Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
NCBI PubMed ID: 8181570Journal NLM ID: 0155157Publisher: Elsevier
Institutions: Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, Germany
N-Oligosaccharyltransferase catalyzes the N-glycosylation of asparagine residues of nascent polypeptide chains in the endoplasmic reticulum, a pathway highly conserved in all eukaryotes. An enzymatically active complex was isolated from microsomal membranes from Saccharomyces cerevisiae, which is composed of four proteins: Wbp1p and Swp1p (previously found to be encoded by two essential genes necessary for N-glycosylation in vivo and in vitro) and two additional proteins with a molecular mass of 60/62 kDa and 34 kDa. The 60/62 component represents differentially glycosylated forms of a protein that has sequence homology to ribophorin I. Wbp1p and Swp1p reveal homology to mammalian OST 48 and ribophorin II, respectively. Ribophorin I and II and OST 48 were recently shown to be constituents of the mammalian transferase from dog pancreas. The data reveal a high conservation of the organization of this enzyme activity.
Structure type: oligomer
Location inside paper: Glc3Man9GlcNAc2
Trivial name: Glc3Man9GlcNAc2
Compound class: N-glycan, high-mannose
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_232584,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
Methods: SDS-PAGE, immunoafinity chromatography, immunoabsorption
Biosynthesis and genetic data: genetic data
Comments, role: supposed structure
NCBI Taxonomy refs (TaxIDs): 4932Reference(s) to other database(s): CCSD:
46824, CBank-STR:21302
Show glycosyltransferases
There is only one chemically distinct structure: