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4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucopyranose
not a common substrate for alpha-glucosidase I
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
4°C, pH 6.25
-
-
?
4-methylumbelliferyl-alpha-D-glucoside
4-methylumbelliferone + alpha-D-glucose
-
pH 4.0, 60 min, 37°C
-
-
?
4-methylumbelliferyl-alpha-D-glucoside + H2O
4-methylumbelliferone + D-glucose
4-nitrophenyl D-alpha-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
pH 4.3
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3-tetramethylrhodamine + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3-tetramethylrhodamine
cleaves the terminal alpha-1,2-linked glucose
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O-(CH2)8COOCH3
?
Glc3Man5GlcNAc + H2O
D-glucose + Glc2Man5GlcNAc
Glc3Man6GlcNAc + H2O
D-glucose + Glc2Man6GlcNAc
Glc3Man7GlcNAc + H2O
D-glucose + Glc2Man7GlcNAc
Glc3Man8GlcNAc + H2O
D-glucose + Glc2Man8GlcNAc
Glc3Man9GlcNAc + H2O
D-glucose + Glc2Man9GlcNAc
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
Glc3Man9GlcNAc2-pyridylamine + H2O
Glc2Man9GlcNAc2-pyridylamine + D-glucose
Glcalpha(1->2)Glcalpha(1->3)Glcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)Manbeta(1->4)GlcNacbeta(1->4)GlcNacbeta-pyridylamine + H2O
Glcalpha(1->3)Glcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)Manbeta(1->4)GlcNacbeta(1->4)GlcNacbeta-pyridylamine + D-glucose
kojibiose
?
-
pH 5.0, 35°C, 30 min
-
-
?
Maltoheptaose
?
-
pH 5.0, 35°C, 30 min
-
-
?
Maltohexaose
?
-
pH 5.0, 35°C, 30 min
-
-
?
maltopentaose
?
-
pH 5.0, 35°C, 30 min
-
-
?
maltose
?
-
pH 5.0, 35°C, 30 min
-
-
?
Maltotetraose
?
-
pH 5.0, 35°C, 30 min
-
-
?
maltotriose
?
-
pH 5.0, 35°C, 30 min
-
-
?
nigerose
?
-
pH 5.0, 35°C, 30 min
-
-
?
trehalose
?
-
pH 5.0, 35°C, 30 min
-
-
?
additional information
?
-
4-methylumbelliferyl-alpha-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
-
formation of alpha-glucose is delayed with respect to beta-glucose: enzyme operates with inversion of anomeric configuration
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
synthetic substrate, formation of the product demonstrates that the enzyme operates with inversion of anomeric configuration
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
-
formation of alpha-glucose is delayed with respect to beta-glucose: enzyme operates with inversion of anomeric configuration
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
synthetic trisaccharide
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
synthetic trisaccharide
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
synthetic substrate
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
synthetic substrate, formation of the product demonstrates that the enzyme operates with inversion of anomeric configuration
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O
beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3
-
synthetic substrate
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O-(CH2)8COOCH3
?
-
residues E613 and D617 play a crucial role in maintaining enzyme activity
-
-
?
alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O-(CH2)8COOCH3
?
-
residues E613 and D617 play a crucial role in maintaining enzyme activity
-
-
?
Glc3Man5GlcNAc + H2O
D-glucose + Glc2Man5GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man5GlcNAc + H2O
D-glucose + Glc2Man5GlcNAc
-
hydrolyzed at a rate similar to that of natural substrate Glc3Man9GlcNAc2
-
-
?
Glc3Man5GlcNAc + H2O
D-glucose + Glc2Man5GlcNAc
-
-
-
-
?
Glc3Man5GlcNAc + H2O
D-glucose + Glc2Man5GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man5GlcNAc + H2O
D-glucose + Glc2Man5GlcNAc
-
11% activity compared with Glc3Man9GlcNAc
-
?
Glc3Man6GlcNAc + H2O
D-glucose + Glc2Man6GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man6GlcNAc + H2O
D-glucose + Glc2Man6GlcNAc
-
slowly hydrolyzed
-
?
Glc3Man6GlcNAc + H2O
D-glucose + Glc2Man6GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man6GlcNAc + H2O
D-glucose + Glc2Man6GlcNAc
-
15% activity compared with Glc3Man9GlcNAc
-
?
Glc3Man7GlcNAc + H2O
D-glucose + Glc2Man7GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man7GlcNAc + H2O
D-glucose + Glc2Man7GlcNAc
-
slowly hydrolyzed
-
?
Glc3Man7GlcNAc + H2O
D-glucose + Glc2Man7GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man7GlcNAc + H2O
D-glucose + Glc2Man7GlcNAc
-
30% activity compared with Glc3Man9GlcNAc
-
?
Glc3Man8GlcNAc + H2O
D-glucose + Glc2Man8GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man8GlcNAc + H2O
D-glucose + Glc2Man8GlcNAc
-
slowly hydrolyzed
-
?
Glc3Man8GlcNAc + H2O
D-glucose + Glc2Man8GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man8GlcNAc + H2O
D-glucose + Glc2Man8GlcNAc
-
85% activity compared with Glc3Man9GlcNAc
-
?
