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Information on EC 3.2.1.207 - mannosyl-oligosaccharide alpha-1,3-glucosidase
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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
-
sec61b
-
glycan-processing
-
dnajb11
-
glc1man9glcnac2
-
glucosidases
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
alpha glucosidase II, alpha-glucosidase II, CTHT_0046400, CTHT_0064960, CWH41, endoplasmic reticulum glucosidase II, ER glucosidase II, G-II, GANAB, GAS2, 
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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
-
-
-
-
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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PATHWAY SOURCE
PATHWAYS
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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
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + 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
-
?
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 + 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
-
-
?
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
?
-
-
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
-
-
?
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
?
-
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
-
-
?
additional information
?
-
-
the enzyme is involved in the processing of protein-linked N-glycans in the endoplasmic reticulum of filamentous fungi
-
-
?
additional information
?
-
-
deletion of the glucosidase II gene in Trypanosoma brucei reveals novel N-glycosylation mechanisms in the biosynthesis of variant surface glycoprotein
-
-
?
additional information
?
-
-
endoplasmic reticulum glucosidase II is required for pathogenicity of Ustilago maydis
-
-
?
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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
-
-
?
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
?
-
-
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
?
-
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
?
-
-
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 enzyme heterodimer is required to efficiently deglucosylate the physiological substrates G2M9 and G1M9
-
-
?
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 enzyme is involved in the processing of protein-linked N-glycans in the endoplasmic reticulum of filamentous fungi
-
-
?
additional information
?
-
-
the enzyme is involved in the processing of protein-linked N-glycans in the endoplasmic reticulum of filamentous fungi
-
-
?
additional information
?
-
-
deletion of the glucosidase II gene in Trypanosoma brucei reveals novel N-glycosylation mechanisms in the biosynthesis of variant surface glycoprotein
-
-
?
additional information
?
-
-
endoplasmic reticulum glucosidase II is required for pathogenicity of Ustilago maydis
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S,2R,3R,4R)-4-(hydroxymethyl)-5-[5-([(2R)-2,5,7,8-tetramethyl-2-[(4R,8R)-4,8,12-trimethyltridecyl]-3,4-dihydro-2H-chromen-6-yl]oxy)pentyl]cyclohexane-1,2,3-triol
-
inhibitor affects only myeloid lineage immune cells
(1S,2S,3R,6S)-6-[[(2R,3S,4S,5R,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-methoxyoxan-4-yl]amino]-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol
-
valienamine-derived N1->3-linked pseudosaccharide
(1S,2S,3R,6S)-6-[[(2R,3S,4S,5S,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-methoxyoxan-4-yl]amino]-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol
-
valienamine-derived N1->3-linked pseudosaccharide
1-deoxynojirimycin
-
more specific inhibitor of alpha-glucosidase II than of alpha-glucosidase I
2,6-dideoxy-2,6-imino-7-O-(beta-D-glucopyranosyl)-D-glycero-L-glucoheptitol
-
MDL
2,6-dideoxy-2,6-imino-7-O-(beta-D-glucopyranosyl)-D-glycero-L-glucoheptitol
-
-
bromoconduritol
-
binds to the low- but not high-affinity site for maltose and p-nitrophenyl-alpha-D-glucoside
bromoconduritol
-
i.e. 6-bromo-3,4,5-trihydroxycyclohex-1-ene. In the presence of 0.3 mM bromoconduritol the cleavage-2 is strongly inhibited (the consumption of Glc1Man9GlcNAc2 is less than 10% even after 24 h). The consumption of Glc2Man9GlcNAc2 is about 20% after 1 h, while that in the absence of bromoconduritol is about 70%. For the cleavage-1, the extent of inhibition increases as the preincubation time elongates. The binding of bromoconduritol to glucosidase-II is an irreversible and slow process
bromoconduritol
-
i.e. 6-bromo-3,4,5-trihydroxycyclohex-1-ene, inhibits both cleavage activities of glucosidase II. The inhibitory activity toward cleavage-2, i.e. cleavage of the second of two alpha1->3 linked Glc residues, is 6fold higher than that toward cleavage-1, i.e. removal of the penultimate Glc residue to generate Glc1Man9GlcNAc2. Inhibition is irreversible
additional information
the enzyme from silkworm is not sensitive to the alpha-glucosidase inhibitors from mulberry leaves; the enzyme from silkworm is not very sensitive to the alpha-glucosidase inhibitors from mulberry leaves
-
additional information
the enzyme from silkworm is not sensitive to the alpha-glucosidase inhibitors from mulberry leaves; the enzyme from silkworm is not very sensitive to the alpha-glucosidase inhibitors from mulberry leaves
-
additional information
NaCl, NaH2PO4, Na2SO4, NaNO3, KCl, MgCl2, or EDTA up to 40 mM do not affect activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calreticulin
-
75 micromol, conversion of Glc2Man7-residue to Glc1Man7-residue
-
calreticulin
-
in higher concentrations faster hydrolysis of Glc2Man9-residue
-
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
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway.
Carcinogenesis
Publisher Correction: PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway.
Carcinoma
Glucosidase II beta subunit (GluII?) plays a role in autophagy and apoptosis regulation in lung carcinoma cells in a p53-dependent manner.
Carcinoma
PRKCSH GAG trinucleotide repeat is a mutational target in gastric carcinomas with high-level microsatellite instability.
Cysts
Abnormal hepatocystin caused by truncating PRKCSH mutations leads to autosomal dominant polycystic liver disease.
Cysts
An in vitro model of polycystic liver disease using genome-edited human inducible pluripotent stem cells.
Cysts
Boy with autosomal recessive polycystic kidney and autosomal dominant polycystic liver disease.
Cysts
Chromosomal abnormalities in hepatic cysts point to novel polycystic liver disease genes.
Cysts
Cysts of PRKCSH mutated polycystic liver disease patients lack hepatocystin but express Sec63p.
Cysts
Extensive mutational analysis of PRKCSH and SEC63 broadens the spectrum of polycystic liver disease.
Cysts
Ganab Haploinsufficiency Does Not Cause Polycystic Kidney Disease or Polycystic Liver Disease in Mice.
Cysts
Hepatocystin is not secreted in cyst fluid of hepatocystin mutant polycystic liver patients.
Cysts
Liver cyst gene knockout in cholangiocytes inhibits cilium formation and Wnt signaling.
Cysts
Loss of heterozygosity is present in SEC63 germline carriers with polycystic liver disease.
Cysts
Mutations in GANAB, Encoding the Glucosidase II? Subunit, Cause Autosomal-Dominant Polycystic Kidney and Liver Disease.
Cysts
PRKCSH Genetic Mutation Was Not Found in Taiwanese Patients with Polycystic Liver Disease.
Cysts
PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation.
Cysts
Secondary, Somatic Mutations Might Promote Cyst Formation in Patients with Autosomal-Dominant Polycystic Liver Disease.
Diabetes Complications
DDOST, PRKCSH and LGALS3, which encode AGE-receptors 1, 2 and 3, respectively, are not associated with diabetic nephropathy in type 1 diabetes.
