Undecaprenyl-diphosphooligosaccharide-protein glycotransferase
Appearance
(Redirected from PGLB)
Undecaprenyl-diphosphooligosaccharide-protein glycotransferase | |||||||||
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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 | ||||||||
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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
[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)