Glc3Man9GlcNAc + H2O
D-glucose + Glc2Man9GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc + H2O
D-glucose + Glc2Man9GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc + H2O
D-glucose + Glc2Man9GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc + H2O
D-glucose + Glc2Man9GlcNAc
-
very good substrate: activity is highest against free oligosaccharide which contains a single N-acetylglucosamine at the reducing end and is lowered about 10% by the presence of a second N-acetylglucosamine at the reducing end
-
?
Glc3Man9GlcNAc + H2O
D-glucose + Glc2Man9GlcNAc
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
trimming of the alpha1,2-linked glucosyl residue constitutive of the N-glycan precursor
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
alpha-glucosidase I removes the outermost alpha1,2-glucose unit from the N-linked core Glc3Man9GlcNAc2
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
3 glucose residues are required for catalysis
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
3 glucose residues are required for catalysis
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
-
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
no significant difference in enzyme activity towards free, peptide-bound, or lipid-linked oligosaccharide, lipid- and peptide-linked oligosaccharide are hydrolyzed at a rate only 10% lower than free oligosaccharide
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
slowly hydrolyzed, free and peptide-bound Glc3Man9GlcNAc2 oligosaccharides are hydrolyzed at similar rates, both being about threefold better substrates than the lipid-linked structure
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
activity with oligosaccharide-lipid 2.5 times higher than with glycosylated alpha-lactalbumin and 3 times higher than with free oligosaccharide
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
lower activity than towards free oligosaccharide substrates
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2-lipid + H2O
D-glucose + Glc2Man9GlcNAc2-lipid
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
no significant difference in enzyme activity towards free, peptide-bound, or lipid-linked oligosaccharide, lipid- and peptide-linked oligosaccharide are hydrolyzed at a rate only 10% lower than free oligosaccharide
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
free and peptide-bound Glc3Man9GlcNAc2 oligosaccharides are hydrolyzed at similar rates, both being about threefold better substrates than the lipid-linked structure
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
Glc-containing oligosaccharide attached to S-carboxymethylated alpha-lactalbumin
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
lower activity than towards free oligosaccharide substrates
-
?
Glc3Man9GlcNAc2-peptide + H2O
D-glucose + Glc2Man9GlcNAc2-peptide
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
?
Glc3Man9GlcNAc2-pyridylamine + H2O
Glc2Man9GlcNAc2-pyridylamine + D-glucose
-
-
-
?
Glc3Man9GlcNAc2-pyridylamine + H2O
Glc2Man9GlcNAc2-pyridylamine + D-glucose
-
-
-
?
Glcalpha(1->2)Glcalpha(1->3)Glcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)Manbeta(1->4)GlcNacbeta(1->4)GlcNacbeta-pyridylamine + H2O
Glcalpha(1->3)Glcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)Manbeta(1->4)GlcNacbeta(1->4)GlcNacbeta-pyridylamine + D-glucose
-
-
-
?
Glcalpha(1->2)Glcalpha(1->3)Glcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)Manbeta(1->4)GlcNacbeta(1->4)GlcNacbeta-pyridylamine + H2O
Glcalpha(1->3)Glcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)Manbeta(1->4)GlcNacbeta(1->4)GlcNacbeta-pyridylamine + D-glucose
-
-
-
?
additional information
?
-
-
controls the first committed step for N-glycan trimming, involved in the formation of protein bodies, cell differentiation, accumulation of seed storage proteins and embryo development
-
-
?
additional information
?
-
first step in N-glycan processing, required for the function of only a small subset of N-glycoproteins, mutant seedlings swell slightly, but are not able to elongate or grow to any extent
-
-
?
additional information
?
-
the enzyme does not hydrolyze the terminal alpha(1-2)-linkage of Glc2Man9GlcNAc2-pyridylamine
-
-
?
additional information
?
-
the enzyme does not hydrolyze the terminal alpha(1-2)-linkage of Glc2Man9GlcNAc2-pyridylamine
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
structure of the Glc3 branch rather than the more distant domains of the oligosaccharide molecule are controlling specificity
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-beta-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-beta-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
p-nitrophenyl-glucosides: no substrates
-
-
?
additional information
?
-
-
p-nitrophenyl-glucosides: no substrates
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
glucosidase I is a control enzyme for the regulation of glycoprotein processing
-
-
?
additional information
?
-
-
glucosidase I is a control enzyme for the regulation of glycoprotein processing
-
-
?
additional information
?
-
-
play a crucial role in the overall regulation of glycoprotein biosynthesis
-
-
?
additional information
?
-
-
significant role in protein folding by allowing the binding of glycoproteins to the endoplasmic reticulum chaperones calnexin and calreticulin
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
key enzyme in the biosynthesis of asparagines-linked oligosaccharides catalyzing the first processing event after the en bloc transfer of Glc3Man9GlcNAc2 to proteins
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
substrate selectivity
-
-
?
additional information
?
-
-
p-NO2-phenyl-alpha-glucoside and p-NO2-phenyl-beta-glucoside: no substrates
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
processing alpha-glucosidases in the endoplasmic reticulum act in concert with two lectin chaperones, membrane-bound calnexin and its soluble homolog calreticulin, and with the enzyme UDP-glucose:glycoprotein glucosyltransferase to facilitate glycoprotein folding
-
-
?
additional information
?
