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Information on EC 3.2.1.207 - mannosyl-oligosaccharide alpha-1,3-glucosidase
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EC Tree
3.2.1.207 mannosyl-oligosaccharide alpha-1,3-glucosidaseIUBMB Comments
This eukaryotic enzyme cleaves off sequentially the two alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
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Word Map
- 3.2.1.207
-
polycystic
- cyst
-
hepatocystin
-
cystogenesis
-
adpld
- polycystin-1
-
cholangiocytes
-
glucosidases
-
glc1man9glcnac2
-
glycan-processing
-
dnajb11
-
sec61b
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
prkcsh, ganab, giibeta, er glucosidase ii, alpha glucosidase ii, glucosidase ii beta-subunit, endoplasmic reticulum glucosidase ii, plant glucosidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glucosidase II
CTHT_0046400
CTHT_0064960
CWH41
endoplasmic reticulum glucosidase II
ER glucosidase II
GANAB
GII
GLS2
glucosidase II
GTB1
PRKCSH
-
-
-
-
ROT2
SPAC1002.03c
trimming glucosidase II
type II-like alpha-glucosidase
alpha-glucosidase II
-
-
-
-
CTHT_0046400
Thermochaetoides thermophila DSM 1495
G0SG42; G0S9M2
gene name, beta-subunit
-
CTHT_0064960
Thermochaetoides thermophila DSM 1495
G0SG42; G0S9M2
gene name, alpha-subunit
-
ER glucosidase II
-
-
-
-
GANAB
-
-
-
-
GTB1
-
-
-
-
GTB1
-
subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum
ROT2
-
-
-
-
trimming glucosidase II
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GlcMan9GlcNAc2-[protein] + H2O = Man9GlcNAc2-[protein] + beta-D-glucopyranose
(2)
-
-
-
Glc2Man9GlcNAc2-[protein] + H2O = GlcMan9GlcNAc2-[protein] + beta-D-glucopyranose
Glc2Man9GlcNAc2 + H2O = Man9GlcNAc2 + glucose
-
Glc2Man9GlcNAc2-[protein] + H2O = GlcMan9GlcNAc2-[protein] + beta-D-glucopyranose
Glc2Man9GlcNAc2 + H2O = Man9GlcNAc2 + glucose
-
Glc2Man9GlcNAc2-[protein] + H2O = GlcMan9GlcNAc2-[protein] + beta-D-glucopyranose
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
-
remove second glucose residue of glycans, incubation time 10 min at 37°C
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SYSTEMATIC NAME
IUBMB Comments
Glc2Man9GlcNAc2-[protein] 3-alpha-glucohydrolase (configuration-inverting)
This eukaryotic enzyme cleaves off sequentially the two alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
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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
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucopyranose
-
high affinity
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
4-methylumbelliferyl-alpha-D-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc + H2O
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc + D-glucose
-
preferred substrate
-
-
?
D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc + H2O
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc + D-glucose
-
less than 10of the activity with alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc
-
-
?
D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc + H2O
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc + D-glucose
-
less than 5% of the activity with alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc
-
-
?
Glc2Man9GlcNAc2 (G2M9)-protein + H2O
?
-
glucosidase II plays a key role in glycoprotein processing in the endoplasmic reticulum. This enzyme trims two alpha-1,3-linked glucose residues, Glcalpha1,3Glc (cleavage 1) and Glcalpha1,3Man (cleavage 2) from high-mannose type Glc2Man9GlcNAc2 (G2M9)-proteins. A crowded milieu that contains bovine serum albumin greatly enhances the second trimming step (cleavage 2), which deglucosylates Glc1Man9GlcNAc2, but not the first trimming step (cleavage 1), which removes the terminal glucose residue from Glc2Man9GlcNAc2
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + beta-D-glucopyranose
-
-
-
-
?
GlcMan9GlcNAc + H2O
Man9GlcNAc + D-glucose
-
enzyme expression in Schizosaccharomyces pombe mutants either glucosidase II-alpha or both glucosidase II-alpha and -beta minus after cells transformed with the cDNA sequences of Arabidopsis thaliana glucosidase II-alpha encoding gene
-
?
GlcNAcalpha(1->3)GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
GlcNAcalpha(1->3)GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-Gly-BODIPY + H2O
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-Gly-BODIPY + D-glucose
-
-
-
-
?
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-Gly-BODIPY + H2O
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-Gly-BODIPY + D-glucose
-
-
-
-
?
mannose oligosaccharide + H2O
?
