Enzymes
UniProtKB help_outline | 3 proteins |
Reaction participants Show >> << Hide
- Name help_outline a ganglioside GM4 (d18:1(4E)) Identifier CHEBI:78482 Charge -1 Formula C36H62N2O16R SMILEShelp_outline CCCCCCCCCCCCC\C=C\[C@@H](O)[C@H](CO[C@@H]1O[C@H](CO)[C@H](O)[C@H](O[C@@]2(C[C@H](O)[C@@H](NC(C)=O)[C@@H](O2)[C@H](O)[C@H](O)CO)C([O-])=O)[C@H]1O)NC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 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-neuraminosyl-(2→8)-N-acetyl-α-neuraminosyl-(2→3)-β-D-galactosyl-(1↔1ʼ)-N-acylsphing-4-enine Identifier CHEBI:90858 Charge -2 Formula C47H78N3O24R SMILEShelp_outline O([C@@H]1O[C@@H]([C@@H]([C@@H]([C@H]1O)O[C@]2(O[C@]([C@@H]([C@H](C2)O)NC(C)=O)([C@@H]([C@@H](CO)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)[H])C([O-])=O)O)CO)C[C@@H]([C@@H](/C=C/CCCCCCCCCCCCC)O)NC(=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 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:48924 | RHEA:48925 | RHEA:48926 | RHEA:48927 | |
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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
More general form(s) of this reaction
Publications
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Molecular cloning and expression of a sixth type of alpha 2,8-sialyltransferase (ST8Sia VI) that sialylates O-glycans.
Takashima S., Ishida H.K., Inazu T., Ando T., Ishida H., Kiso M., Tsuji S., Tsujimoto M.
A novel member of the mouse alpha2,8-sialyltransferase (ST8Sia) family, designated ST8Sia VI, was identified by BLAST analysis of expressed sequence tags. The sequence of ST8Sia VI encodes a protein of 398 amino acids and shows 42.0 and 38.3% amino acid sequence identities to mouse alpha2,8-sialyl ... >> More
A novel member of the mouse alpha2,8-sialyltransferase (ST8Sia) family, designated ST8Sia VI, was identified by BLAST analysis of expressed sequence tags. The sequence of ST8Sia VI encodes a protein of 398 amino acids and shows 42.0 and 38.3% amino acid sequence identities to mouse alpha2,8-sialyltransferases ST8Sia I (GD3 synthase) and ST8Sia V (GD1c, GT1a, GQ1b, and GT3 synthases), respectively. The recombinant soluble form of ST8Sia VI expressed in COS-7 cells exhibited alpha2,8-sialyltransferase activity toward both glycolipids and glycoproteins that have the NeuAcalpha2,3(6)Gal sequence at the nonreducing end of their carbohydrate groups. This enzyme formed NeuAcalpha2,8NeuAc structures, but not oligosialic or polysialic acid structures. Analysis of the fetuin sialylated by ST8Sia VI indicated that ST8Sia VI prefers O-glycans to N-glycans as acceptor substrates. Substrate specificities and kinetic properties also showed that ST8Sia VI prefers O-glycans to glycolipids as acceptor substrates. ST8Sia VI also exhibited activity toward oligosaccharides such as sialyllactose and sialyllactosamine, and the structure of the minimal acceptor substrate for ST8Sia VI was determined as the NeuAcalpha2,3(6)Gal sequence. The expression of the ST8Sia VI gene was ubiquitous, and the highest expression was observed in kidney, with three major transcripts of 8.2, 3.8, and 2.7 kb. This is the first report of a mammalian alpha2,8-sialyltransferase that sialylates O-glycans preferentially. << Less
J. Biol. Chem. 277:24030-24038(2002) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.