Diabetes Mellitus, Type 1
DDOST, PRKCSH and LGALS3, which encode AGE-receptors 1, 2 and 3, respectively, are not associated with diabetic nephropathy in type 1 diabetes.
Diabetic Nephropathies
DDOST, PRKCSH and LGALS3, which encode AGE-receptors 1, 2 and 3, respectively, are not associated with diabetic nephropathy in type 1 diabetes.
Kidney Diseases
Novel mutations of PKD genes in Chinese patients suffering from autosomal dominant polycystic kidney disease and seeking assisted reproduction.
Kidney Diseases
Recent advances of mTOR inhibitors use in autosomal dominant polycystic kidney disease: is the road still open?
Liver Diseases
A genetic interaction network of five genes for human polycystic kidney and liver diseases defines polycystin-1 as the central determinant of cyst formation.
Liver Diseases
A noncoding variant in GANAB explains isolated polycystic liver disease (PCLD) in a large family.
Liver Diseases
Abnormal hepatocystin caused by truncating PRKCSH mutations leads to autosomal dominant polycystic liver disease.
Liver Diseases
An interaction between human Sec63 and nucleoredoxin may provide the missing link between the SEC63 gene and polycystic liver disease.
Liver Diseases
Chromosomal abnormalities in hepatic cysts point to novel polycystic liver disease genes.
Liver Diseases
Cysts of PRKCSH mutated polycystic liver disease patients lack hepatocystin but express Sec63p.
Liver Diseases
Expanding the variability of the ADPKD-GANAB clinical phenotype in a family of Italian ancestry.
Liver Diseases
Extensive mutational analysis of PRKCSH and SEC63 broadens the spectrum of polycystic liver disease.
Liver Diseases
Ganab Haploinsufficiency Does Not Cause Polycystic Kidney Disease or Polycystic Liver Disease in Mice.
Liver Diseases
Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease.
Liver Diseases
Hepatocystin is not secreted in cyst fluid of hepatocystin mutant polycystic liver patients.
Liver Diseases
Large Deletions in GANAB and SEC63 Explain 2 Cases of Polycystic Kidney and Liver Disease.
Liver Diseases
Liver cyst gene knockout in cholangiocytes inhibits cilium formation and Wnt signaling.
Liver Diseases
Mutations in GANAB, Encoding the Glucosidase II? Subunit, Cause Autosomal-Dominant Polycystic Kidney and Liver Disease.
Liver Diseases
Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease.
Liver Diseases
N-glycosylation determines the abundance of the transient receptor potential channel TRPP2.
Liver Diseases
Polycystic liver disease is a disorder of cotranslational protein processing.
Liver Diseases
PRKCSH Genetic Mutation Was Not Found in Taiwanese Patients with Polycystic Liver Disease.
Liver Diseases
PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation.
Liver Diseases
Secondary and tertiary structure modeling reveals effects of novel mutations in polycystic liver disease genes PRKCSH and SEC63.
Liver Diseases
Secondary, Somatic Mutations Might Promote Cyst Formation in Patients with Autosomal-Dominant Polycystic Liver Disease.
Liver Diseases
Severe Polycystic Liver Disease Is Not Caused by Large Deletions of the PRKCSH Gene.
Liver Diseases
Whole-exome sequencing reveals LRP5 mutations and canonical Wnt signaling associated with hepatic cystogenesis.
Lymphatic Metastasis
Acidic microenvironment plays a key role in human melanoma progression through a sustained exosome mediated transfer of clinically relevant metastatic molecules.
mannosyl-oligosaccharide alpha-1,3-glucosidase deficiency
An in vitro model of polycystic liver disease using genome-edited human inducible pluripotent stem cells.
Migraine Disorders
A 3-Mb region for the familial hemiplegic migraine locus on 19p13.1-p13.2: exclusion of PRKCSH as a candidate gene. Dutch Migraine Genetic Research Group.
Migraine with Aura
A 3-Mb region for the familial hemiplegic migraine locus on 19p13.1-p13.2: exclusion of PRKCSH as a candidate gene. Dutch Migraine Genetic Research Group.
Neoplasm Metastasis
Acidic microenvironment plays a key role in human melanoma progression through a sustained exosome mediated transfer of clinically relevant metastatic molecules.
Neoplasms
A five-mRNA signature associated with post-translational modifications can better predict recurrence and survival in cervical cancer.
Neoplasms
PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway.
Polycystic Kidney Diseases
Chromosomal abnormalities in hepatic cysts point to novel polycystic liver disease genes.
Polycystic Kidney Diseases
Expanding the variability of the ADPKD-GANAB clinical phenotype in a family of Italian ancestry.
Polycystic Kidney Diseases
GANAB and PKD1 Variations in a 12 Years Old Female Patient With Early Onset of Autosomal Dominant Polycystic Kidney Disease.
Polycystic Kidney Diseases
Ganab Haploinsufficiency Does Not Cause Polycystic Kidney Disease or Polycystic Liver Disease in Mice.
Polycystic Kidney Diseases
Large Deletions in GANAB and SEC63 Explain 2 Cases of Polycystic Kidney and Liver Disease.
Polycystic Kidney Diseases
Mutational screening of PKD1 and PKD2 in Indian ADPKD patients identified 95 genetic variants.
Polycystic Kidney Diseases
Mutations in GANAB, Encoding the Glucosidase II? Subunit, Cause Autosomal-Dominant Polycystic Kidney and Liver Disease.
Polycystic Kidney Diseases
Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease.
Polycystic Kidney Diseases
Novel mutations of PKD genes in Chinese patients suffering from autosomal dominant polycystic kidney disease and seeking assisted reproduction.
Polycystic Kidney Diseases
PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation.
Polycystic Kidney Diseases
Recent advances of mTOR inhibitors use in autosomal dominant polycystic kidney disease: is the road still open?
Polycystic Kidney, Autosomal Dominant
Chromosomal abnormalities in hepatic cysts point to novel polycystic liver disease genes.
Polycystic Kidney, Autosomal Dominant
Expanding the variability of the ADPKD-GANAB clinical phenotype in a family of Italian ancestry.
Polycystic Kidney, Autosomal Dominant
GANAB and PKD1 Variations in a 12 Years Old Female Patient With Early Onset of Autosomal Dominant Polycystic Kidney Disease.
Polycystic Kidney, Autosomal Dominant
Ganab Haploinsufficiency Does Not Cause Polycystic Kidney Disease or Polycystic Liver Disease in Mice.
Polycystic Kidney, Autosomal Dominant
Mutational screening of PKD1 and PKD2 in Indian ADPKD patients identified 95 genetic variants.
Polycystic Kidney, Autosomal Dominant
Mutations in GANAB, Encoding the Glucosidase II? Subunit, Cause Autosomal-Dominant Polycystic Kidney and Liver Disease.
Polycystic Kidney, Autosomal Dominant
Novel GANAB variants associated with polycystic liver disease.
