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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
-
-
-
-
?
4-methylumbellyferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + D-glucose
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-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
-
-
?
Glc2Man7GlcNAc2 + H2O
GlcMan7GlcNAc2 + D-glucose
-
-
-
-
?
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
GlcMan9GlcNAc2 + D-glucopyranose
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucose
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
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
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + glucose
GlcMan7GlcNAc2 + H2O
Man7GlcNAc2 + D-glucose
-
-
-
-
?
GlcMan9GlcNAc + H2O
D-glucose + Man9GlcNAc
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
-
?
GlcMan9GlcNAc2 + H2O
D-glucose + Man9GlcNAc2
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + beta-D-glucopyranose
-
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + 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-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
-
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
alpha-D-glucose
-
-
-
-
?
maltose + H2O
alpha-D-glucose + 1,5-anhydrofructose
maltotriose + 2 H2O
3 D-glucose
-
-
-
?
mannose oligosaccharide + H2O
?
-
substrate specificity of wild-type and mutant enzymes with different mannose oligosaccharides, overview
-
-
?
N-glycan + H2O
? + D-glucose
nigerose + H2O
2 D-glucose
p-nitrophenyl-2-deoxy-alpha-D-glucopyranoside + H2O
p-nitrophenol + 2-deoxy-alpha-D-glucose
-
very effective substrate, other deoxy derivatives are not hydrolyzed
-
-
?
sucrose + H2O
2 D-glucose
-
-
-
?
synthetic high-mannose-type glycan + H2O
?
-
-
-
-
?
additional information
?
-
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
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
i.e. G1M9, usage of synthetic methotrexate-coupled glycan substrate, G1M9-MTX
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
i.e. G1M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
i.e. G1M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
Glc2Man9GlcNAc2 + H2O

GlcMan9GlcNAc2 + D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucose
-
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucose
-
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucose
-
-
-
?
Glc2Man9GlcNAc2 + H2O

Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-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
-
-
-
?
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
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O

Man9GlcNAc2 + glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + glucose
-
-
-
-
?
GlcMan9GlcNAc + H2O

D-glucose + Man9GlcNAc
-
-
-
?
GlcMan9GlcNAc + H2O
D-glucose + Man9GlcNAc
-
-
-
?
GlcMan9GlcNAc2 + H2O

D-glucose + Man9GlcNAc2
-
-
-
?
GlcMan9GlcNAc2 + H2O
D-glucose + Man9GlcNAc2
-
-
-
?
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
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
G2M9, usage of synthetic methotrexate-coupled glycan substrate, G2M9-MTX
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
i.e. G2M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
i.e. G2M9, alpha-mannosidase-treated glycan from jack bean, structure, overview
-
-
?
GlcMan9GlcNAc2 + H2O

Man9GlcNAc2 + D-glucose
-
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucose
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucose
-
-
-
?
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
-
-
-
-
?
isomaltose + H2O

?
-
digested at barely detectable level
-
-
?
isomaltose + H2O
?
-
digested at barely detectable level
-
-
?
kojibiose + H2O

?
-
-
-
-
?
kojibiose + H2O
?
-
-
-
-
?
maltohexaose + H2O

maltopentaose + D-glucose
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
-
-
-
?
maltose + H2O

?
-
-
-
-
?
maltose + H2O
?
-
-
-
-
?
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
-
?
N-glycan + H2O

? + D-glucose
-
-
-
?
N-glycan + H2O
? + D-glucose
-
-
-
?
nigerose + H2O

2 D-glucose
-
-
-
?
nigerose + H2O
2 D-glucose
-
-
-
?
nigerose + H2O
2 D-glucose
-
-
-
?
nigerose + H2O
2 D-glucose
-
-
-
?
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)
-
-
?
trehalose + H2O

?
-
digested at barely detectable level
-
-
?
trehalose + H2O
?
-
digested at barely detectable level
-
-
?
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
?
-
no activity with N-glycan
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + D-glucopyranose
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
additional information
?
-
Glc2Man9GlcNAc2 + H2O

GlcMan9GlcNAc2 + D-glucopyranose
-
i.e. G1M9
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O

Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-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
-
-
-
-
?
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
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-glucose
-
-
-
-
?
GlcMan9GlcNAc2 + H2O

Man9GlcNAc2 + D-glucopyranose
-
G2M9
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
-
-
-
?
GlcMan9GlcNAc2 + H2O
Man9GlcNAc2 + D-glucopyranose
-
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
1,4-dideoxy-1,4-imino-D-arabinitol
2,6-anhydro-1-benzamide-D-glycero-D-ido-heptitol
-
-
2,6-dideoxy-2,6-imino-7-O-(beta-D-glucopyranosyl)-D-glycero-L-glucoheptitol
australine
0.01 mM, 20% inhibition
calreticulin
-
slower hydrolysis of Glc1Man9-residue to Glc0Man9-residue
-
D-glucono-1,5-lactone
-
-
epigallocatechin gallate
-
-
gallocatechin gallate
-
-
N-5-Carboxypentyl-1-deoxynojirimycin
-
-
N-butyldeoxynojirimycin
-
-
NaCl
-
optimum activity in presence of 0.1-0.2 M, inhibitory above 0.2 M
p-chloromercuribenzenesulfonate
-
-
p-nitrophenyl-alpha-D-glucoside
-
-
p-nitrophenyl-alpha-D-mannoside
-
-
p-nitrophenyl-beta-D-glucoside
-
-
p-nitrophenyl-beta-D-mannoside
-
-
1,4-dideoxy-1,4-imino-D-arabinitol

-
1,4-dideoxy-1,4-imino-D-arabinitol
-
1-deoxynojirimycin

-
1-deoxynojirimycin
0.01 mM, 60% inhibition
1-deoxynojirimycin
-
0.1 mM, complete inhibition
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

0.01 mM, 40% inhibition
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
Ca2+

-
-
Ca2+
40 mM, 63% loss of activity
castanospermine

-
castanospermine
0.01 mM, 10% inhibition
D-glucose

-
D-glucose
-
10 mM, 75% inhibition
deoxynojirimycin

-
an alpha-glucosidase-specific inhibitor
deoxynojirimycin
competitive, strong inhibition
maltose

-
-
nigerose

-
-
Tris

-
-
turanose

-
-
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
-
additional information
-
not inhibited by australine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 Essential for TRPM7 Function During Early Embryogenesis.
Cysts
Hepatocystin is not secreted in cyst fluid of hepatocystin mutant polycystic liver patients.
Cysts
Insights into Autosomal Dominant Polycystic Kidney Disease from Genetic Studies.
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
Mutations in PRKCSH cause isolated autosomal dominant polycystic 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.
Cysts
The zebrafish as a model to study 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.
Fibrosarcoma
Blood-based biomarkers for detecting mild osteoarthritis in the human knee.
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
Genetics and mechanisms of hepatic cystogenesis.
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
Mutations in SEC63 cause autosomal dominant polycystic liver disease.
Liver Diseases
N-glycosylation determines the abundance of the transient receptor potential channel TRPP2.
Liver Diseases
Novel GANAB variants associated with polycystic liver disease.
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.
Liver Diseases
[Cystic liver diseases. Genetics and cell biology]
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 GANAB variants associated with 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.
Virus Diseases
Animal models of biliary injury and altered bile acid metabolism.
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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
0.0708 - 0.5102
1,4-dideoxy-1,4-imino-D-arabinitol
0.00024 - 0.0727
1-deoxynojirimycin
0.4
6-deoxy-D-glucose
Candida albicans
pH 7.5, 37°C
0.041 - 0.262
bromoconduritol
0.001 - 0.0501
castanospermine
1.3
D-glucose
Candida albicans
pH 7.5, 37°C
0.00082 - 0.0112
deoxynojirimycin
4
Man7GlcNAc2
Rattus norvegicus
-
-
40
Man9GlcNAc2
Rattus norvegicus
-
-
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
0.0079
1-deoxynojirimycin
Spodoptera frugiperda
recombinant enzyme, pH 6,5, 37°C
0.0727
1-deoxynojirimycin
Bombyx mori
recombinant enzyme, pH 6,5, 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
0.041
bromoconduritol
Rattus norvegicus
-
cleavage-2, pH 7.4, 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
0.262
bromoconduritol
Rattus norvegicus
-
cleavage-1, pH 7.4, 37°C
0.001
castanospermine

