceptor substrate specificities are the same; i.e., gangliosides serve as predominant acceptors for the latter over O-glycosidically linked oligosaccharides of glycoproteins, which are much better acceptors for the former. << Less
Biochemistry 33:5772-5776(1994) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Molecular cloning and expression of human Gal beta 1,3GalNAc alpha 2,3-sialyltransferase (hST3Gal II).
Kim Y.-J., Kim K.-S., Kim S.-H., Kim C.-H., Ko J.H., Choe I.-S., Tsuji S., Lee Y.-C.
A cDNA of human Gal beta 1,3GalNAc alpha 2,3-sialytransferase (hST3Gal II) which has been known to exhibit much more acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins, was isolated from the human liver cDNA library by plaque hybridization using the cD ... >> More
A cDNA of human Gal beta 1,3GalNAc alpha 2,3-sialytransferase (hST3Gal II) which has been known to exhibit much more acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins, was isolated from the human liver cDNA library by plaque hybridization using the cDNA of mouse ST3Gal II (mST3Gal II) cloned previously as a probe. Comparative analysis of this cDNA with mST3Gal II indicates 89 and 94% homologies in the nucleotide and amino acid levels, respectively, between the two sequences in the predicted coding region. Northern analysis indicated that the expression of hST3Gal II mRNA is tissue-specific, it being prominent in skeletal muscle and heart, while that in lung and kidney is very low. This enzyme expressed in COS cells showed a similar activity with that of mST3Gal II. << Less
Biochem. Biophys. Res. Commun. 228:324-327(1996) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups.
Kitagawa H., Paulson J.C.
Sialyltransferases are a family of 10-12 enzymes that catalyze the transfer of sialic acid to carbohydrate groups of glycoproteins and glycolipids. Three sialyltransferase cDNAs have been cloned, revealing a highly conserved sialylmotif in the catalytic domain of these enzymes. Using a polymerase ... >> More
Sialyltransferases are a family of 10-12 enzymes that catalyze the transfer of sialic acid to carbohydrate groups of glycoproteins and glycolipids. Three sialyltransferase cDNAs have been cloned, revealing a highly conserved sialylmotif in the catalytic domain of these enzymes. Using a polymerase chain reaction-based approach, we cloned a 150-base pair fragment of a new sialymotif from human placenta mRNA, which was then used as a probe to clone the complete coding sequence of the corresponding gene from a cDNA library. Like the other members of the sialyltransferase gene family cloned to date, the new cDNA coded for a protein predicted to have an NH2-terminal signal-anchor sequence and had the sialylmotif located in the center of the molecule. Comparison with the three other cloned sialyltransferases revealed extensive sequence homology that was not recognized earlier. Expression of a soluble recombinant form of the protein in COS-1 cells produced an active sialyltransferase, which used oligosaccharide, glycoprotein, and glycolipid acceptor substrates with terminal galactose in the Gal beta 1,3GalNAc and Gal beta 1, 4GlcNAc sequences but not the Gal beta 1,3GlcNAc sequence. The sialylated products were sensitive to digestion with the Newcastle disease virus sialidase, which is specific for sialic acid-galactose linkages in the alpha 2,3 linkage. The results suggest that this new member of the sialyltransferase gene family is the enzyme previously described as a glycolipid sialyltransferase activity (SAT-3), which forms the terminal sequences NeuAc alpha-2,3Gal beta 1,3GalNAc-R and NeuAc alpha 2,3Gal beta 1, 4GlcNAc-R. << Less
J. Biol. Chem. 269:1394-1401(1994) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Cloning and expression of cDNA for a human Gal(beta1-3)GalNAc alpha2,3-sialyltransferase from the CEM T-cell line.
Giordanengo V., Lefebvre J.-C.