-
-
role in the folding of newly formed glycoprotein and in endoplasmic reticulum quality control
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
glucosidase I modifies N-glucans. Sequential cleavage of the outermost alpha1,2-linked glucose residue. First de-glucosylation step catalyzed by glucosidase I (removal of glucose 1) occurs as soon as the core glycan has been transferred to the nascent chain by oligosaccharyltransferase
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
processing alpha-glucosidases in the endoplasmic reticulum act in concert with two lectin chaperones, membrane-bound calnexin and its soluble homolog calreticulin, and with the enzyme UDP-glucose:glycoprotein glucosyltransferase to facilitate glycoprotein folding
-
-
?
additional information
?
-
-
role in the folding of newly formed glycoprotein and in endoplasmic reticulum quality control
-
-
?
additional information
?
-
-
trimming of the glucose residues is identical in Saccharomyces cerevisiae and in mammalian cells
-
-
?
additional information
?
-
-
essential for maturation of glycoproteins containing N-glycans in mammalian cells, alpha-glucosidase I has been conserved through eukaryotic evolution from yeast to mammals
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
glucosidase I modifies N-glucans. Sequential cleavage of the outermost alpha1,2-linked glucose residue. First de-glucosylation step catalyzed by glucosidase I (removal of glucose 1) occurs as soon as the core glycan has been transferred to the nascent chain by oligosaccharyltransferase
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
comparison of free and linked oligosaccharides as substrates: activity is lower against linked substrates than against free substrates
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
critical role in overall biosynthesis and regulation of protein N-glycosylation
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
very slightly active with Glc2Man9GlcNAc2
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-glucosides: no substrates
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
indirect role in cell wall beta1,6-glucan biosynthesis and/or in beta1,6-glucan insertion into the cell wall
-
-
?
additional information
?
-
-
indirect role in cell wall beta1,6-glucan biosynthesis and/or in beta1,6-glucan insertion into the cell wall
-
-
?
additional information
?
-
-
cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner
-
-
?
additional information
?
-
-
cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner
-
-
?
additional information
?
-
-
cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner
-
-
?
additional information
?
-
-
trimming of the glucose residues is identical in Saccharomyces cerevisiae and in mammalian cells
-
-
?
additional information
?
-
-
significant role in protein folding by allowing the binding of glycoproteins to the endoplasmic reticulum chaperones calnexin and calreticulin
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
key enzyme in the biosynthesis of asparagines-linked oligosaccharides catalyzing the first processing event after the en bloc transfer of Glc3Man9GlcNAc2 to proteins
-
-
?
additional information
?
-
-
regulates one of the key steps in asparagines-linked glycoprotein biosynthesis
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
very slightly active with Glc2Man9GlcNAc2
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
methylumbelliferyl-beta-glucosides: no substrates
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
aryl-alpha-D-glucosides: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-beta-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
glucose processing is essential for pro-receptor transport and maturation
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
Glc1Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
Glc2Man9GlcNAc2: not a substrate
-
-
?
additional information
?
-
-
substrate and product specificity
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
first enzyme of processing of N-linked oligosaccharides in plants, plant glucosidase I might be analogous to glucosidase I of animal cells
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
alpha-glucosidase I removes the outermost alpha1,2-glucose unit from the N-linked core Glc3Man9GlcNAc2
-
-
?
additional information
?
-
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
hydrolyses specifically terminal alpha1,2-linked glucose residue
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
specific involvement in the N-linked oligosaccharide-processing pathway
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
Glc3Man9GlcNAc2 + H2O
?
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
controls the first committed step for N-glycan trimming, involved in the formation of protein bodies, cell differentiation, accumulation of seed storage proteins and embryo development
-
-
?
additional information
?
-
first step in N-glycan processing, required for the function of only a small subset of N-glycoproteins, mutant seedlings swell slightly, but are not able to elongate or grow to any extent
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
glucosidase I is a control enzyme for the regulation of glycoprotein processing
-
-
?
additional information
?
-
-
glucosidase I is a control enzyme for the regulation of glycoprotein processing
-
-
?
additional information
?
-
-
play a crucial role in the overall regulation of glycoprotein biosynthesis
-
-
?
additional information
?
-
-
significant role in protein folding by allowing the binding of glycoproteins to the endoplasmic reticulum chaperones calnexin and calreticulin
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
key enzyme in the biosynthesis of asparagines-linked oligosaccharides catalyzing the first processing event after the en bloc transfer of Glc3Man9GlcNAc2 to proteins
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
processing alpha-glucosidases in the endoplasmic reticulum act in concert with two lectin chaperones, membrane-bound calnexin and its soluble homolog calreticulin, and with the enzyme UDP-glucose:glycoprotein glucosyltransferase to facilitate glycoprotein folding
-
-
?
additional information
?
-
-
role in the folding of newly formed glycoprotein and in endoplasmic reticulum quality control
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
processing alpha-glucosidases in the endoplasmic reticulum act in concert with two lectin chaperones, membrane-bound calnexin and its soluble homolog calreticulin, and with the enzyme UDP-glucose:glycoprotein glucosyltransferase to facilitate glycoprotein folding
-
-
?
additional information
?
-
-
role in the folding of newly formed glycoprotein and in endoplasmic reticulum quality control
-
-
?
additional information
?
-
-
trimming of the glucose residues is identical in Saccharomyces cerevisiae and in mammalian cells
-
-
?
additional information
?
