Reaction participants Show >> << Hide
- Name help_outline a ganglioside GD1b Identifier CHEBI:82939 Charge -2 Formula C52H82N4O39R2 SMILEShelp_outline CC(=O)N[C@@H]1[C@@H](O)C[C@@](O[C@H](CO)[C@@H](O)[C@@H]2O[C@@](C[C@H](O)[C@H]2NC(C)=O)(O[C@@H]2[C@@H](O)[C@H](O[C@H]3[C@H](O)[C@@H](O)[C@H](OC[C@H](NC([*])=O)[C@H](O)[*])O[C@@H]3CO)O[C@H](CO)[C@@H]2O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O[C@@H]3O[C@H](CO)[C@H](O)[C@H](O)[C@H]3O)[C@H]2NC(C)=O)C([O-])=O)(O[C@H]1[C@H](O)[C@H](O)CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 14 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 72 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ganglioside GT1b Identifier CHEBI:82940 Charge -3 Formula C63H98N5O47R2 SMILEShelp_outline CC(=O)N[C@@H]1[C@@H](O)C[C@@](O[C@H](CO)[C@@H](O)[C@@H]2O[C@@](C[C@H](O)[C@H]2NC(C)=O)(O[C@@H]2[C@@H](O)[C@H](O[C@H]3[C@H](O)[C@@H](O)[C@H](OC[C@H](NC([*])=O)[C@H](O)[*])O[C@@H]3CO)O[C@H](CO)[C@@H]2O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O[C@@H]3O[C@H](CO)[C@H](O)[C@H](O[C@@]4(C[C@H](O)[C@@H](NC(C)=O)[C@@H](O4)[C@H](O)[C@H](O)CO)C([O-])=O)[C@H]3O)[C@H]2NC(C)=O)C([O-])=O)(O[C@H]1[C@H](O)[C@H](O)CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 10 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 151 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:48240 | RHEA:48241 | RHEA:48242 | RHEA:48243 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase.
Lee Y.-C., Kojima N., Wada E., Kurosawa N., Nakaoka T., Hamamoto T., Tsuji S.
Based on the sequences of the highly conserved segments in the previously cloned sialyltransferases, a cDNA encoding a new type of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase (ST3GalA.2) has been isolated from both mouse and rat brain cDNA libraries. The cDNA sequences included an open reading ... >> More
Based on the sequences of the highly conserved segments in the previously cloned sialyltransferases, a cDNA encoding a new type of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase (ST3GalA.2) has been isolated from both mouse and rat brain cDNA libraries. The cDNA sequences included an open reading frame coding for 350 amino acids, and the primary structure of this enzyme suggested a putative domain structure consisting of four regions, like that in other glycosyltransferases. The deduced amino acid sequence of ST3GalA.2 (mouse) showed 76% identity in the active domain with that of the previously cloned mouse Gal beta 1,3GalNAc alpha 2,3-sialyltransferase (ST3GalA.1 (Lee, Y.-C., Kurosawa, N., Hamamoto, T., Nakaoka, T., and Tsuji, S. (1993) Eur. J. Biochem. 216, 377-385)). Northern blotting indicated that the expression of ST3GalA.2 mRNA is tissue-specific, it being prominent in brain and liver, while that in the other tissues is very low. This enzyme expressed in COS-7 cells exhibited transferase activity only toward the disaccharide moiety of Gal beta 1,3GalNAc of glycolipids as well as glycoproteins and oligosaccharides like ST3GalA.1, but showed a difference in acceptor substrate preference, i.e. asialo-GM1 and GM1 were much more suitable substrates for ST3GalA.2 than for ST3GalA.1. << Less
J. Biol. Chem. 269:10028-10033(1994) [PubMed] [EuropePMC]
This publication is cited by 3 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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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.