Undecaprenyl-diphosphooligosaccharide-protein glycotransferase
Undecaprenyl-diphosphooligosaccharide-protein glycotransferase (EC 2.4.99.19, PglB) is an enzyme with systematic name tritrans,heptacis-undecaprenyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligosaccharidotransferase.[1][2] This enzyme catalyses the following chemical reaction
- tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
This is a bacterial enzyme that is isolated from Campylobacter jejuni and Campylobacter lari.
References
- ↑ Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D. (2010). "Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases". J. Biol. Chem. 285 (7): 4941–4950. doi:10.1074/jbc.M109.081752. PMID 20007322.
- ↑ Lizak, C., Gerber, S., Numao, S., Aebi, M. and Locher, K.P. (2011). "X-ray structure of a bacterial oligosaccharyltransferase". Nature 474: 350–355. doi:10.1038/nature10151. PMID 21677752.
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