Polycystic Kidney, Autosomal Dominant
Novel mutations of PKD genes in Chinese patients suffering from autosomal dominant polycystic kidney disease and seeking assisted reproduction.
Polycystic Kidney, Autosomal Dominant
Polycystic Kidney Disease without an Apparent Family History.
Polycystic Kidney, Autosomal Dominant
Prevalence Estimates of Polycystic Kidney and Liver Disease by Population Sequencing.
Polycystic Kidney, Autosomal Dominant
PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation.
Polycystic Kidney, Autosomal Dominant
Recent advances of mTOR inhibitors use in autosomal dominant polycystic kidney disease: is the road still open?
Polycystic Kidney, Autosomal Dominant
Updated Canadian Expert Consensus on Assessing Risk of Disease Progression and Pharmacological Management of Autosomal Dominant Polycystic Kidney Disease.
Situs Inversus
PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation.
Spinal Cord Injuries
Down-regulating Circular RNA Prkcsh suppresses the inflammatory response after spinal cord injury.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
4-Methylumbelliferyl-alpha-D-glucopyranoside
-
in 25 mM HEPES buffer, pH 7.2, at 37°C
2.37
4-nitrophenyl alpha-D-glucopyranoside
recombinant enzyme, pH 6,5, 37°C
2.82
4-nitrophenyl alpha-D-glucopyranoside
recombinant enzyme, pH 6,5, 37°C
0.49
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-tyrosine
-
Glc2Man7GlcNAc2
15 - 23
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-tyrosine
-
Glc2Man9GlcNAc2
0.5
p-nitrophenyl-alpha-D-glucopyranoside
pH 7.5, 37°C, alpha1-beta complex
0.52
p-nitrophenyl-alpha-D-glucopyranoside
pH 7.5, 37°C, alpha2-beta complex
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008763
epicatechin gallate
-
37°C, hydrolysis of 4-methylumbelliferyl-alpha-D-glucoside
0.0131
epicatechin gallate
-
37°C, hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
0.06815
epigallocatechin
-
37°C, hydrolysis of 4-methylumbelliferyl-alpha-D-glucoside
0.07599
epigallocatechin
-
37°C, hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
0.02948
epigallocatechin gallate
-
37°C, hydrolysis of 4-methylumbelliferyl-alpha-D-glucoside
0.03281
epigallocatechin gallate
-
37°C, hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
0.07062
gallocatechin
-
37°C, hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
0.07893
gallocatechin
-
37°C, hydrolysis of 4-methylumbelliferyl-alpha-D-glucoside
0.002027
gallocatechin gallate
-
37°C, hydrolysis of 4-methylumbelliferyl-alpha-D-glucoside
0.002545
gallocatechin gallate
-
37°C, hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
0.002247
N-butyldeoxynojirimycin
-
37°C, hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
0.00519
N-butyldeoxynojirimycin
-
37°C, hydrolysis of 4-methylumbelliferyl-alpha-D-glucoside
0.03628
propyl gallate
-
37°C, hydrolysis of 4-methylumbelliferyl-alpha-D-glucoside
0.04312
propyl gallate
-
37°C, hydrolysis of 4-nitrophenyl alpha-D-glucopyranoside
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
(1S,2R,3R,4R)-4-(hydroxymethyl)-5-[5-([(2R)-2,5,7,8-tetramethyl-2-[(4R,8R)-4,8,12-trimethyltridecyl]-3,4-dihydro-2H-chromen-6-yl]oxy)pentyl]cyclohexane-1,2,3-triol
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.072 - 0.143
(1S,2S,3R,6S)-6-[[(2R,3S,4S,5R,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-methoxyoxan-4-yl]amino]-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol
0.236
(1S,2S,3R,6S)-6-[[(2R,3S,4S,5S,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-methoxyoxan-4-yl]amino]-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol
Rattus norvegicus
-
cleavage-2, pH not specified in the publication, temperature not specified in the publication
0.072
(1S,2S,3R,6S)-6-[[(2R,3S,4S,5R,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-methoxyoxan-4-yl]amino]-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol
Rattus norvegicus
-
cleavage-1, pH not specified in the publication, temperature not specified in the publication
0.143
(1S,2S,3R,6S)-6-[[(2R,3S,4S,5R,6S)-3,5-dihydroxy-2-(hydroxymethyl)-6-methoxyoxan-4-yl]amino]-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol
Rattus norvegicus
-
cleavage-2, pH not specified in the publication, temperature not specified in the publication
0.0708
1,4-dideoxy-1,4-imino-D-arabinitol
Spodoptera frugiperda
recombinant enzyme, pH 6,5, 37°C
0.5102
1,4-dideoxy-1,4-imino-D-arabinitol
Bombyx mori
recombinant enzyme, pH 6,5, 37°C
0.00024
1-deoxynojirimycin
Sporothrix schenckii
-
using nigerose as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.00045
1-deoxynojirimycin
Sporothrix schenckii
-
using 4-methylumbelliferyl-alpha-D-glucopyranoside as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.00065
1-deoxynojirimycin
Sporothrix schenckii
-
using kojibiose as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.00074
1-deoxynojirimycin
Sporothrix schenckii
-
using maltose as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.041
bromoconduritol
Rattus norvegicus
-
inhibitory activity of inhibitor against the cleavage-2 reaction, in 10 mM HEPES (pH 7.4), at 37°C
0.2616
bromoconduritol
Rattus norvegicus
-
inhibitory activity of inhibitor against the cleavage-1 reaction, in 10 mM HEPES (pH 7.4), at 37°C
0.0011
castanospermine
Rattus norvegicus
-
inhibitory activity of inhibitor against the cleavage-2 reaction, in 10 mM HEPES (pH 7.4), at 37°C
0.0013
castanospermine
Rattus norvegicus
-
inhibitory activity of inhibitor against the cleavage-1 reaction, in 10 mM HEPES (pH 7.4), at 37°C
0.00145
castanospermine
Sporothrix schenckii
-
using 4-methylumbelliferyl-alpha-D-glucopyranoside as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.0032
castanospermine
Sporothrix schenckii
-
using nigerose as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.004
castanospermine
Sporothrix schenckii
-
using kojibiose as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.0068
castanospermine
Sporothrix schenckii
-
using maltose as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.00082
deoxynojirimycin
Rattus norvegicus
-
inhibitory activity of inhibitor against the cleavage-1 reaction, in 10 mM HEPES (pH 7.4), at 37°C
0.0112
deoxynojirimycin
Rattus norvegicus
-
inhibitory activity of inhibitor against the cleavage-2 reaction, in 10 mM HEPES (pH 7.4), at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0535
-
soluble enzyme extract, using 4-methylumbelliferyl-alpha-D-glucopyranoside as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
