Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline N-acetyl-α-neuraminosyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-D-galactosamine Identifier CHEBI:156406 Charge -1 Formula C25H41N2O19 InChIKeyhelp_outline KMRCGPSUZRGVOV-RYGDDSFPSA-M SMILEShelp_outline OC1[C@@H]([C@H]([C@@H](O)[C@H](O1)CO)O[C@H]2[C@@H]([C@@H](O[C@]3(O[C@]([C@@H]([C@H](C3)O)NC(C)=O)([C@@H]([C@H](O)CO)O)[H])C([O-])=O)[C@H]([C@H](O2)CO)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 84 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acetyl-α-neuraminosyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminosyl-(2→6)]-N-acetyl-D-galactosamine Identifier CHEBI:156407 Charge -2 Formula C36H57N3O27 InChIKeyhelp_outline QDVVSMLRZUPDCM-NQXGSQGUSA-L SMILEShelp_outline OC1[C@@H]([C@H]([C@@H](O)[C@H](O1)CO[C@]2(O[C@]([C@@H]([C@H](C2)O)NC(C)=O)([C@@H]([C@H](O)CO)O)[H])C([O-])=O)O[C@H]3[C@@H]([C@@H](O[C@]4(O[C@]([C@@H]([C@H](C4)O)NC(C)=O)([C@@H]([C@H](O)CO)O)[H])C([O-])=O)[C@H]([C@H](O3)CO)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 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:65288 | RHEA:65289 | RHEA:65290 | RHEA:65291 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Molecular cloning and functional expression of two members of mouse NeuAc-alpha-2,3Gal-beta-1,3GalNAc GalNAc-alpha2,6-sialyltransferase family, ST6GalNAc III and IV.
Lee Y.-C., Kaufman M., Kitazume-Kawaguchi S., Kono M., Takashima S., Kurosawa N., Liu H., Pircher H., Tsuji S.
Two cDNA clones encoding NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2, 6-sialyltransferase have been isolated from mouse brain cDNA libraries. One of the cDNA clones is a homologue of previously reported rat ST6GalNAc III according to the amino acid sequence identity (94.4%) and the substrate specif ... >> More
Two cDNA clones encoding NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2, 6-sialyltransferase have been isolated from mouse brain cDNA libraries. One of the cDNA clones is a homologue of previously reported rat ST6GalNAc III according to the amino acid sequence identity (94.4%) and the substrate specificity of the expressed recombinant enzyme, while the other cDNA clone includes an open reading frame coding for 302 amino acids. The deduced amino acid sequence is not identical to those of other cloned mouse sialyltransferases, although it shows the highest sequence similarity with mouse ST6GalNAc III (43.0%). The expressed soluble recombinant enzyme exhibited activity toward NeuAcalpha2, 3Galbeta1, 3GalNAc, fetuin, and GM1b, while no significant activity was detected toward Galbeta1,3GalNAc or asialofetuin, or the other glycoprotein substrates tested. The sialidase sensitivity of the 14C-sialylated residue of fetuin, which was sialylated by this enzyme with CMP-[14C]NeuAc, was the same as that of ST6GalNAc III. These results indicate that the expressed enzyme is a new type of GalNAcalpha2,6-sialyltransferase, which requires sialic acid residues linked to Galbeta1,3GalNAc residues for its activity; therefore, we designated it mouse ST6GalNAc IV. Although the substrate specificity of this enzyme is similar to that of ST6GalNAc III, ST6GalNAc IV prefers O-glycans to glycolipids. Glycolipids, however, are better substrates for ST6GalNAc III. << Less
J. Biol. Chem. 274:11958-11967(1999) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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A novel glycosyltransferase with a polyglutamine repeat; a new candidate for GD1alpha synthase (ST6GalNAc V).
Ikehara Y., Shimizu N., Kono M., Nishihara S., Nakanishi H., Kitamura T., Narimatsu H., Tsuji S., Tatematsu M.
The fifth type GalNAcalpha2,6-sialyltransferase (mST6GalNAc V) was cloned from a mouse brain cDNA library. mST6GalNAc V exhibited type II transmembrane topology containing a polyglutamine repeat, which showed 42.6% and 44.8% identity to mouse ST6GalNAc III and IV, respectively. Northern blot analy ... >> More
The fifth type GalNAcalpha2,6-sialyltransferase (mST6GalNAc V) was cloned from a mouse brain cDNA library. mST6GalNAc V exhibited type II transmembrane topology containing a polyglutamine repeat, which showed 42.6% and 44.8% identity to mouse ST6GalNAc III and IV, respectively. Northern blot analysis revealed that the mST6GalNAc V gene was specifically expressed in forebrain and cerebellum. mST6GalNAc V exhibited GD1alpha synthetic activity from GM1b the same as mST6GalNAc III and IV. The activity ratio of GM1b toward fetuin and the expression pattern were completely different among the three ST6GalNAcs. Interestingly, the polyglutamine repeat number was different from that of inbred mice. We report the first glycosyltransferase with a polymorphic polyglutamine repeat. << Less
FEBS Lett. 463:92-96(1999) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.