3.2.1.106: mannosyl-oligosaccharide glucosidase
This is an abbreviated version!
For detailed information about mannosyl-oligosaccharide glucosidase, go to the full flat file.
Word Map on EC 3.2.1.106
-
3.2.1.106
-
pompe
-
lysosomal
-
glycogen
-
infantile
-
n-linked
-
late-onset
-
cardiac
-
maltase
-
cardiomyopathy
-
mannose
-
myopathy
-
glycogenosis
-
castanospermine
-
infantile-onset
-
neuromuscular
-
mannosidase
-
alglucosidase
-
gsdii
-
ventilation
-
asparagine-linked
-
3.2.1.20
-
n-glycans
-
mannose-6-phosphate
-
high-mannose
-
glucosidases
-
1-deoxynojirimycin
-
swainsonine
-
acarbose
-
lipid-linked
-
limb-girdle
-
n-butyldeoxynojirimycin
-
isomaltose
-
analysis
-
cardiomegaly
-
endoglucosaminidase
-
deoxymannojirimycin
-
turanose
-
glycogen-storage
-
ventilator-free
-
alpha-glucoside
-
pharmacology
-
medicine
-
cardiorespiratory
-
ci-mpr
-
n-glycoproteins
-
pseudodeficiency
-
cation-independent
-
amyloglucosidase
- 3.2.1.106
- pompe
- lysosomal
- glycogen
-
infantile
-
n-linked
-
late-onset
- cardiac
- maltase
- cardiomyopathy
- mannose
- myopathy
- glycogenosis
- castanospermine
-
infantile-onset
- neuromuscular
-
mannosidase
-
alglucosidase
-
gsdii
-
ventilation
-
asparagine-linked
-
3.2.1.20
- n-glycans
- mannose-6-phosphate
-
high-mannose
- glucosidases
- 1-deoxynojirimycin
- swainsonine
- acarbose
-
lipid-linked
-
limb-girdle
- n-butyldeoxynojirimycin
- isomaltose
- analysis
- cardiomegaly
-
endoglucosaminidase
- deoxymannojirimycin
- turanose
-
glycogen-storage
-
ventilator-free
- alpha-glucoside
- pharmacology
- medicine
-
cardiorespiratory
-
ci-mpr
- n-glycoproteins
-
pseudodeficiency
-
cation-independent
- amyloglucosidase
Reaction
Synonyms
(Glc3)-glucosidase, acid alpha-glucosidase, alpha-glucosidase I, CHO-GAA, CWH41, Cwh41p, GAA, GCSI, Glc I, Glc3 oligosaccharide glucosidase, Glc3-glucosidase, Glc3-oligosaccharide glucosidase, Glc3-OS-glucosidase, Glc3Man9GlcNAc2 oligosaccharide glucosidase, Glc3Man9NAc2 oligosaccharide glucosidase, glucosidase 1, glucosidase I, glucosidase, mannosyloligosaccharide, glucosidase-1, glycoengineered acid alpha-glucosidase, HP-GAA, K12 YgjK protein, KNOPF, mannosyl-oligosaccharide glucosidase, mannosylglycerate hydrolase, MOGS, oxime-neo-rhGAA, PGI, processing alpha-glucosidase I, processing exoglucosidase I, processing glucosidase I, rhGAA, tgGAA, trimming enzyme I, trimming glucosidase I, Tt8MGH, YgjK
ECTree
3.2.1.106 mannosyl-oligosaccharide glucosidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.106 - mannosyl-oligosaccharide glucosidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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
-
-
?
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
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
-
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
-
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
-
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
-
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
?
-
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
?
-
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
?
-
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
-
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
-
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
-
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
-
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
-
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
?
-
-
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
?
-
-
p-nitrophenyl-beta-D-glucopyranoside: not a substrate
-
-
?
additional information
?
-
-
p-nitrophenyl-beta-D-glucopyranoside: not a substrate
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
p-nitrophenyl-beta-D-glucopyranoside: 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 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
?
-
-
also acts, more slowly, on the corresponding glycolipids and glycopeptides
-
-
?
additional information
?
-
-
p-nitrophenyl-alpha-D-glucopyranoside: 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
?
-
-
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
-
-
?