0.457
-
after 8.5fold purification, using 4-methylumbelliferyl-alpha-D-glucopyranoside as substrate, in 25 mM HEPES buffer, pH 7.2, at 37°C
4.53
4.65
4.53
recombinant enzyme, pH 6,5, 37°C, substrate 4-nitrophenyl alpha-D-glucopyranoside
4.53
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 6.5, 37°C
4.65
recombinant enzyme, pH 6,5, 37°C, substrate 4-nitrophenyl alpha-D-glucopyranoside
4.65
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 6.5, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.5 - 7
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
G0SG42 i.e. alpha-subunit, G0S9M2 i.e. beta-subunit
G0SG42; G0S9M2
UniProt
brenda
G0SG42 i.e. alpha-subunit, G0S9M2 i.e. beta-subunit
G0SG42; G0S9M2
UniProt
brenda
PSL4 and PSL5 encode for the beta- and alpha-subunit, respectively
-
-
brenda
L8B8U1 i.e. alpha subunit, L8B6C5 i.e. beta subunit
UniProt
brenda
two isoforms derived by alternative spicing, isofoms 2 contains a 22 amino acid insert
-
-
brenda
alpha1 isofrom of the alpha subunit, isoforms are formed by alternative splicing
SwissProt
brenda
alpha2 isoform of the alpha subunit, contains a 66 bp insert, isoforms are formed by alternative splicing
SwissProt
brenda
two isoforms derived by alternative spicing, isofoms 2 contains a 22 amino acid insert
-
-
brenda
two isoforms derived by alternative spicing, isofoms 2 contains a 22 amino acid insert
-
-
brenda
-
136899, 136901, 136904, 136905, 136910, 136912, 136914, 136915, 136917, 136919, 654580, 655677, 656338, 663990, 680378, 680700, 690899, 709871, 714044, 714414, 744210, 744497, 744498
-
-
brenda
two isoforms derived by alternative spicing, isofoms 2 contains a 22 amino acid insert
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
and larva, lower transcript expression level than in larvae and pupae
brenda
additional information
tissue-specific expression pattern of the enzyme, overview
brenda
-
-
136901, 136904, 136905, 136910, 136912, 136914, 136917, 646733, 654580, 655677, 656338, 663990, 680378, 680700, 690899, 709871, 714044, 714414, 744497, 744498
brenda
mRNA level and enzyme activity reach its peak level in the mid- or late lactation stages, like other N-glycosylation enzymes, and shows an up-regulation of 2.5-4fold at mid- to late lactation
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
in most species the endoplasmic reticulum localization is mediated by the glucosidase II-beta subunit
brenda
the soluble alpha subunit is retained in the endoplasmic reticulum through its interaction with the HDEL-containing beta subunit
brenda
-
the soluble alpha subunit is retained in the endoplasmic reticulum through its interaction with the HDEL-containing beta subunit
-
brenda
-
50% of total enzyme activity in a mixed membrane fraction
brenda
-
50% of total enzyme activity in a mixed membrane fraction
-
brenda
additional information
the enzyme has a signal peptide in the N-terminus
-
brenda
additional information
the enzyme has a signal peptide in the N-terminus
-
brenda
additional information
-
the enzyme contains a signal peptide (first 23 amino acids) sequence
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme contains a glycoside hydrolase family 31 motif containing the conserved WXDMNE sequence, which is essential for enzymatic activity
malfunction
-
loss-of-function in the Arabidopsis thaliana glucosidaseII beta-subunit gene confers an polypeptide elf18-insensitive phenotype
metabolism
-
glucosidase-II has a promiscuous activity as a broad specificity hexosidase
physiological function
additional information
physiological function
-
alpha- and beta-subunits of endoplasmic reticulum resident glucosidase II are essential for stable accumulation and quality control of the elf18 receptor EFR but not the flg22 receptor FLS2, overview. Subunit GIIalpha mediates the catalytic activity of the enzyme whereas subunit GIIbeta directly interacts with and holds GIIalpha in the ER through its ER retention signal. Subunit GIIbeta is required for EFR-mediated anthocyanin repression
physiological function
-
glucosidase II is a glycan-processing enzyme that trims two alpha1,3-linked glucose residues from N-glycan on newly synthesized glycoproteins. Trimming of the first alpha1,3-linked glucose from Glc2Man9GlcNAc2 is important for a glycoprotein to interact with calnexin/calreticulin, and cleavage of the innermost glucose from GlcMan9GlcNAc2 sets glycoproteins free from the CNX/CRT cycle and allows them to proceed to the Golgi apparatus
physiological function
-
glucosidase II plays a key role in glycoprotein biogenesis in the endoplasmic reticulum. It is responsible for the sequential removal of the two innermost glucose residues from the glycan, Glc3Man9GlcNAc2, transferred to Asn residues in proteins. The enzyme participates in the calnexin/calreticulin cycle, it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
physiological function
-
glucosidase II plays a key role in glycoprotein biogenesis in the endoplasmic reticulum. It is responsible for the sequential removal of the two innermost glucose residues from the glycan, Glc3Man9GlcNAc2, transferred to Asn residues in proteins. The enzyme participates in the calnexin/calreticulin cycle, it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
physiological function
-
glucosidaseII beta-subunit is required for EFR (a plasma-membrane immunity receptor) function
physiological function
the enzyme is continuously requirement in correct folding of cell surface proteins
physiological function
the enzyme is important for N-glycosylation processing and quality control of nascent glycoproteins
physiological function
the enzyme is important for N-glycosylation processing and quality control of nascent glycoproteins
physiological function
-
the enzyme is involved in quality control of glycoprotein folding in the endoplasmic reticulum, overview
physiological function
enzyme null mutants tend to aggregate, display reduced growth rates, have a lower content of cell wall phosphomannan and other changes in cell wall composition, underglycosylated beta-N-acetylhexosaminidase, and have a constitutively activated PKC-Mkc1 cell wall integrity pathway. Cells are also attenuated in virulence in a murine model of systemic infection and stimulated an altered pro- and anti-inflammatory cytokine profile from human monocytes
physiological function
