EC |
2.4.99.19 |
Accepted name: |
undecaprenyl-diphosphooligosaccharide—protein glycotransferase |
Reaction: |
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-β-D-glycosyl linkage to protein L-asparagine |
Other name(s): |
PglB |
Systematic name: |
tritrans,heptacis-undecaprenyl-diphosphooligosaccharide:protein-L-asparagine N-β-D-oligosaccharidotransferase |
Comments: |
A bacterial enzyme that has been isolated from Campylobacter jejuni [1] and Campylobacter lari [2]. It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N′-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa’-Ser/Thr- (Xaa and Xaa’ not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D. Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J. Biol. Chem. 285 (2010) 4941–4950. [DOI] [PMID: 20007322] |
2. |
Lizak, C., Gerber, S., Numao, S., Aebi, M. and Locher, K.P. X-ray structure of a bacterial oligosaccharyltransferase. Nature 474 (2011) 350–355. [DOI] [PMID: 21677752] |
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[EC 2.4.99.19 created 2012] |
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