Enzymes
| UniProtKB help_outline | 1,195 proteins |
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Namehelp_outline
an N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein]
Identifier
RHEA-COMP:14369
Reactive part
help_outline
- Name help_outline an N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-Asn residue Identifier CHEBI:60615 Charge 0 Formula C46H75N5O32 SMILEShelp_outline [C@@H]1([C@@H]([C@H]([C@@H]([C@H](O1)CO)O)O)NC(C)=O)O[C@@H]2[C@H](O[C@@H]([C@H]([C@@H]2O)O)CO)O[C@@H]3[C@@H]([C@@H](O[C@@H]([C@H]3O)CO[C@@H]4[C@H]([C@H]([C@@H]([C@H](O4)CO)O)O)O)O[C@H]5[C@@H]([C@H]([C@@H](O[C@@H]5CO)O[C@H]6[C@@H]([C@H]([C@@H](O[C@@H]6CO)NC(C[C@@H](C(=O)*)N*)=O)NC(C)=O)O)NC(C)=O)O)O 2D coordinates Mol file for the small molecule Search links Involved in 3 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
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Namehelp_outline
an N4-{β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein]
Identifier
RHEA-COMP:17732
Reactive part
help_outline
- Name help_outline N4-{β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-Asn residue Identifier CHEBI:187873 Charge 0 Formula C54H88N6O37 SMILEShelp_outline [C@H]1([C@H]([C@H]([C@@H]([C@H](O1)CO)O[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O)O)NC(C)=O)O)O[C@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)NC(C)=O)O[C@@H]4[C@@H]([C@@H](O[C@@H]([C@H]4O)CO[C@@H]5[C@H]([C@H]([C@@H]([C@H](O5)CO)O)O)O)O[C@H]6[C@@H]([C@H]([C@@H](O[C@@H]6CO)O[C@H]7[C@@H]([C@H]([C@@H](O[C@@H]7CO)NC(C[C@@H](C(=O)*)N*)=O)NC(C)=O)O)NC(C)=O)O)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 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:69615 | RHEA:69616 | RHEA:69617 | RHEA:69618 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes.
Oguri S., Yoshida A., Minowa M.T., Takeuchi M.
N-acetylglucosaminyltransferase (GnT)-IV catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-glycans. Two human GnT-IV isozymes (GnT-IVa and GnT-IVb) had been identified, which exhibit different expression profiles among human tissues ... >> More
N-acetylglucosaminyltransferase (GnT)-IV catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-glycans. Two human GnT-IV isozymes (GnT-IVa and GnT-IVb) had been identified, which exhibit different expression profiles among human tissues and cancer cell lines. To clarify the enzymatic properties of the respective enzymes, their kinetic parameters were determined using recombinant full-length enzymes expressed in COS7 cells. The K (m) of human GnT-IVb for UDP-GlcNAc was estimated to be 0.24 mM, which is 2-fold higher than that of human GnT-IVa. The K (m) values of GnT-IVb for pyridylaminated (PA) acceptor sugar chains with different branch numbers were 3-to 6-fold higher than those of GnT-IVa. To compare substrate specificities more precisely, we generated recombinant soluble enzymes of human GnT-IVa and GnT-IVb with N-terminal flag tags. Both enzymes showed similar substrate specificities as determined using fourteen PA-sugar chains. They preferred complex-type N-glycans over hybrid-types. Among the complex-type N-glycans tested, the relative activities of both enzymes were increased in proportion to the number of GlcNAc branches on the Man alpha1-6 arm. The Man alpha1-6 arm of the acceptors was not essential for their activities because a linear pentasaccharide lacking this arm, GlcNAcbeta1-2Manalpha1-3Manbeta1-4GlcNAcbeta1-4 GlcNAc-PA, was a substrate for both enzymes. These results indicate that human GnT-IVb exhibits the same acceptor substrate specificities as human GnT-IVa, although GnT-IVb has lower affinities for donors or acceptors than GnT-IVa. This suggests that GnT-IVa is more active than GnT-IVb under physiological conditions and that it primarily contributes to the biosynthesis of N-glycans. << Less
Glycoconj. J. 23:473-480(2006) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.