gene Rot2 complements a Saccharomyces cerevisiae Rot2 mutant. When expressed in a Candida albicans rot2 mutant, Sporothrix schenckii Rot2 partially increases the levels of alpha-glucosidase activity, but fails to restore the N-linked glycosylation defect associated to the mutation
physiological function
lack of ModA activity does not prevent intracellular transport and proteolytic processing of the lysosomal enzymes, alpha-mannosidase and beta-glucosidase, but slows down the rate at which the glucosylated precursors leave the rough endoplasmic reticulum. Enzymes N-acetylglucosaminidase and acid phosphatase are secreted much less efficiently from lysosomal compartments by the mutant strain
physiological function
MAL1 down-regulation produces an extremely stunted phenotype with curled leaves and tuber yield is decreased by 90% compared to control values. Plants with down-regulated glucosidase II activity show a greater degree of plasmolysis, and an increase in the size of mesophyll intracellular spaces in leaves. Cell walls also change in structure as a result of MAL1 down-regulation. In leaves from antisense lines, the steady-state transcript level corresponding to the endoplasmic reticulum chaperone, BiP, is enhanced
physiological function
compared to wild-type, a Gas2 RNAi cell line is much more sensitive to dithiothreitol treatment and has higher levels of autophagy. Both caspase-3 and heat-stressed cell suspension lysate can cleave Gas2, producing a 14 kDa N-terminal fragment. Conditional expression of this C-terminal fragment results in enhanced caspase-3-like activity in the protoplasts under heat stress
physiological function
-
enzyme null mutants tend to aggregate, display reduced growth rates, have a lower content of cell wall phosphomannan and other changes in cell wall composition, underglycosylated beta-N-acetylhexosaminidase, and have a constitutively activated PKC-Mkc1 cell wall integrity pathway. Cells are also attenuated in virulence in a murine model of systemic infection and stimulated an altered pro- and anti-inflammatory cytokine profile from human monocytes
-
physiological function
-
the enzyme is continuously requirement in correct folding of cell surface proteins
-
additional information
high concentration of alpha-glucosidase inhibitors from mulberry leaves accumulate in Bombyx mori by feeding, silkworm does not show any toxic symptom against these inhibitors and N-glycosylation of recombinant proteins is not affected
additional information
high concentration of alpha-glucosidase inhibitors from mulberry leaves accumulate in Bombyx mori by feeding, silkworm does not show any toxic symptom against these inhibitors and N-glycosylation of recombinant proteins is not affected
additional information
-
the inability of beta-subunit MRH domain to efficiently recognize glucose eliminates the potential for the beta-subunit to compete with the catalytic alpha-subunit of GII for glucose present in arm A of the N-glycan, ligand binding structures, overview. Possible models for the influence of Trp409 in enzyme activity
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GANAB_DICDI
943
1
108772
Swiss-Prot
Secretory Pathway (Reliability: 1)
GANAB_HUMAN
944
1
106874
Swiss-Prot
Mitochondrion (Reliability: 4)
GANAB_MACFA
944
1
106890
Swiss-Prot
Mitochondrion (Reliability: 5)
GANAB_MOUSE
944
1
106911
Swiss-Prot
Mitochondrion (Reliability: 5)
GANAB_PIG
944
1
106662
Swiss-Prot
Mitochondrion (Reliability: 4)
GLU2A_ORYSJ
919
0
103215
Swiss-Prot
Mitochondrion (Reliability: 4)
GLU2A_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
923
1
106282
Swiss-Prot
Secretory Pathway (Reliability: 1)
GLU2A_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
954
0
110266
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A6J8D6F6_MYTCO
938
0
107520
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7R8HA48_LEPSM
587
0
67908
TrEMBL
other Location (Reliability: 2)
O24375_SOLTU
919
1
105417
TrEMBL
Secretory Pathway (Reliability: 2)
Q2V621_CANAX
830
0
96269
TrEMBL
Secretory Pathway (Reliability: 1)
Q5A4X3_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
871
0
100059
TrEMBL
-
PSL5_ARATH
921
0
104275
Swiss-Prot
Secretory Pathway (Reliability: 4)
GLU2B_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
506
0
57075
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000 - 123000
104000
105000
alphabeta, x * 105000, recombinant alpha-subunit, SDS-PAGE, beta-subunit not specified in the publication
105206
alphabeta, x * 105206, alpha-subunit, sequence calculation, x * 106000, recombinant alpha-subunit, SDS-PAGE, beta-subunit not specified in the publication
106000
107000
11000
-
alpha, beta, 1 * 11000 + 1 * 80000, catalytic alpha subunit and beta subunit of unknown function
110000
116000
117000
molecular mass of protein extract of both glucosidase II-alpha and -beta minus Schizosaccharomyces pombe mutant cells after cells transformed with the cDNA sequences of Arabidopsis thaliana glucosidase II-alpha encoding gen and after deglycosylation
119000
western blot analysis of protein extract of both glucosidase II-alpha and -beta minus Schizosaccharomyces pombe mutant cells after cells transformed with the cDNA sequences of Arabidopsis thaliana glucosidase II-alpha encoding gene
260000 - 290000
80000
104000
deduced from cDNA sequences of Arabidopsis thaliana glucosidase II-alpha encoding gene
106000
alphabeta, x * 105206, alpha-subunit, sequence calculation, x * 106000, recombinant alpha-subunit, SDS-PAGE, beta-subunit not specified in the publication
110000
-
SDS-PAGE, a second band corresponds to a molecular weight of 68000 and is supposed to be a proteolytically degraded fragment
110000
-
alpha, beta, 1 * 110000 + 1 * ?, SDS-PAGE, catalytic alpha subunit and beta subunit of unknown function
116000
-
alpha, beta, 1 * 116000 + 1 * 80000, SDS-PAGE, the beta subunit contains two domains that are capable to associate with the alpha subunit
80000
-
alpha, beta, 1 * 11000 + 1 * 80000, catalytic alpha subunit and beta subunit of unknown function
80000
-
alpha, beta, 1 * 116000 + 1 * 80000, SDS-PAGE, the beta subunit contains two domains that are capable to associate with the alpha subunit
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
homodimer
tetramer
additional information
?
x * 104633, calculated for alpha subunit, plus x* 59514, calculated for beta subunit
?
-
x * 125000, alpha-subunit, x * 58000, beta-subunit, calculated from sequence
?