Complementary DNA encoding a human Gal(beta1-3)GalNAc alpha2,3-sialyltransferase type II (hST3Gal II) was cloned from a CEM T-cell cDNA library using a 23-base oligonucleotide probe. The sequence of this probe was established on the basis of a slightly divergent sialylmotif L that was obtained by ... >> More
Complementary DNA encoding a human Gal(beta1-3)GalNAc alpha2,3-sialyltransferase type II (hST3Gal II) was cloned from a CEM T-cell cDNA library using a 23-base oligonucleotide probe. The sequence of this probe was established on the basis of a slightly divergent sialylmotif L that was obtained by polymerase chain reaction with degenerate oligonucleotide primers based on the conserved sialylmotif L of mammalian Gal(beta1-3)GalNAc alpha2,3-sialyltransferases. It was thus confirmed that a short oligonucleotide probe may be sensitive and highly specific. The nucleotide and amino acid sequences of hST3Gal II show, respectively, 56.3% and 49.3% similarity to hST3Gal I [Kitagawa, H. & Paulson, J. C. (1994) J. Biol. Chem. 269, 17872-17878] and 88.1% and 93.7% similarity to murine ST3Gal II [Lee, Y. C., Kojima, N., Wada, E., Kurosawa, N., Nakaoka, T., Hamamoto, T. & Tsuji, S. (1994) J. Biol. Chem. 269, 10028-10033]. hST3Gal II mRNA was highly expressed in heart, liver, skeletal muscle and various lymphoid tissues but not in brain and kidney. A soluble form of hST3Gal II expressed in COS-7 cells was tested in vitro for substrate specificity and kinetic properties. Asialofetuin and asialo-bovine submaxillary mucin appeared better substrates for hST3Gal II than for its murine counterpart as previously reported [Kojima, N., Lee, Y.-C., Hamamoto, T., Kurosawa, N. & Tsuji, S. (1994) Biochemistry 33, 5772-5776]. In previous studies, we have shown hyposialylation of O-glycans attached to two major lymphocyte CD43 and CD45 cell surface molecules in human-immunodeficiency-virus-1(HIV-1)-infected T-cell lines. Since comparable levels of hST3Gal I and hST3Gal II mRNA and enzymatic activity were observed in parental and HIV-1-infected CEM T-cell lysates, the sialylation defect associated with HIV infection of this cell line is probably due to a mechanism different from a simple altered catalytic activity of these sialyltransferases. << Less
Eur. J. Biochem. 247:558-566(1997) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.
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The enzymic synthesis of disialoganglioside: rat brain cytidine-5'-monophospho-N-acetylneuraminic acid: monosialoganglioside (G M1 ) sialyltransferase.
Yip M.C.
Biochim Biophys Acta 306:298-306(1973) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Molecular cloning and expression of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase from mouse brain.
Lee Y.-C., Kurosawa N., Hamamoto T., Nakaoka T., Tsuji S.
DNA clones encoding beta-galactoside alpha 2,3-sialyltransferase have been isolated from mouse brain cDNA libraries using sequence information obtained from the conserved amino acid sequence of the previously cloned enzymes. The cDNA sequence revealed an open reading frame coding for 337 amino aci ... >> More
DNA clones encoding beta-galactoside alpha 2,3-sialyltransferase have been isolated from mouse brain cDNA libraries using sequence information obtained from the conserved amino acid sequence of the previously cloned enzymes. The cDNA sequence revealed an open reading frame coding for 337 amino acids, and the deduced amino acid sequence showed 80% identity with that of porcine submaxillary gland Gal beta 1,3GalNAc alpha 2,3-sialyltransferase. The primary structure of this enzyme suggested a putative domain structure, like that in other glycosyltransferases, consisting of a short NH2-terminal cytoplasmic domain, a signal-membrane anchor domain, a proteolytically sensitive stem region, and a large COOH-terminal active domain. The identity of this enzyme was confirmed by construction of a recombinant sialyltransferase in which the NH2-terminal part including the cytoplasmic tail, signal-anchor domain and stem region was replaced with an immuno-globulin signal sequence. The expression of this recombinant in COS-7 cells resulted in secretion of a catalytically active and soluble form of the enzyme into the medium. This enzyme exhibited the transferase activity toward only the disaccharide moiety of Gal beta 1,3GalNAc of glycoproteins and glycolipids, no significant activity being detected for the other substrates tested. << Less
Eur. J. Biochem. 216:377-385(1993) [PubMed] [EuropePMC]
This publication is cited by 7 other entries.