| 别名 |
(GnT)-III, acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-glycopeptide beta4-, III, beta(1,4)-N-acetylglucosaminyltransferase III, beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, beta-1,4-N-acetylglucosaminyltransferase III, beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase, beta1,4-N-acetylglucosaminyltransferase III, GlcNAc-transferase-III, GlcNAcTase-III, GnT-III, GnTIII, Golgi beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase III, MGAT3, N-acetyl-glucosaminyltransferase III, N-acetylglucosaminyltransferase III, N-acetylglucosaminyltransferase-III, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III, uridine diphosphate (UDP)-N-acetylglucosamin/beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase III, uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase III |
| Comments |
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 ¦Â-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. |