-
-
essential for maturation of glycoproteins containing N-glycans in mammalian cells, alpha-glucosidase I has been conserved through eukaryotic evolution from yeast to mammals
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
catalyzes initial step in post-glycosylation processing of cellular glycoprotein
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
critical role in overall biosynthesis and regulation of protein N-glycosylation
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
indirect role in cell wall beta1,6-glucan biosynthesis and/or in beta1,6-glucan insertion into the cell wall
-
-
?
additional information
?
-
-
indirect role in cell wall beta1,6-glucan biosynthesis and/or in beta1,6-glucan insertion into the cell wall
-
-
?
additional information
?
-
-
cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner
-
-
?
additional information
?
-
-
cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner
-
-
?
additional information
?
-
-
cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner
-
-
?
additional information
?
-
-
trimming of the glucose residues is identical in Saccharomyces cerevisiae and in mammalian cells
-
-
?
additional information
?
-
-
significant role in protein folding by allowing the binding of glycoproteins to the endoplasmic reticulum chaperones calnexin and calreticulin
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
key enzyme in the biosynthesis of asparagines-linked oligosaccharides catalyzing the first processing event after the en bloc transfer of Glc3Man9GlcNAc2 to proteins
-
-
?
additional information
?
-
-
regulates one of the key steps in asparagines-linked glycoprotein biosynthesis
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
glucose processing is essential for pro-receptor transport and maturation
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins
-
-
?
additional information
?
-
-
involved in processing of asparagine-linked oligosaccharides
-
-
?
additional information
?
-
-
first enzyme of processing of N-linked oligosaccharides in plants, plant glucosidase I might be analogous to glucosidase I of animal cells
-
-
?
additional information
?
-
-
involved in the formation of high mannose and complex glycoproteins
-
-
?
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1-deoxymannojirimycin
-
very slight inhibition, Ki = 0.19 mM
2,5-Dihydroxymethyl-3,4-dihydroxypyrrolidine
-
plant pyrrolidine alkaloid, DMDP, 0.04 mM: 50% inhibition
2,6-anhydro-1-benzamide-D-glycero-D-ido-heptitol
-
18.2% inhibition at 1 mM
4-nitrophenyl-2-deoxy-alpha-D-glucopyranoside
-
56.2% inhibition at 5 mM
4-nitrophenyl-3-deoxy-alpha-D-glucopyranoside
-
71.7% inhibition at 5 mM
4-nitrophenyl-4-deoxy-alpha-D-glucopyranoside
-
18.5% inhibition at 5 mM
4-nitrophenyl-5-deoxy-alpha-D-glucopyranoside
-
22.2% inhibition at 5 mM
4-nitrophenyl-6-deoxy-alpha-D-glucopyranoside
-
32.3% inhibition at 5 mM
Ag+
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
australine
39% inhibition at 0.02 mM
bromoconduritol
22% inhibition at 0.02 mM
chloride
-
inhibitory above 0.3 M, 0.5 M: 30% inhibition
diethyl dicarbonate
-
55% inhibition at 1 mM after 30 min
ethyl-3-(3-(dimethylamino)propyl)carbodiimide
-
90% inhibition at 50 mM after 60 min at pH 6.8, 4°C, preincubation with deoxynorjirmycin prevents
glycerol
-
2% or higher: 25% or more inhibition
heavy-metal ions
-
potent inhibitors, inhibition reversed by adding an excess of dithiothreitol
-
Hg2+
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
Man9GlcNAc
-
1 mM thyroglobulin-derived Man9GlcNAc: 22% inhibition
N,N-dimethyl-1-deoxynojirimycin
N-(5-carboxypentyl)-1-deoxynojirimycin
N-(6'-(2'',4''-dinitrophenylamino)hexyl)-1-deoxynojirimycin
-
-
N-(6'-(4''-azido-2''-nitrophenylamino)hexyl)-1-deoxynojirimycin
-
highly potent inhibitor of alpha-glucosidase I
N-5-carboxypentyl-1-deoxymannojirimycin
-
very slight inhibition, Ki = 0.1 mM
N-butyl-1-deoxynojirimycin
-
strong inhibition, Ki = 0.00009 mM
N-butyldeoxynojirimycin
-
-
N-decanoyl-1-deoxynojirimycin
-
very slight inhibition, Ki = 0.07 mM
N-decyl-1-deoxynojirimycin
-
strong inhibition, Ki = 0.0004 mM
N-dodecyl-1-deoxynojirimycin
-
slight inhibition
N-hexyl-1-deoxynojirimycin
-
strong inhibition, Ki = 0.00013 mM
N-methyl-1-deoxymannojirimycin
-
very slight inhibition, Ki = 0.017 mM
N-methyl-1-deoxynojirimycin
p-Aminophenyl-beta-thioglucoside
-
100 mM: 73% inhibition
p-nitrophenyl-alpha-D-glucoside
p-nitrophenyl-beta-D-glucoside
phosphate
-