-
substrate specificity of wild-type and mutant enzymes with different mannose oligosaccharides, overview
-
-
?
p-nitrophenyl-2-deoxy-alpha-D-glucopyranoside + H2O
p-nitrophenol + 2-deoxy-alpha-D-glucose
-
very effective substrate, other deoxy derivatives are not hydrolyzed
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-methylumbellyferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
?
4-methylumbellyferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
cleavage by the single alpha-subunit, the beta-subunit is not required for activity
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
the GIIbeta subunit is not required for GIIalpha activity toward the substrate
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
the GIIbeta subunit is not required for GIIalpha activity toward the substrate
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
Glc2Man9GlcNAc2 + 2 H2O
Man9GlcNAc2 + 2 D-glucose
-
enzyme expression in Schizosaccharomyces pombe mutants either glucosidase II-alpha or both glucosidase II-alpha and -beta minus after cells transformed with the cDNA sequences of Arabidopsis thaliana glucosidase II-alpha encoding gene
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
synthetic methotrexate-coupled glycan substrate, G1M9-MTX
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
synthetic methotrexate-coupled glycan substrate, G1M9-MTX
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
i.e. G1M9, usage of synthetic methotrexate-coupled glycan substrate, G1M9-MTX
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
i.e. G1M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
i.e. G1M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucose
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
involved in the Calnexin Cycle
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
processing of asparagine-linked oligosaccharides
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
removal of glucose residues allows newly synthesized glycoproteins to interact with calnexin and calreticulin, that are part of the chaperone mechanism
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
synthetic methotrexate-coupled glycan substrate, G2M9-MTX
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
synthetic methotrexate-coupled glycan substrate, G2M9-MTX
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
G2M9, usage of synthetic methotrexate-coupled glycan substrate, G2M9-MTX
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
i.e. G2M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
i.e. G2M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
GlcMan9GlcNAc2-pyridylamine + H2O
Man9GlcNAc2-pyridylamine + D-glucose
-
-
-
?
GlcMan9GlcNAc2-pyridylamine + H2O
Man9GlcNAc2-pyridylamine + D-glucose
-
-
-
?
GlcNAcalpha(1->3)GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
-
-
-
-
?
GlcNAcalpha(1->3)GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
-
-
-
-
?
GlcNAcalpha(1->3)GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
-
-
-
-
?
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
-
-
-
-
?
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
-
-
-
-
?
GlcNAcalpha(1->3)Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + D-glucose
-
-
-
-
?
maltose + H2O
alpha-D-glucose + 1,5-anhydrofructose
-
-
1,5-anhydrofructose is produced as a side product
-
?
maltose + H2O
alpha-D-glucose + 1,5-anhydrofructose
-
-
1,5-anhydrofructose is produced as a side product
-
?
nigerose + H2O
?
-
preferred substrate over kojibiose, trehalose, and isomaltose (clear preference of the enzyme for the alpha1,3 bond)
-
-
?
nigerose + H2O
?
-
preferred substrate over kojibiose, trehalose, and isomaltose (clear preference of the enzyme for the alpha1,3 bond)
-
-
?
additional information
?
-
-
glucosidase II is a glycoprotein-processing enzyme that successively cleaves two alpha1,3-linked glucose residues from N-linked oligosaccharides in the endoplasmic reticulum
-
-
?
additional information
?
-
-
the mutant lacking the beta-subunit is inactive with both Glc2Man9GlcNAc2 and GlcMan9GlcNAc2
-
-
?
additional information
?
-
-
glucosidase II is a glycoprotein-processing enzyme that successively cleaves two alpha1,3-linked glucose residues from N-linked oligosaccharides in the endoplasmic reticulum
-
-
?
additional information
?
-
-
the mutant lacking the beta-subunit is inactive with both Glc2Man9GlcNAc2 and GlcMan9GlcNAc2
-
-
?
additional information
?
-
no activity of the single alpha-subunit with N-glycan, the enzyme complex of the alpha- and beta-subunits is required for N-glycan cleavage
-
-
?
additional information
?
-
no activity of the single alpha-subunit with N-glycan, the enzyme complex of the alpha- and beta-subunits is required for N-glycan cleavage
-
-
?
additional information
?
-
involved in early glycoprotein biogenesis, catalyzes the hydrolysis of two alpha-1,3-linked glucose residues present on all Asn-linked precursor oligosaccharides
-
-
?
additional information
?
-
involved in early glycoprotein biogenesis, catalyzes the hydrolysis of two alpha-1,3-linked glucose residues present on all Asn-linked precursor oligosaccharides
-
-
?
additional information
?
