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ProteomicsAnalysis of the substrate specificities and reaction kinetics of the yeast oligosaccharyltransferase isoforms
Oligosaccharyltransferase (OST) catalyzes the central step in N-linked protein glycosylation, the transfer of a pre-assembled oligosaccharide from its lipid carrier onto asparagine residues of secretory proteins. The prototypic hetero-octameric OST complex from the yeast Saccharomyces cerevisiae exi...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-05-19 | PXD024590 | Pride
Site-occupancy Yeast oligosaccharyltransferase Substract specificity 
UnknownSubstrate specificities and reaction kinetics of the yeast oligosaccharyltransferase isoforms.
Not available
S-EPMC8191290 | biostudies-literature
UnknownOligosaccharyltransferase subunits bind polypeptide substrate to locally enhance N-glycosylation.
Not available
S-EPMC4256483 | biostudies-literature
UnknownUncoupling the hydrolysis of lipid-linked oligosaccharide from the oligosaccharyl transfer reaction by point mutations in yeast oligosaccharyltransferase.
Not available
S-EPMC7681024 | biostudies-literature
UnknownOxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.
Not available
S-EPMC2708779 | biostudies-literature
ProteomicsAnalysis of Substrate Specificity of Trypanosoma brucei OSTs by Functional Expression in Yeast
N-linked protein glycosylation is an essential and highly conserved post-translational modification in eukaryotes. The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to asparagine residues of nascent polypeptide chains is catalyzed by the oligosaccharyltransferase (OST) in the ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-11-03 | PXD007215 | Pride
Lipid linked oligosaccharide specificity Oligosaccharyltransferase N-linked glycosylation Glycosylation occupancy analysis Trypanosoma brucei 
UnknownStructural basis for the function of a minimembrane protein subunit of yeast oligosaccharyltransferase.
Not available
S-EPMC374328 | biostudies-literature
UnknownRefined topology model of the STT3/Stt3 protein subunit of the oligosaccharyltransferase complex.
Not available
S-EPMC5500801 | biostudies-literature
ProteomicsQuantitative Profiling of N-linked Glycosylation Machinery in Yeast Saccharomyces cerevisiae
Asparagine-linked glycosylation is a common posttranslational protein modification regulating the structure, stability and function of many proteins. The N-linked glycosylation machinery involves enzymes responsible for the assembly of the lipid-linked oligosaccharide (LLO), which is then transferre...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-10-12 | PXD006435 | Pride
Er (endoplasmatic reticulum) ost (oligosaccharyltransferase) glcnac (n-acetyl-glucosamine) llo (lipid-linked oligosaccharide) ms (mass spectrometry) prm (parallel reaction monitoring) silac (stable isotope labelling with amino acids in cell culture) 
UnknownStructure-guided identification of a new catalytic motif of oligosaccharyltransferase.
Not available
S-EPMC2206122 | biostudies-literature
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