inhibitory above 0.3 M, 0.5 M: 30% inhibition
sulfate
-
0.1-0.2 M: 15-20% inhibition, somewhate more inhibitory at higher concentrations
Tris/maleate
-
10 mM: 60% inhibition
Trypsin
-
up to 40% inhibition in the presence of Lubrol PX, without Lubrol PX: no inhibition
-
1-deoxynojirimycin
-
1-deoxynojirimycin
-
strong inhibition
1-deoxynojirimycin
-
0.01 mM: 80% inhibition; strong inhibition
1-deoxynojirimycin
-
strong inhibition
1-deoxynojirimycin
-
strong inhibition; strong inhibition, Ki = 0.0001 mM
1-deoxynojirimycin
-
50% inhibition
1-deoxynojirimycin
-
strong inhibition
1-deoxynojirimycin
-
strong inhibition
1-deoxynojirimycin
-
strong inhibition
1-deoxynojirimycin
-
0.01 mM: 50% inhibition
1-deoxynojirimycin
-
strong inhibition
1-deoxynojirimycin
-
strong inhibition; strong inhibition, Ki = 0.0021 mM
1-deoxynojirimycin
-
strong inhibition
castanospermine
-
castanospermine
-
15% inhibition
castanospermine
-
plant indolizidine alkaloid, strong inhibition
CM-9-78
-
-
Co2+
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
Cu2+
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
Cu2+
-
partial inhibition
D-glucose
-
no significant inhibition, 10 mM: 13% inhibition
D-glucose
-
5 mM: 25% inhibition
D-mannose
-
10 mM: no inhibition
D-mannose
-
1 mM: 4% inhibition, 25 mM: 60% inhibition
D-mannose
-
5 mM: 25% inhibition
kojibiose
-
kojibiose
-
alpha-1,2-linked glucose disaccharide
kojibiose
-
1 mM: 76% inhibition; alpha-1,2-linked glucose disaccharide
kojibiose
-
alpha-1,2-linked glucose disaccharide
kojibiose
-
alpha-1,2-linked glucose disaccharide
kojibiose
-
alpha-1,2-linked glucose disaccharide; Ki = 0.095 mM
kojibiose
-
0.5 mM: 50% inhibition; alpha-1,2-linked glucose disaccharide
N,N-dimethyl-1-deoxynojirimycin
-
strong inhibition
N,N-dimethyl-1-deoxynojirimycin
-
strong inhibition; strong inhibition, Ki = 0.0004 mM
N,N-dimethyl-1-deoxynojirimycin
-
specific inhibitor; strong inhibition
N,N-dimethyl-1-deoxynojirimycin
-
strong inhibition
N,N-dimethyl-1-deoxynojirimycin
-
specific inhibitor; strong inhibition
N,N-dimethyl-1-deoxynojirimycin
-
strong inhibition; strong inhibition, Ki = 0.0005 mM
N-(5-carboxypentyl)-1-deoxynojirimycin
-
strong inhibition
N-(5-carboxypentyl)-1-deoxynojirimycin
-
slight inhibition
N-(5-carboxypentyl)-1-deoxynojirimycin
-
-
N-(5-carboxypentyl)-1-deoxynojirimycin
-
strong inhibition
N-(5-carboxypentyl)-1-deoxynojirimycin
-
strong inhibition; strong inhibition, Ki = 0.0005 mM
N-(5-carboxypentyl)-1-deoxynojirimycin
-
strong inhibition
N-(5-carboxypentyl)-1-deoxynojirimycin
-
strong inhibition; strong specific inhibition, Ki = 0.00045 mM
N-butyl-deoxynojirimycin
-
-
N-butyl-deoxynojirimycin
-
-
N-butyl-deoxynojirimycin
-
-
N-butyl-deoxynojirimycin
-
-
N-ethylmaleimide
-
N-ethylmaleimide
-
inhibition when membranes are disrupted with Lubrol PX or saponin, inhibition abolished completely in the presence of dithiothreitol
N-methyl-1-deoxynojirimycin
-
strong inhibition
N-methyl-1-deoxynojirimycin
-
strong inhibition; strong inhibition, Ki = 0.00007 mM
N-methyl-1-deoxynojirimycin
-
-
N-methyl-1-deoxynojirimycin
-
strong inhibition
N-nonyl-deoxynojirimycin
-
-
N-nonyl-deoxynojirimycin
-
-
N-nonyl-deoxynojirimycin
-
-
Nojirimycin
-
potent inhibitor
Nojirimycin
-
strong inhibition, 0.1 mM: 40% inhibition, 0.16 mM: 50% inhibition
octyl-beta-glucoside
-
-
octyl-beta-glucoside
-
10 mM: 90% inhibition
OSL-95II
-
-
p-nitrophenyl-alpha-D-glucoside
-
0.0005 mM: 19% inhibition
p-nitrophenyl-alpha-D-glucoside
-
5 mM
p-nitrophenyl-alpha-D-glucoside
-
-
p-nitrophenyl-beta-D-glucoside
-
0.0005 mM: 14% inhibition
p-nitrophenyl-beta-D-glucoside
-
5 mM
p-nitrophenyl-beta-D-glucoside
-
-
PBDNJ0801
-
-
PBDNJ0803
-
-
PBDNJ0804
-
-
Tris
-
-
Tris
-
20 mM: 50% inhibition
Zn2+
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
additional information
-
-
-
additional information
-
no inhibition by conduritol B epoxide, bromoconduritols a and B, acarbose at 1 mM
-
additional information
-
no inhibition by alpha,alpha'-bipyridyl and o-phenanthroline; no inhibition by EDTA; no significant inhibition by nigerose, Glc(alpha1-3)Glc disaccharide, maltose, gentibiose, cellobiose, sucrose
-
additional information
-
-
-
additional information
-
inhibition of glucosidase I as a function of pH, pH dependence of inhibition, the inhibiting species is the cationic form of the inhibitor; no inhibition by EDTA
-
additional information
