EC 2.4.1.143 - α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.1.143

Names

Accepted name:
α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Other names:
N-acetylglucosaminyltransferase II
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
α-1,6-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase
UDP-GlcNAc:mannoside α1-6 acetylglucosaminyltransferase
acetylglucosaminyltransferase II
uridine diphosphoacetylglucosamine-α-1,6-mannosylglycoprotein β-1-2-N-acetylglucosaminyltransferase
uridine diphosphoacetylglucosamine-α-D-mannoside β1-2-acetylglucosaminyltransferase
uridine diphosphoacetylglucosamine-mannoside α1→6-acetylglucosaminyltransferase
GnTII
MGAT2 (gene name)
GlcNAc-T II
UDP-N-acetyl-D-glucosamine:6-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Systematic name:
UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→6)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)

Reaction

Comments:

The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its activity initiates the synthesis of the second antenna of di-antennary complex N-glycans. While the natural substrate (produced by EC 3.2.1.114, mannosyl-oligosaccharide 1,3-1,6-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→6)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→3)]-β-D-Man-R.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008455
CAS Registry Number: 105913-04-0
UniProtKB/Swiss-Prot:

References

  1. Bendiak, B. and Schacter, H.
    Control of glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:α-D-mannoside β1-2 N-acetylglucosaminyltransferase II from rat liver.
    J. Biol. Chem. 262: 5775-5783 (1987). [PMID: 2952644]
  2. Harpaz, N. and Schachter, H.
    Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity.
    J. Biol. Chem. 255: 4885-4893 (1980). [PMID: 6445358]
  3. Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M.
    Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa.
    Biochemistry 20: 967-976 (1981). [PMID: 6452163]
  4. Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L.
    The nonidentity of porcine N-acetylglucosaminyltransferases I and II.
    J. Biol. Chem. 256: 11477-11482 (1981). [PMID: 6457827]
  5. Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G.
    Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type.
    Methods Enzymol. 98: 98-134 (1983). [PMID: 6366476]
  6. Bendiak, B. and Schachter, H.
    Control of glycoprotein synthesis. Kinetic mechanism, substrate specificity, and inhibition characteristics of UDP-N-acetylglucosamine:α-D-mannoside β-1-2 N-acetylglucosaminyltransferase II from rat liver.
    J. Biol. Chem. 262: 5784-5790 (1987). [PMID: 2952644]
  7. Tan, J., D'Agostaro, A. F., Bendiak, B., Reck, F., Sarkar, M., Squire, J. A., Leong, P., Schachter, H.
    The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein.
    Eur. J. Biochem. 231: 317-328 (1995). [PMID: 7635144]

[EC 2.4.1.143 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984)]