Enzymes
| UniProtKB help_outline | 3 proteins |
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- Name help_outline N-acetyl-α-neuraminosyl-(2→3)-β-D-galactosyl-(1↔1ʼ)-ceramide Identifier CHEBI:82643 Charge -1 Formula C21H33N2O16R2 SMILEShelp_outline [H][C@]1(O[C@@](C[C@H](O)[C@H]1NC(C)=O)(O[C@H]1[C@@H](O)[C@@H](CO)O[C@@H](OC[C@H](NC([*])=O)[C@H](O)[*])[C@@H]1O)C([O-])=O)[C@H](O)[C@H](O)CO 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-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→8)-N-acetyl-α-neuraminosyl-(2→3)-β-D-galactosyl-(1↔1ʼ)-ceramide Identifier CHEBI:90859 Charge -2 Formula C32H49N3O24R2 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](*)O)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 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:48928 | RHEA:48929 | RHEA:48930 | RHEA:48931 | |
|---|---|---|---|---|
| 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 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.
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Molecular cloning and expression of human alpha2,8-sialyltransferase (hST8Sia V).
Kim Y.-J., Kim K.-S., Do S.-I., Kim C.-H., Kim S.-K., Lee Y.-C.
The cDNA encoding human alpha2,8-sialyltransferase (hST8Sia V) which exhibits activity toward gangliosides, GM1b, GD1a, GT1b, and GD3, was isolated by screening of human brain cDNA library with a DNA probe generated from the cDNA sequence of mouse ST8Sia V (mST8Sia V) and by 5'-RACE of mRNA from h ... >> More
The cDNA encoding human alpha2,8-sialyltransferase (hST8Sia V) which exhibits activity toward gangliosides, GM1b, GD1a, GT1b, and GD3, was isolated by screening of human brain cDNA library with a DNA probe generated from the cDNA sequence of mouse ST8Sia V (mST8Sia V) and by 5'-RACE of mRNA from human brain tissue. Comparative analysis of this cDNA with mST8Sia V showed that each sequence of the predicted coding region contains 84% identity in both nucleotide and amino acid. Northern analysis of this cDNA indicated that, in contrast to mST8Sia V, two different sizes of transcripts corresponding to 11 and 2.5 kb were expressed in both human fetal and adult brain, while the transcript of 2.5 kb was detected only in adult heart and skeletal muscle. The enzyme expressed in COS cells showed a substrate specificity very similar to that of mST8Sia V. << Less
Biochem. Biophys. Res. Commun. 235:327-330(1997) [PubMed] [EuropePMC]
This publication is cited by 7 other entries.