2-deoxyglucose, 3-deoxyglucose or 6-deoxyglucose do not have any effect on the enzyme activity; the enzyme is completely insensitive to diethyl pyrocarbonate
-
additional information
-
2-deoxyglucose, 3-deoxyglucose or 6-deoxyglucose do not have any effect on the enzyme activity; the enzyme is completely insensitive to diethyl pyrocarbonate
-
additional information
-
no inhibition by alpha- or beta-linked glucose disaccharides; no inhibition by methyl-beta-D-glucoside, sophorose laminaribiose, cellobiose, gentiobiose and methyl-alpha-D-glucoside
-
additional information
-
-
-
additional information
-
no inhibition by 1-deoxymannojirimycin
-
additional information
-
-
-
additional information
-
no inhibition by bromoconduritol
-
additional information
-
inhibitors of processing glucosidase enhances anti CD3-induced interleukin-2 production and cause an accumulation of glucose-containing high-mannose-type oligosaccharides and suppress the secretion of interleukin-4, interferon-gamma and interleukin-5. Processing inhibitors inhibit the N-linked oligosaccharide processing of cytokines, inhibition of processing enzyme glucosidase I induces a decreased secretion of cytokines with N-linked oligosaccharides
-
additional information
-
-
-
additional information
-
no inhibition by EDTA
-
additional information
-
no inhibition by EDTA
-
additional information
-
no inhibition by 1 mM EDTA or 1 mM o-phenanthroline
-
additional information
-
no inhibition by dithiothreitol, 2-mercaptoethanol, Mg2+, Mn2+, EDTA, potassium phosphate
-
additional information
-
no inhibition by 1-deoxymannojirimycin
-
additional information
-
no inhibition by 1 mM EDTA or 1 mM o-phenanthroline
-
additional information
-
no inhibition by alpha-1,3-, alpha-1,4-, and alpha-1,6-linked glucose disaccharides; no inhibition by EDTA; no inhibition by nigerose, maltose, isomaltose at 2 mM; no inhibition by swainsonine, deoxymannojirimycin or 1,4-dideoxy-1,4-imino-D-mannitol
-
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Grinna, L.S.; Robbins, P.W.
Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
J. Biol. Chem.
255
2255-2258
1980
Rattus norvegicus
brenda
Bause E.; Erkens, R.; Schweden, J.; Jaenicke, L.
Purification and characterization of trimming glucosidase I from Saccharomyces cerevisiae
FEBS Lett.
206
208-212
1986
Bos taurus, Saccharomyces cerevisiae
-
brenda
Kilker, R.D.Jr.; Saunier, B.; Tkacz, J.S.; Herscovics, A.
Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2
J. Biol. Chem.
256
5299-5303
1981
Saccharomyces cerevisiae, Saccharomyces cerevisiae X-2180
brenda
Hettkamp, H.; Legler, G.; Bause, E.
Purification by affinity chromatography of glucosidase I, an endoplasmic reticulum hydrolase involved in the processing of asparagine-linked oligosaccharides
Eur. J. Biochem.
142
85-90
1984
Bos taurus
brenda
Grinna, L.S.; Robbins, P.W.
Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides
J. Biol. Chem.
254
8814-8818
1979
Rattus norvegicus
brenda
Michael, J.M.; Kornfeld, S.
Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides
Arch. Biochem. Biophys.
199
249-258
1980
Bos taurus
brenda
Zamarripa-Morales, S.; Villagomez-Castro, J.C.; Calvo-Mendez, C.; Flores-Carreon, A.; Lopez-Romero, E.
Entamoeba histolytica: identification and properties of membrane-bound and soluble alpha-glucosidases
Exp. Parasitol.
93
109-115
1999
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS
brenda
Herscovics, A.
Importance of glycosidases in mammalian glycoprotein biosynthesis
Biochim. Biophys. Acta
1473
96-107
1999
Homo sapiens, Mammalia
brenda
Herscovics, A.
Processing glycosidases of Saccharomyces cerevisiae
Biochim. Biophys. Acta
1426
275-285
1999
Saccharomyces cerevisiae, Mammalia
brenda
Palcic, M.M.; Scaman, C.H.; Otter, A.; Szpacenko, A.; Romaniouk, A.; Li, Y.X.; Vijay, I.K.
Processing alpha-glucosidase I is an inverting glycosidase
Glycoconj. J.
16
351-355
1999
Bos taurus, Saccharomyces cerevisiae
brenda
Rush, J.S.; Waechter, C.J.
Topological studies on the enzymes catalyzing the biosynthesis of Glc-P-dolichol and the triglucosyl cap of Glc3Man9GlcNAc2-P-P-dolichol in microsomal vesicles from pig brain: use of the processing glucosidases I/II as latency markers
Glycobiology
8
1207-1213
1998
Rattus norvegicus, Sus scrofa
brenda
Kosuge, T.; Tamura, T.; Nariuchi, H.; Toyoshima, S.
Effect of inhibitors of glycopotein processing on cytokine secretion and production in anti CD3-stimulated T cells
Biol. Pharm. Bull.
23
1-5
2000
Mus musculus, Mus musculus C57BL/6
brenda
Elting, J.J.; Chen, W.W.; Lennarz, W.J.
Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains
J. Biol. Chem.
255
2325-2331
1980
Gallus gallus
brenda
Szumilo, T.; Kaushal, G.P.; Elbein, A.D.
Purification and properties of glucosidase I from mung bean seedlings
Arch. Biochem. Biophys.
247
261-271
1986
Vigna radiata
brenda
Hettkamp, H.; Bause, E.; Legler, G.
Inhibition by nojirimycin and 1-deoxynojirimycin of microsomal glucosidases from calf liver acting on the glycoprotein oligosaccharides Glc1-3Man9GlcNAc2
Biosci. Rep.
2
899-906
1982
Bos taurus
brenda
Liu, T.; Stetson, B.; Turco, S.J.; Hubbard, S.C.; Robbins, P.W.
Arrangement of glucose residues in the lipid-linked oligosaccharide precursor of asparaginyl oligosaccharides
J. Biol. Chem.
254
4554-4559
1979
Talaromyces funiculosus, Rattus norvegicus, Talaromyces funiculosus QM474
brenda
Kalz-Fuller, B.; Bieberich, E.; Bause, E.
Cloning and expression of glucosidase I from human hippocampus
Eur. J. Biochem.
231
344-351
1995
Homo sapiens, Sus scrofa
brenda
Kalz-Fuller, B.; Heidrich-Kaul, C.; Nthen, M; Bause, E.; Schwanitz, G.
Localization of the human glucosidase I gene to chromosome 2p12-p13 by fluorescence in situ hybridization and PCR analysis of somatic cell hybrids
Genomics
34
442-443
1996
Homo sapiens
brenda
Simons, J.F.; Ebersold, M.; Helenius, A.
Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p
EMBO J.
17
396-405
1998
Saccharomyces cerevisiae
brenda
Romero, P.A.; Dijkgraaf, G.J.P.; Shahinian, S.; Herscovics, A.; Bussey, H.
The yeast CWH41 gene encodes glucosidase I
Glycobiology
7
997-1004
1997
Saccharomyces cerevisiae
brenda
Jiang, B.; Sheraton, J.; Ram, A.F.J.; Dijkgraaf, G.J.P.; Klis, F.M.; Bussey, H.
CWH41 encodes a novel endoplasmic reticulum membrane N-glycoprotein involved in beta1,6-glucan assembly
J. Bacteriol.
178
1162-1171
1996
Saccharomyces cerevisiae
brenda
Shailubhai, K.; Pratta, M.A.; Vijay, I.K.
Purification and characterization of glucosidase I involved in N-linked glycoprotein processing in bovine mammary gland
Biochem. J.
247
555-562
1987
Bos taurus, Cavia porcellus, Mus musculus, Rattus norvegicus
brenda
Shailubhai, K.; Pukazhenthi, B.S.; Saxena, E.S.; Varma, G.M.; Vijay, I.K.
Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain
J. Biol. Chem.
266
16587-16593
1991
Rattus norvegicus
brenda
Bause, E.; Schweden, J.; Gross, A.; Orthen, B.
Purification and characterization of trimming glucosidase I from pig liver
Eur. J. Biochem.
183
661-669
1989
Bos taurus, Homo sapiens, Sus scrofa
brenda
Schweden, J.; Borgmann, C.; Legler, G.; Bause, E.
Characterization of calf liver glucosidase I and its inhibition by basic sugar analogs
Arch. Biochem. Biophys.
248
335-340
1986
Bos taurus
brenda
Boisson, M.; Gomord, V.; Audran, C.; Berger, N.; Dubreucq, B.; Granier, F.; Lerouge, P.; Faye, L.; Caboche, M.; Lepiniec, L.
Arabidopsis glucosidase I mutants reveal a critical role of N-glycan trimming in seed development
EMBO J.
20
1010-1019
2001
Arabidopsis thaliana
brenda
Dhanawansa, R.; Faridmoayer, A.; Van der Merwe, G.; Li, Y.X.; Scaman, C.H.
Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing alpha glucosidase I
Glycobiology
12
229-234
2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae AH22
brenda
Hakamata, W.; Muroi, M.; Nishio, T.; Oku, T.; Takatsuki, A.
Recognition properties of processing alpha-glucosidase I and alpha-glucosidase II
J. Carbohydr. Chem.
23
27-39
2004
Rattus norvegicus
-
brenda
Gillmor, C.S.; Poindexter, P.; Lorieau, J.; Palcic, M.M.; Somerville, C.
Alpha-glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
J. Cell. Biol.
156
1003-1013
2002
Arabidopsis thaliana (F4HTM3)
brenda
Faridmoayer, A.; Scaman, C.H.
An improved purification procedure for soluble processing alpha-glucosidase I from Saccharomyces cerevisiae overexpressing CWH41
Protein Expr. Purif.
33
11-18
2004
Saccharomyces cerevisiae
brenda
Tonozuka, T.; Uechi, A.; Mizuno, M.; Ichikawa, K.; Nishikawa, A.; Sakano, Y.
Crystallization and preliminary X-ray analysis of Escherichia coli K12 YgjK protein, a member of glycosyl hydrolase family 63
Acta Crystallogr. Sect. D
60
1284-1285
2004
Escherichia coli
brenda
Faridmoayer, A.; Scaman, C.H.
Truncations and functional carboxylic acid residues of yeast processing alpha-glucosidase I
Glycoconj. J.
24
429-437
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae AH22
brenda
Ruddock, L.W.; Molinari, M.
