Enzymes
| UniProtKB help_outline | 3 proteins |
Reaction participants Show >> << Hide
- Name help_outline a globoside GalGb4Cer Identifier CHEBI:140691 Charge 0 Formula C36H60N2O28R2 SMILEShelp_outline CC(=O)N[C@H]1[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@H](O[C@@H]3[C@H](O)[C@@H](O)[C@H](O[C@H]4[C@H](O)[C@@H](O)[C@H](OC[C@H](NC([*])=O)[C@H](O)[*])O[C@@H]4CO)O[C@@H]3CO)[C@@H]2O)O[C@H](CO)[C@H](O)[C@@H]1O[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-N-acetyl-α-D-glucosamine Identifier CHEBI:57705 (Beilstein: 4286654) help_outline Charge -2 Formula C17H25N3O17P2 InChIKeyhelp_outline LFTYTUAZOPRMMI-CFRASDGPSA-L SMILEShelp_outline CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 93 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a globoside GlcNAc-(β1→6)-GalGb4Cer Identifier CHEBI:140702 Charge 0 Formula C44H73N3O33R2 SMILEShelp_outline [C@H]([C@@H](*)O)(NC(=O)*)CO[C@@H]1O[C@@H]([C@@H](O[C@@H]2O[C@@H]([C@H](O[C@@H]3[C@@H]([C@@H](O[C@H]4[C@@H]([C@H]([C@@H](O)[C@H](O4)CO[C@H]5[C@@H]([C@H]([C@H](O)[C@H](O5)CO)O)NC(C)=O)O[C@@H]6O[C@@H]([C@H](O)[C@@H]([C@H]6O)O)CO)NC(C)=O)[C@H]([C@H](O3)CO)O)O)[C@@H]([C@H]2O)O)CO)[C@@H]([C@H]1O)O)CO 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 UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 637 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 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56900 | RHEA:56901 | RHEA:56902 | RHEA:56903 | |
|---|---|---|---|---|
| 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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The expression of IV6 beta[Gal beta 1-4(Fuc alpha 1-3)GlcNAc]-Gb5Cer in mouse kidney is controlled by the Gsl-5 gene through regulation of UDP-GlcNAc:Gb5Cer beta 1-6N-acetylglucosaminyltransferase activity.
Sekine M., Hashimoto Y., Inagaki F., Yamakawa T., Suzuki A.
We reported the polymorphic expression of GL-Y (IV6 beta[Gal beta 1-4(Fuc alpha 1-3)GlcNAc]-Gb5Cer in kidneys of inbred strains of mice in previous papers [J. Biochem. 101, 553-562 and 563-568 (1987)]. DBA/2 mice express a large amount of GL-X (Gb5Cer), but not GL-Y, in their kidneys, because of a ... >> More
We reported the polymorphic expression of GL-Y (IV6 beta[Gal beta 1-4(Fuc alpha 1-3)GlcNAc]-Gb5Cer in kidneys of inbred strains of mice in previous papers [J. Biochem. 101, 553-562 and 563-568 (1987)]. DBA/2 mice express a large amount of GL-X (Gb5Cer), but not GL-Y, in their kidneys, because of a defect on a single autosomal gene (Gsl-5). This suggested that DBA/2 mice lack the ability to transfer GlcNAc onto the C-6 position of GalNAc of Gb5Cer or GL-X. In this study, we characterized UDP-GlcNAc:GL-X beta 1-6N-acetylglucosaminyltransferase (beta 1-6GlcNAc transferase) in the microsomal fraction of mouse kidney. Maximum activity was detected with an incubation mixture containing sodium cacodylate buffer (pH 6.4), 0.1% Zwittergent 3-16 and 1 mM EDTA. Divalent cations were not required. The apparent Km values for UDP-GlcNAc and GL-X were 0.42 and 0.12 mM, respectively. The product of the enzymatic reaction was identified as IV6 beta GlcNAc-Gb5Cer by means of 1H-NMR spectroscopy and permethylation analyses. Then, we measured the beta 1-6GlcNAc transferase activity in the microsomal fractions of kidneys of inbred strains of mice and progeny obtained on mating. WHT/Ht, C57BL/10, BALB/c, and C3H/He mice, which express GL-Y in their kidneys, exhibited detectable amounts of activity, whereas CBA and DBA/2 mice, which do not express GL-Y, did not exhibit detectable activity.(ABSTRACT TRUNCATED AT 250 WORDS) << Less
J Biochem 108:103-108(1990) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Purification and characterization of UDP-GlcNAc:IV3 beta Gal-Gb4Cer beta-1,6-GlcNAc transferase from mouse kidney.
Sekine M., Hashimoto Y., Suzuki M., Inagaki F., Takio K., Suzuki A.
The Gsl-5 gene mapped on mouse chromosome 19 controls the expression of IV6 beta Gal beta 1-4(Fuc alpha 1-3)GlcNAc, IV3 beta Gal-Gb4Cer in mouse kidney through regulation of the activity of UDP-GlcNAc:IV3 beta Gal-Gb4Cer beta-1,6-Glc-NAc transferase (GNT), which transfers GlcNAc to the C-6 positio ... >> More
The Gsl-5 gene mapped on mouse chromosome 19 controls the expression of IV6 beta Gal beta 1-4(Fuc alpha 1-3)GlcNAc, IV3 beta Gal-Gb4Cer in mouse kidney through regulation of the activity of UDP-GlcNAc:IV3 beta Gal-Gb4Cer beta-1,6-Glc-NAc transferase (GNT), which transfers GlcNAc to the C-6 position of GalNAc of IV3 beta Gal-Gb4Cer (GL-X). Here we report that GNT has been purified to apparent homogeneity from mouse kidney by means of preparation of a microsomal fraction, solubilization with Triton X-100, and sequential column chromatographies on CM-Sepharose, UDP-hexanolamine-Sepharose, and Gg4Ose-Aminocellulo-fine. GNT purified 11,000-fold from the microsomal fraction exhibited a specific activity of 26.15 mumol/min/mg protein and an apparent molecular mass of 50 kDa on SDS-polyacrylamide gel electrophoresis. The Km values for UDP-GlcNAc and GL-X were 0.36 and 0.11 mM, respectively. Among glycolipids tested as substrates, GL-X was the best and Gg4Cer the next best, but Lc3Cer, Gb4Cer, and GM1 did not act as a substrate. GNT was also able to transfer GlcNAc to Gal beta 1-3GalNAc beta 1-benzyl and Gal beta 1-3GalNAc alpha 1-p-nitrophenyl at C-6 of GalNAc through beta linkage but not to GlcNAc beta-3GalNAc alpha 1-p-nitrophenyl. The purified GNT was digested with lysyl endopeptidase, and four peptides generated were sequenced. The sequence of four peptides spanning 35 amino acid residues in total exhibited 80% homology with that of the reported human core 2 GlcNAc transferase. << Less
J. Biol. Chem. 269:31143-31148(1994) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.