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
| Undecaprenyl-diphosphooligosaccharide-protein glycotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.99.19 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- 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
edit- ^ Maita N, Nyirenda J, Igura M, Kamishikiryo J, Kohda D (February 2010). "Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases". The Journal of Biological Chemistry. 285 (7): 4941–50. doi:10.1074/jbc.M109.081752. PMC 2836098. PMID 20007322.
- ^ Lizak C, Gerber S, Numao S, Aebi M, Locher KP (June 2011). "X-ray structure of a bacterial oligosaccharyltransferase". Nature. 474 (7351): 350–5. doi:10.1038/nature10151. PMID 21677752. S2CID 205225231.
External links
edit- Undecaprenyl-diphosphooligosaccharide-protein+glycotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