-
existence of 2 isoforms with molecular masses of 107000 and 112000 Da in various organs, SDS-PAGE
dimer
alpha, beta, two different isoforms of the alpha subunit identified, alpha1 is the short and alpha2 the long isoform, both isoforms form dimers with the beta subunit, only dimeric form shows catalytic activity
dimer
alpha, beta, two different isoforms of the alpha subunit identified, alpha1 is the short and alpha2 the long isoforms, both isoforms forms dimers with the beta subunit, only dimeric form shows catalytic activity
dimer
-
alpha, beta, 1 * 116000 + 1 * 80000, SDS-PAGE, the beta subunit contains two domains that are capable to associate with the alpha subunit
dimer
-
alpha, beta, 1* 116000 + 1 * 84000, SDS-PAGE, catalytically active alpha subunit, beta subunit with unknown function
dimer
-
alpha, beta, 1 * 110000 + 1 * ?, SDS-PAGE, catalytic alpha subunit and beta subunit of unknown function
dimer
-
alpha, beta, 1 * 11000 + 1 * 80000, catalytic alpha subunit and beta subunit of unknown function
heterodimer
-
the enzyme is a heterodimer whose alpha-subunit contains a glycosidase active site, while the beta-subunit confers the substrate specificity toward di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit
heterodimer
-
the enzyme is a heterodimer whose alpha-subunit contains a glycosidase active site, while the beta-subunit confers the substrate specificity toward di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit
-
heterodimer
alphabeta, x * 105000, recombinant alpha-subunit, SDS-PAGE, beta-subunit not specified in the publication
heterodimer
G0SG42; G0S9M2
1 * alpha subunit, 1 * beta-subunit, crystallization data
heterodimer
-
1 * alpha subunit, 1 * beta-subunit, crystallization data
-
heterodimer
-
glucosidase II is a heterodimeric complex consisting of a catalytic alpha subunit GIIalpha, and a tightly associated beta subunit GIIbeta that contains a mannose 6-phosphate receptor homology domain, MRH domain, which is responsible for the glucose trimming process via its putative sugar-binding activity
heterodimer
-
the alpha subunit bears the active site, and the beta subunit modulates the subunit alpha activity through its C-terminal mannose 6-phosphate receptor homologous domain
heterodimer
-
the enzyme is a heterodimer whose alpha-subunit GIIalpha bears the glycosyl hydrolase active site, whereas its beta-subunit GIIbeta is involved in GIIbeta endoplasmic reticulum retention and folding, but does not efficiently deglucosylate the physiological substrates Glc2Man9GlcNAc2 and Glc1Man9GlcNAc2
heterodimer
-
the enzyme is a heterodimer whose alpha-subunit GIIalpha bears the glycosyl hydrolase active site, whereas its beta-subunit GIIbeta is involved in GIIbeta endoplasmic reticulum retention and folding, but does not efficiently deglucosylate the physiological substrates Glc2Man9GlcNAc2 and GlcMan9GlcNAc2. GIIbeta is required for an efficient in vitro glucose trimming from G2M9 and G1M9, and processing of both middle and innermost glucoses
heterodimer
-
the alpha subunit bears the active site, and the beta subunit modulates the subunit alpha activity through its C-terminal mannose 6-phosphate receptor homologous domain
heterodimer
alphabeta, x * 105206, alpha-subunit, sequence calculation, x * 106000, recombinant alpha-subunit, SDS-PAGE, beta-subunit not specified in the publication
additional information
enzyme peptide proteolysis and fragment analysis, overview
additional information
-
enzyme peptide proteolysis and fragment analysis, overview
-
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
-
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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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the catalytic alpha subunit complexed with two different glucosyl ligands containing the scissile bonds of first and second-step reactions. The nonreducing terminal disaccharide moieties of the two kinds of substrates can be accommodated in a gourd-shaped bilocular pocket
G0SG42; G0S9M2
structure of a complex formed between the alpha-subunit GIIa and the GIIa-binding domain of the beta-subunit GIIb. GIIa forms a heterodimeric structure through its distal C-terminal domain
G0SG42; G0S9M2
small-angle X-ray scattering and crystal structures of enzyme alone and in complex with key ligands of its catalytic cycle and antiviral iminosugars. A conformational rearrangement is needed for the simultaneous binding of a monoglucosylated glycan to both subunits. An insertion between the +1 and +2 subsites contributes to the enzyme's activity and substrate specificity, and the presence of D-mannose at the +1 subsite renders the acid catalyst less efficient during the cleavage of the monoglucosylated substrate
structures of a trypsinolytic fragment, alone and in complex with catalytic cycle ligands, and four different broad-spectrum antiviral iminosugar inhibitors
mannose 6-phosphate receptor homology domain of GII beta subunit bound to mannose, to 1.6 A resolution. No major difference in the overall fold of ligand-bound and unbound structures, but a repositioning of side chains throughout the binding pocket, including Y372
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
rsw3
Substitution of Ser599 by a Phe residue, inactivation of the alpha-subunit under non-permissive temperature because mutant is strongly temperature-sensitive
D556A
Q420E
-
site-directed mutagenesis of the mannose 6-phosphate receptor homology domain of the beta-subunit, GIIbeta-MRH, leading to reduced activity with substrates G1M9 and G2M9
Y410A
-
site-directed mutagenesis of the mannose 6-phosphate receptor homology domain of the beta-subunit, GIIbeta-MRH, leading to reduced activity with substrates G1M9 and G2M9
W409A
W409F
-
site-directed mutagenesis of the beta subunit MRH domain, the mutant shows altered ligand binding actvity compared to the wild-type beta-subunit
additional information
W409A
-
site-directed mutagenesis of the beta subunit MRH domain, the mutant shows altered ligand binding actvity compared to the wild-type beta-subunit
additional information
-
construction of psl knockout mutants, EFR-mediated signaling is severely impaired in strong subunit beta psl4 mutant plants, and partially and differentially impaired in weak psl5, gIIalpha, mutant plants. EFR signaling is partially and differentially impaired without a significant decrease of the receptor steady-state levels in 2 weakly dysfunctional gIIalpha alleles, designated psl5-1 and rsw3. Phenotypes, overview
additional information
-
construction of strains of gene disruptants lacking either the glucosidase II alpha- or beta-subunit. The mutant lacking the beta-subunit is inactive with both Glc2Man9GlcNAc2 and Glc1Man9GlcNAc2, but activity can be restored by adding the beta-subunit fraction, overview
additional information
-
construction of strains of gene disruptants lacking either the glucosidase II alpha- or beta-subunit. The mutant lacking the beta-subunit is inactive with both Glc2Man9GlcNAc2 and Glc1Man9GlcNAc2, but activity can be restored by adding the beta-subunit fraction, overview
-
additional information
-
a mutant enzyme with the mutant subunit IIbeta loses the sugar-binding activity of the GIIbeta-MRH domain, but hydrolyzes 4-nitrophenyl-alpha-glucopyranoside, although the capacity to remove glucose residues from G1M9 and G2M9 is significantly decreased, phenotype, overview
additional information
-
construction of several truncated forms of the beta subunit with different capabilities of binding the alpha subunit
additional information
-
limited trypsin digestion of the alpha subunit resultes in a fully active fragment of 70000 Da
additional information
-
construction of alpha or beta-subunit deletion mutant strains, disruption of subunit GIIalpha leads to complete loss of enzyme activity, while in the absence of GIIbeta, the catalytic subunit GIIalpha of Schizosaccharomyces pombe folds to an active conformation able to hydrolyze 4-nitrophenyl alpha-D-glucopyranoside, phenotypes, overview
