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ENZYME entry: EC

Accepted Name
beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase.
Alternative Name(s)
beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase.
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
  • 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 and GlcNAc-T V (EC, and thus increased activity of GlcNAc- T III leads to a decrease in highly branched N-glycan structures.
  • Formerly EC
PRIAM enzyme-specific profiles2.4.1.144
KEGG Ligand Database for Enzyme Nomenclature2.4.1.144
IUBMB Enzyme Nomenclature2.4.1.144
MEDLINEFind literature relating to
Rhea expert-curated reactions2.4.1.144
Q09327, MGAT3_HUMAN;  Q10470, MGAT3_MOUSE;  Q02527, MGAT3_RAT;  

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