-
-
glucosidase II is a glycan-processing enzyme that trims two alpha1,3-linked glucose residues from N-glycan on newly synthesized glycoproteins
-
-
?
additional information
?
-
-
the isolated beta-subunit domain GIIbeta-MRH binds to high-mannose-type glycans in HeLaS3 cells, most strongly to the glycans with the alpha1,2-linked mannobiose structure, overview
-
-
?
additional information
?
-
-
Catalyzes the hydrolysis of the inner two alpha-1,3-linked glucose residues present in all N-linked immature oligosaccharides, associates with and glycosylates the protein CD45, possible role in CD45 regulation
-
-
?
additional information
?
-
-
involved in early glycoprotein biogenesis, catalyzes the hydrolysis of two alpha-1,3-linked glucose residues present on all Asn-linked precursor oligosaccharides
-
-
?
additional information
?
-
the catalytic enzyme alpha subunit, with the help of mannose 6-phosphate receptor homology domain of the beta-subunit, sequentially hydrolyzes two alpha1-3-linked glucose residues in the second step of N-linked oligosaccharide-mediated protein folding
-
-
?
additional information
?
-
the catalytic enzyme alpha subunit, with the help of mannose 6-phosphate receptor homology domain of the beta-subunit, sequentially hydrolyzes two alpha1-3-linked glucose residues in the second step of N-linked oligosaccharide-mediated protein folding
-
-
?
additional information
?
-
-
kinetic model for the interaction of glucosidase with calnexin/calreticulin
-
-
?
additional information
?
-
-
the enzyme heterodimer is required to efficiently deglucosylate the physiological substrates G2M9 and G1M9
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-
?
additional information
?
-
-
the interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta with mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement
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-
?
additional information
?
-
-
the GTB1 subunit of glucosidase II is required for glycoprotein processing in the endoplasmic reticulum, specifically required for the final glucose-trimming event during normal glycoprotein processing
-
-
?
additional information
?
-
-
the enzyme heterodimer is required to efficiently deglucosylate the physiological substrates G2M9 and G1M9
-
-
?
additional information
?
-
-
the interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta with mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement
-
-
?
additional information
?
-
-
interaction of the beta-subunit MRH domain with mannosyl-alpha-(1,2)-mannose, mannose 6-phosphate, mannosyl-N-acetylglucsamine, or glucose 6-phosphate, ligand binding structures, overview
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-
?
additional information
?
-
enzyme hydrolyzes alpha-(1->3)- and also alpha-(1->2)-, alpha-(1->4)-, and alpha-(1->6)-glucosidic linkages, and 4-nitrophenyl alpha-D-glucoside
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-
?
additional information
?
-
enzyme hydrolyzes alpha-(1->3)- and also alpha-(1->2)-, alpha-(1->4)-, and alpha-(1->6)-glucosidic linkages, and 4-nitrophenyl alpha-D-glucoside
-
-
?
additional information
?
-
-
the enzyme is involved in the processing of protein-linked N-glycans in the endoplasmic reticulum of filamentous fungi
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-
?
additional information
?
-
-
the enzyme is involved in the processing of protein-linked N-glycans in the endoplasmic reticulum of filamentous fungi
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-
?
additional information
?
-
-
deletion of the glucosidase II gene in Trypanosoma brucei reveals novel N-glycosylation mechanisms in the biosynthesis of variant surface glycoprotein
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-
?
additional information
?
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-
endoplasmic reticulum glucosidase II is required for pathogenicity of Ustilago maydis
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-
?
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NATURAL SUBSTRATE
NATURAL 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
Glc2Man9GlcNAc2 (G2M9)-protein + H2O
?
-
glucosidase II plays a key role in glycoprotein processing in the endoplasmic reticulum. This enzyme trims two alpha-1,3-linked glucose residues, Glcalpha1,3Glc (cleavage 1) and Glcalpha1,3Man (cleavage 2) from high-mannose type Glc2Man9GlcNAc2 (G2M9)-proteins. A crowded milieu that contains bovine serum albumin greatly enhances the second trimming step (cleavage 2), which deglucosylates Glc1Man9GlcNAc2, but not the first trimming step (cleavage 1), which removes the terminal glucose residue from Glc2Man9GlcNAc2
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
involved in the Calnexin Cycle
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
processing of asparagine-linked oligosaccharides
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
removal of glucose residues allows newly synthesized glycoproteins to interact with calnexin and calreticulin, that are part of the chaperone mechanism
-
-
?
GlcMan9GlcNAc2 + H2O