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ENZYME entry: EC 2.4.1.144
Accepted Name |
beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase.
|
Alternative Name(s) |
beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase. |
GlcNAc-T III. |
GnTIII. |
N-acetylglucosaminyltransferase III. |
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase
III. |
uridine diphosphoacetylglucosamine-glycopeptide beta4-
acetylglucosaminyltransferase III. |
Reaction catalysed |
N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine <=> H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP |
Comment(s) |
- The enzyme, found in vertebrates, participates in the processing of
N-glycans in the Golgi apparatus.
- The residue added by the enzyme at position 4 of the beta-linked
mannose of the trimannosyl core of N-glycans is known as a bisecting
GlcNAc.
- Unlike GlcNAc residues added to other positions, it is not extended
or modified.
- In addition, its presence prevents the action of other branching
enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145)
and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-
T III leads to a decrease in highly branched N-glycan structures.
- Formerly EC 2.4.1.51.
|
Cross-references |
BRENDA | 2.4.1.144 |
EC2PDB | 2.4.1.144 |
ExplorEnz | 2.4.1.144 |
PRIAM enzyme-specific profiles | 2.4.1.144 |
KEGG Ligand Database for Enzyme Nomenclature | 2.4.1.144 |
IUBMB Enzyme Nomenclature | 2.4.1.144 |
IntEnz | 2.4.1.144 |
MEDLINE | Find literature relating to 2.4.1.144 |
MetaCyc | 2.4.1.144 |
Rhea expert-curated reactions | 2.4.1.144 |
UniProtKB/Swiss-Prot |
|
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.-.-
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