N-glycan processing in ER quality control
J. Cell Sci.
119
4373-4380
2006
Homo sapiens, Mus musculus
brenda
Saint-Jore-Dupas, C.; Nebenfuehr, A.; Boulaflous, A.; Follet-Gueye, M.L.; Plasson, C.; Hawes, C.; Driouich, A.; Faye, L.; Gomord, V.
Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway
Plant Cell
18
3182-3200
2006
Arabidopsis thaliana
brenda
McVie-Wylie, A.J.; Lee, K.L.; Qiu, H.; Jin, X.; Do, H.; Gotschall, R.; Thurberg, B.L.; Rogers, C.; Raben, N.; OCallaghan, M.; Canfield, W.; Andrews, L.; McPherson, J.M.; Mattaliano, R.J.
Biochemical and pharmacological characterization of different recombinant acid alpha-glucosidase preparations evaluated for the treatment of Pompe disease
Mol. Genet. Metab.
94
448-455
2008
Cricetulus griseus
brenda
Kurakata, Y.; Uechi, A.; Yoshida, H.; Kamitori, S.; Sakano, Y.; Nishikawa, A.; Tonozuka, T.
Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63
J. Mol. Biol.
381
116-128
2008
Escherichia coli
brenda
Zhu, Y.; Jiang, J.L.; Gumlaw, N.K.; Zhang, J.; Bercury, S.D.; Ziegler, R.J.; Lee, K.; Kudo, M.; Canfield, W.M.; Edmunds, T.; Jiang, C.; Mattaliano, R.J.; Cheng, S.H.
Glycoengineered Acid alpha-Glucosidase With Improved Efficacy at Correcting the Metabolic Aberrations and Motor Function Deficits in a Mouse Model of Pompe Disease
Mol. Ther.
17
954-963
2009
Homo sapiens
brenda
Chang, J.; Wang, L.; Ma, D.; Qu, X.; Guo, H.; Xu, X.; Mason, P.M.; Bourne, N.; Moriarty, R.; Gu, B.; Guo, J.T.; Block, T.M.
Novel imino sugar derivatives demonstrate potent antiviral activity against flaviviruses
Antimicrob. Agents Chemother.
53
1501-1508
2009
Bovine viral diarrhea virus 1, Dengue virus, West Nile virus
brenda
Frade-Perez, M.D.; Hernandez-Cervantes, A.; Flores-Carreon, A.; Mora-Montes, H.M.
Biochemical characterization of Candida albicans alpha-glucosidase I heterologously expressed in Escherichia coli
Antonie van Leeuwenhoek
98
291-298
2010
Candida albicans (Q2V621), Candida albicans
brenda
Boulaflous, A.; Saint-Jore-Dupas, C.; Herranz-Gordo, M.; Pagny-Salehabadi, S.; Plasson, C.; Garidou, F.; Kiefer-Meyer, M.; Ritzenthaler, C.; Faye, L.; Gomord, V.
Cytosolic N-terminal arginine-based signals together with a luminal signal target a type II membrane protein to the plant ER
BMC Plant Biol.
9
144
2009
Arabidopsis thaliana (F4HTM3)
brenda
Rawlings, A.; Lomas, H.; Pilling, A.; Lee, M.; Alonzi, D.; Rountree, J.; Jenkinson, S.; Fleet, G.; Dwek, R.; Jones, J.; Butters, T.
Synthesis and biological characterisation of novel N-alkyl-deoxynojirimycin glucosidase inhibitors
ChemBioChem
10
1101-1105
2009
Rattus norvegicus
brenda
Miyazaki, T.; Matsumoto, Y.; Matsuda, K.; Kurakata, Y.; Matsuo, I.; Ito, Y.; Nishikawa, A.; Tonozuka, T.
Heterologous expression and characterization of processing alpha-glucosidase I from Aspergillus brasiliensis ATCC 9642
Glycoconj. J.
28
563-571
2011
Aspergillus brasiliensis (G1UJA9), Aspergillus brasiliensis ATCC 9642 (G1UJA9)
brenda
Sadat, M.A.; Moir, S.; Chun, T.W.; Lusso, P.; Kaplan, G.; Wolfe, L.; Memoli, M.J.; He, M.; Vega, H.; Kim, L.J.; Huang, Y.; Hussein, N.; Nievas, E.; Mitchell, R.; Garofalo, M.; Louie, A.; Ireland, D.C.; Grunes, C.; Cimbro, R.; Patel, V.; Holzapfel, G.; Salahuddin, D.; Bristol, T.; Adams, D.; Marciano, B.E.
Glycosylation, hypogammaglobulinemia, and resistance to viral infections
N. Engl. J. Med.
370
1615-1625
2014
Homo sapiens
brenda
Wang, S.; Xu, Y.; Li, Z.; Zhang, S.; Lim, J.M.; Lee, K.O.; Li, C.; Qian, Q.; Jiang, d.e..A.; Qi, Y.
OsMOGS is required for N-glycan formation and auxin-mediated root development in rice (Oryza sativa L.)
Plant J.
78
632-645
2014
Oryza sativa
brenda
Miyazaki, T.; Ichikawa, M.; Iino, H.; Nishikawa, A.; Tonozuka, T.
Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8
J. Struct. Biol.
190
21-30
2015
Thermus thermophilus (Q5SJN0)
brenda