additional information
mutations of the primary binding pocket residues and adjacent W409, all inhibit the activity of GII both in vitro and in vivo, they do not cause a significant change in the overall fold of the GII beta subunit mannose 6-phosphate receptor homology domain but impact locally the stability of the binding pocket
additional information
-
mutations of the primary binding pocket residues and adjacent W409, all inhibit the activity of GII both in vitro and in vivo, they do not cause a significant change in the overall fold of the GII beta subunit mannose 6-phosphate receptor homology domain but impact locally the stability of the binding pocket
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
40
-
100% of activity after 30 min, 10 mM potassium phosphate buffer, pH 7, 0.1% Triton X-100, 5 mM 2-mercaptoethanol
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, stabilization
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 100 mM phosphate buffer, pH 7, 100 mM maltose, 5 mM mercaptoethanol, several weeks
-
4-6°C, 100 mM phosphate buffer, pH 7, 10% glycerol, 5 mM mercaptoethanol, several days
-
4°C, 10 mM potassium phosphate buffer, pH 7, 0.1% Triton X-100, 5 mM 2-mercaptoethanol, 14 days
-
4°C, 10 mM potassium phosphate buffer, pH 7, 0.1% Triton X-100, 5 mM 2-mercaptoethanol, 8 days ethanol treated rats
-
4°C, 2 days, more than 60% loss of activity, presence of 10% v/v glycerol prevents this loss
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged and GFP-tagged subunit by nickel affinity chromatography
recombinant His-tagged beta-subunit by immobilized metal affinity chromatography from Escherichia coli strain BL21(pREP4)
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-subunit, DNA and amino acid sequence determination and analysis, recombinant expression as His-tagged protein in Escherichia coli strain BL21(pREP4)
-
cloning of alpha- and beta-subunits and expression in Escherichia coli strains DH5alpha and JA226
-
expressed with a baculovirus expression system in Sf9 cells, expressed in Cos7 cells
expression in Escherichia coli
expression in Schizosaccharomyces pombe mutants either glucosidase II-alpha or both glucosidase II-alpha and -beta minus, vector pTOTO, vector pREP3X, vector pSGP72
expression of wild-type and mutant beta-subunits and enzymes in HeLaS3 cells, overexpression in HEK 293T cells
-
expression of wild-type and mutant fusion forms of the enzyme in Sf9 insect cells
fragments and full length beta-subunit expressed as GST-fusion protein in Escherichia coli
-
genes Aogls2alpha and/or Aogls2beta encdoing the alpha- und beta-subunit, cloning and expression in Escherichia coli strain DH5alpha
-
recombinant expression of His-tagged alpha-subunits via the vaculovirus transfection system in Sf21AE cells
recombinant expression of His-tagged and GFP-tagged alpha-subunit via the vaculovirus transfection system in Sf21AE cells
recombinant expression of His-tagged and GFP-tagged beta-subunits via the vaculovirus transfection system in Sf21AE cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethanol-sensitive GIIbeta is upregulated by about 70% in ethanol-exposed cerebral cortex
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in live Schizosaccharomyces pombe cells, a decrease in the number of mannoses in the glycan results in decreased glucosidase II activity
in live Schizosaccharomyces pombe cells, a decrease in the number of mannoses in the glycan results in decreased glucosidase II activity
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in live Schizosaccharomyces pombe cells, a decrease in the number of mannoses in the glycan results in decreased glucosidase II activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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synthetic route for fluorescent and biotin-modified activity-based probes for in vitro and in situ monitoring of alpha-glucosidases. alpha-Glucopyranose configured cyclophellitol aziridines label distinct retaining alpha-glucosidases including lysosomal acid alpha-glucosidase and ER alpha-glucosidase II, and this labeling can be tuned by pH
medicine
medicine
inhibitors of the enzyme are used to inhibit cell proliferation and migration in a variety of different pathologies, such as viral infection, cancer, and diabetes
medicine
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inhibitors of the enzyme are used to inhibit cell proliferation and migration in a variety of different pathologies, such as viral infection, cancer, and diabetes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaushal, G.P.; Pan, Y.T.; Tropea, J.E.; Mitchell, M.; Liu, P.; Elbein, A.D.
Selective inhibition of glycoprotein-processing enzymes. Differential inhibition of glucosidases I and II in cell culture
J. Biol. Chem.
263
17278-17283
1988
Vigna radiata
brenda
Saxena, S.; Shailubhai, K.; Dong-Yu, B.; Vijay, I.K.
Purification and characterization of glucosidase II involved in N-linked glycoprotein processing in bovine mammary gland
Biochem. J.
247
563-570
1987
Bos taurus
brenda
Strous, G.J.; Van Kerkhof, P.; Brok, R.; Roth, J.; Brada, D.
Glucosidase II, a protein of the endoplasmic reticulum with high mannose oligosaccharide chains and a rapid turnover
J. Biol. Chem.
262
3620-3625
1987
Rattus norvegicus
brenda
Lucocq, J.M.; Brada, D.; Roth J.
Immunolocalization of the oligosaccharide trimming enzyme glucosidase II
J. Cell Biol.
102
2137-2146
1986
Sus scrofa
brenda
Hino, Y.; Rothman, J.E.
Glucosidase II, a glycoprotein of the endoplasmic reticulum membrane. Proteolytic cleavage into enzymatically active fragments
Biochemistry
24
800-805
1985
Rattus norvegicus
brenda
Brada, D.; Dubach, U.C.
Isolation of a homogeneous glucosidase II from pig kidney microsomes
Eur. J. Biochem.
141
149-156
1984
Sus scrofa
brenda
Tabas, I.; Kornfeld, S.
N-Asparagine-linked oligosaccharides: processing
Methods Enzymol.
83
416-429
1982
Bos taurus
brenda
Burns, D.M.; Touster, O.
Purification and characterization of glucosidase II, an endoplasmic reticulum hydrolase involved in glycoprotein biosynthesis
J. Biol. Chem.
257
9991-10000
1982
Rattus norvegicus
-
brenda
Grinna, L.S.; Robbins, P.W.
Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
J. Biol. Chem.
255
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1980
Rattus norvegicus
brenda
Alonso, J.F.; Santa-Cecilia, A.; Calvo, P.
Effect of bromoconduritol on glucosidase II from rat liver, a new kinetic model for the binding and hydrolysis of the substrate
Eur. J. Biochem.
215
37-42
1993
Rattus norvegicus
brenda
Kaushal, G.P.; Zeng, Y.; Elbein, A.D.
Biosynthesis of glucosidase II in suspension-cultured soybean cells
J. Biol. Chem.
268
14536-14542
1993
Glycine max, Vigna radiata
brenda
Trombetta, E.S.; Simons, J.F.; Helenius, A.
Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit
J. Biol. Chem.
271
27509-27516
1996
Rattus norvegicus
brenda
D'Alessio, C.; FernÓndez, F.; Trombetta, E.S.; Parodi, A.J.
Genetic evidence for the heterodimeric structure of glucosidase II: the effect of disrupting the subunit-encoding genes on glycoprotein folding
J. Biol. Chem.
274
25899-25905
1996
Schizosaccharomyces pombe
brenda
Santa-Cecilia, A.; Alonso, J.F.; Calvo, P.
Glucosidase II from control and ethanol-treated rats: purification and properties
Biol. Chem.
372
373-380
1991
Rattus norvegicus
brenda
Alonso, J.F.; Santa-Cecilia, A.; Chinchetru, M.A.; Calvo, P.
Characterization of the maltase activity of glucosidase II from rat liver: kinetic model
Biol. Chem.
374
977-982
1993
Rattus norvegicus
brenda
Hentges, A.; Bause, E.
Affinity purification and characterization of glucosidase II from pig liver
Biol. Chem.
378
1031-1038
1997
Sus scrofa
brenda
Takeuchi, M.; Kamata, K.; Yoshida, M.; Kameda, Y.; Matsui, K.
Inhibitory effect of pseudo-aminosugars on oligosaccharide glucosidases I and II and on lysosomal alpha-glucosidase from rat liver
J. Biochem.
108
42-46
1990
Rattus norvegicus
brenda
Brada, D.; Kerjaschki, D.; Roth, J.
