2.4.1.256: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase
This is an abbreviated version!
For detailed information about dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.256
-
2.4.1.256
-
lipid-linked
-
oligosaccharide
-
tomography
-
antidepressants
-
ligation-dependent
-
sanger
-
dilatation
-
n-glycosylation
-
neighbouring
-
arrhythmias
-
exercise-induced
-
t-wave
-
12-lead
-
ejection
-
desmosome
-
arrhythmogenic
-
cardiomyopathy
-
bundle-branch
-
electrocardiogram
-
tachycardia
-
culprit
-
borderline
-
antipsychotics
-
probands
- 2.4.1.256
-
lipid-linked
- oligosaccharide
-
tomography
-
antidepressants
-
ligation-dependent
-
sanger
-
dilatation
-
n-glycosylation
-
neighbouring
- arrhythmias
-
exercise-induced
-
t-wave
-
12-lead
-
ejection
-
desmosome
-
arrhythmogenic
-
cardiomyopathy
-
bundle-branch
-
electrocardiogram
-
tachycardia
-
culprit
-
borderline
-
antipsychotics
- probands
Reaction
Synonyms
ALG10, alpha1,2-glucosyltransferase, Die2
ECTree
2.4.1.256 dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferaseAdvanced search results
results (
results (General Information
General Information on EC 2.4.1.256 - dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
alg10 mutant strains accumulate lipid-linked Glc2Man9GlcNAc2. Hypoglycosylation of secreted proteins in alg10 deletion strains demonstrates that the terminal alpha-1,2-linked glucose residue is a key element in substrate recognition by the oligosaccharyltransferase. This ensures that primarily completely assembled oligosaccharide is transferred to protein
physiological function
physiological function
alg10 mutant strains accumulate lipid-linked Glc2Man9GlcNAc2. Hypoglycosylation of secreted proteins in alg10 deletion strains demonstrates that the terminal alpha-1,2-linked glucose residue is a key element in substrate recognition by the oligosaccharyltransferase. This ensures that primarily completely assembled oligosaccharide is transferred to protein. The terminal alpha-1,2 glucose residue on the lipid-bound oligosaccharide serves as a signal to indicate complete assembly of the core oligosaccharide. Once transferred to protein, the removal of this signal by glucosidase I might ensure that glycosylation sites remain glycosylated and are not deglycosylated by the oligosaccharyltransferase complex
physiological function
-
a homozygous Arabidopsis T-DNA insertion mutant accumulates mainly lipid-linked Glc2Man9Glc-NAc2 and displays a severe protein underglycosylation defect. Mutant plants have altered leaf size when grown in soil. The inactivation of the enzyme gene in Arabidopsis results in the activation of the unfolded protein response, increased salt sensitivity and suppression of the phenotype of alpha-glucosidase I-deficient plants
physiological function
Alg10 gene deletion mutants, as well as endoplasmic reticulum lumenal mannosyltransferases (Alg3, Alg9, and Alg12), glucosyltransferases (Alg6, Alg8), or oligosaccharyltransferase subunits (Ost3, Ost5, and Ost6) deletion mutants, show decreased glycan occupancy and altered cell wall proteomes. Mutations in earlier mannosyltransferase or glucosyltransferase steps of glycan biosynthesis have stronger hypoglycosylation phenotypes, but glucosyltransferase defects are more severe
