ID   2.4.1.144
DE   beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase.
AN   beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase.
AN   GlcNAc-T III.
AN   GnTIII.
AN   N-acetylglucosaminyltransferase III.
AN   N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase
AN   III.
AN   uridine diphosphoacetylglucosamine-glycopeptide beta4-
AN   acetylglucosaminyltransferase III.
CA   N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
CA   alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CA   GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+)
CA   + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-
CA   [beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CA   GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
CC   -!- The enzyme, found in vertebrates, participates in the processing of
CC       N-glycans in the Golgi apparatus.
CC   -!- The residue added by the enzyme at position 4 of the beta-linked
CC       mannose of the trimannosyl core of N-glycans is known as a bisecting
CC       GlcNAc.
CC   -!- Unlike GlcNAc residues added to other positions, it is not extended
CC       or modified.
CC   -!- In addition, its presence prevents the action of other branching
CC       enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145)
CC       and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-
CC       T III leads to a decrease in highly branched N-glycan structures.
CC   -!- Formerly EC 2.4.1.51.
DR   Q09327, MGAT3_HUMAN;  Q10470, MGAT3_MOUSE;  Q02527, MGAT3_RAT  ;
//