Call type-specific post-Golgi apparatus localization of a "resident" endoplasmic reticulum glycoprotein, glucosidase II
J. Cell Biol.
110
309-318
1990
Sus scrofa
brenda
Alonso, J.F.; Santa-Cecilia, A.; Calvo, P.
Glucosidase II from rat liver microsomes: kinetic model for binding and hydrolysis
Biochem. J.
278
721-727
1991
Rattus norvegicus
-
brenda
Treml, K.; Meimaroglou, D.; Hentges, A.; Bause, E.
The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver
Glycobiology
10
493-502
2000
Homo sapiens (Q14697)
brenda
Kaushal, G.P.; Pastuszak, I.; Hatanka, K.; Elbein, A.D.
Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells
J. Biol. Chem.
265
16271-16279
1990
Vigna radiata
brenda
Roth, J.; Ziak, M.; Zuber, C.
The role of glucosidase II and endomannosidase in glucose trimming of asparagine-linked oligosaccharides
Biochimie
85
287-294
2003
Bos taurus, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Trombetta, E.S.; Fleming, K.G.; Helenius, A.
Quaternary and domain structure of glycoprotein processing glucosidase II
Biochemistry
40
10717-10722
2001
Rattus norvegicus
brenda
Hirano, K.; Ziak, M.; Kamoshita, K.; Sukenaga, Y.; Kametani, S.; Shiga, Y.; Roth, J.; Akanuma, H.
N-linked oligosaccharide processing enzyme glucosidase II produces 1,5-anhydrofructose as a side product
Glycobiology
10
1283-1289
2000
Rattus norvegicus, Sus scrofa
brenda
Arendt, C.W.; Ostergaard, H.L.
Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit
Glycobiology
10
487-492
2000
Mus musculus
brenda
Pelletier, M.F.; Marcil, A.; Sevigny, G.; Jakob, C.A.; Tessier, D.C.; Chevet, E.; Menard, R.; Bergeron, J.J.M.; Thomas, D.Y.
The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo
Glycobiology
10
815-827
2000
Homo sapiens (P14314), Homo sapiens (Q14697)
brenda
Baldwin, T.A.; Gogela-Spehar, M.; Ostergaard, H.L.
Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction
J. Biol. Chem.
275
32071-32076
2000
Mus musculus
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
Geysens, S.; Pakula, T.; Uusitalo, J.; Dewerte, I.; Penttilae, M.; Contreras, R.
Cloning and characterization of the glucosidase II alpha subunit gene of Trichoderma reesei: a frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain Rut-C30
Appl. Environ. Microbiol.
71
2910-2924
2005
Trichoderma reesei, Trichoderma reesei RUT C-30
brenda
Gamberucci, A.; Konta, L.; Colucci, A.; Giunti, R.; Magyar, J.E.; Mandl, J.; Banhegyi, G.; Benedetti, A.; Csala, M.
Green tea flavonols inhibit glucosidase II
Biochem. Pharmacol.
72
640-646
2006
Rattus norvegicus
brenda
Feng, J.; Romaniouk, A.V.; Samal, S.K.; Vijay, I.K.
Processing enzyme glucosidase II: proposed catalytic residues and developmental regulation during the ontogeny of the mouse mammary gland
Glycobiology
14
909-921
2004
Mus musculus (Q8BHN3)
brenda
Jones, D.C.; Mehlert, A.; Guether, M.L.; Ferguson, M.A.
Deletion of the glucosidase II gene in Trypanosoma brucei reveals novel N-glycosylation mechanisms in the biosynthesis of variant surface glycoprotein
J. Biol. Chem.
280
35929-35942
2005
Trypanosoma brucei
brenda
Wilkinson, B.M.; Purswani, J.; Stirling, C.J.
Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum
J. Biol. Chem.
281
6325-6333
2006
Saccharomyces cerevisiae
brenda
Schirawski, J.; Boehnert, H.U.; Steinberg, G.; Snetselaar, K.; Adamikowa, L.; Kahmann, R.
Endoplasmic reticulum glucosidase II is required for pathogenicity of Ustilago maydis
Plant Cell
17
3532-3543
2005
Ustilago maydis
brenda
Totani, K.; Ihara, Y.; Matsuo, I.; Ito, Y.
Effects of macromolecular crowding on glycoprotein processing enzymes
J. Am. Chem. Soc.
130
2101-2107
2008
Rattus norvegicus
brenda
Totani, K.; Ihara, Y.; Matsuo, I.; Ito, Y.
Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans
J. Biol. Chem.
281
31502-31508
2006
Rattus norvegicus
brenda
Bosis, E.; Nachliel, E.; Cohen, T.; Takeda, Y.; Ito, Y.; Bar-Nun, S.; Gutman, M.
Endoplasmic Reticulum Glucosidase II is inhibited by its end products
Biochemistry
47
10970-10980
2008
Rattus norvegicus
brenda
Soussillane, P.; D'Alessio, C.; Paccalet, T.; Fitchette, A.-C.; Parodi, A.J.; Williamson, R.; Plasson, C.; Faye, L.; Gomord, V.
N-glycan trimming by glucosidase II is essential for Arabidopsis development
Glycoconj. J.
26
597-607
2009
Arabidopsis thaliana (Q9FN05)
brenda
Hu, D.; Kamiya, Y.; Totani, K.; Kamiya, D.; Kawasaki, N.; Yamaguchi, D.; Matsuo, I.; Matsumoto, N.; Ito, Y.; Kato, K.; Yamamoto, K.
Sugar-binding activity of the MRH domain in the ER alpha-glucosidase II beta subunit is important for efficient glucose trimming
Glycobiology
19
1127-1135
2009
Homo sapiens
brenda
Watanabe, T.; Totani, K.; Matsuo, I.; Maruyama, J.; Kitamoto, K.; Ito, Y.
Genetic analysis of glucosidase II beta-subunit in trimming of high-mannose-type glycans
Glycobiology
19
834-840
2009
Aspergillus oryzae, Aspergillus oryzae RIB 40
brenda
Stigliano, I.D.; Caramelo, J.J.; Labriola, C.A.; Parodi, A.J.; DAlessio, C.
Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
Mol. Biol. Cell
20
3974-3984
2009
Rattus norvegicus, Schizosaccharomyces pombe
brenda
Lu, X.; Tintor, N.; Mentzel, T.; Kombrink, E.; Boller, T.; Robatzek, S.; Schulze-Lefert, P.; Saijo, Y.
Uncoupling of sustained MAMP receptor signaling from early outputs in an Arabidopsis endoplasmic reticulum glucosidase II allele
Proc. Natl. Acad. Sci. USA
106
22522-22527
2009
Arabidopsis thaliana
brenda
Torres-Rodriguez, B.I.; Flores-Berrout, K.; Villagomez-Castro, J.C.; Lopez-Romero, E.
Purification and partial biochemical characterization of a membrane-bound type II-like alpha-glucosidase from the yeast morphotype of Sporothrix schenckii
Antonie van Leeuwenhoek
101
313-322
2012
Sporothrix schenckii, Sporothrix schenckii EH206
brenda