Rattus norvegicus
-
cleavage-1, pH 7.4, 37°C
0.001
castanospermine
Rattus norvegicus
-
cleavage-2, pH 7.4, 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
0.0195
castanospermine
Spodoptera frugiperda
recombinant enzyme, pH 6,5, 37°C
0.0501
castanospermine
Bombyx mori
recombinant enzyme, pH 6,5, 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
0.008
deoxynojirimycin
Rattus norvegicus
-
cleavage-1, pH 7.4, 37°C
0.011
deoxynojirimycin
Rattus norvegicus
-
cleavage-2, pH 7.4, 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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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

-
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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?

x * 104633, calculated for alpha subunit, plus x* 59514, calculated for beta subunit
?
-
x * 47000, SDS-PAGE
-
?
-
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
?
x * 105206, calculated for alpha subunit
dimer

alphabeta 1 * 110000 + 1 * 80000
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
-
alphabeta 1 * 104000 + 1 * 58000
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
dimer
-
alpha2, 2 * 110000, SDS-PAGE
heterodimer

alphabeta
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
-
alphabeta
-
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
homodimer

-
2 * 75400, SDS-PAGE
homodimer
-
2 * 75400, SDS-PAGE
-
tetramer

-
4 * 63000-65000, SDS-PAGE, comparison with other values
tetramer
-
alpha4, 4 * 106000
tetramer
-
4 * 100000, SDS-PAGE
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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rsw3
Substitution of Ser599 by a Phe residue, inactivation of the alpha-subunit under non-permissive temperature because mutant is strongly temperature-sensitive
D542N
D542 required for catalytic activity
D564N
D564 required for catalytic activity
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
E114A
-
inactive towards Glc1Man9GlcNAc2
E73A
-
inactive towards Glc1Man9GlcNAc2
D564E
42.7% of wild-type activity
D564N
no activity detectable
E567D
53.2% of wild-type activity
E567Q
no activity detectable
F571A
74.8% of wild-type activity
E114A
-
inactive towards Glc1Man9GlcNAc2
E457Q
-
site-directed mutagenesis
E73A
-
inactive towards Glc1Man9GlcNAc2
Q408E
-
site-directed mutagenesis
R438K
-
site-directed mutagenesis
W409F
-
site-directed mutagenesis of the beta subunit MRH domain, the mutant shows altered ligand binding actvity compared to the wild-type beta-subunit
Y372A
mutation of Y372 substantially decreases GII activity
Y372F
mutation of Y372 substantially decreases GII activity
Y463F
-
site-directed mutagenesis
W409A
-
mutation substantially decreases GII activity
-
Y372A
-
mutation of Y372 substantially decreases GII activity
-
Y372F
-
mutation of Y372 substantially decreases GII activity
-
D556A

G0SG42; G0S9M2
inactive
W409A

-
site-directed mutagenesis of the beta subunit MRH domain, the mutant shows altered ligand binding actvity compared to the wild-type beta-subunit
W409A
mutation substantially decreases GII activity
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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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
2255-2258
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.
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Homo sapiens (Q14697)
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Homo sapiens (P14314), Homo sapiens (Q14697)
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Mus musculus (Q8BHN3)
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Trypanosoma brucei
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Saccharomyces cerevisiae
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Endoplasmic Reticulum Glucosidase II is inhibited by its end products
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2008
Rattus norvegicus
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N-glycan trimming by glucosidase II is essential for Arabidopsis development
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Arabidopsis thaliana (Q9FN05)
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Sugar-binding activity of the MRH domain in the ER alpha-glucosidase II beta subunit is important for efficient glucose trimming
Glycobiology
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2009
Homo sapiens
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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
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834-840
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Aspergillus oryzae, Aspergillus oryzae RIB 40
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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
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Rattus norvegicus, Schizosaccharomyces pombe
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Uncoupling of sustained MAMP receptor signaling from early outputs in an Arabidopsis endoplasmic reticulum glucosidase II allele
Proc. Natl. Acad. Sci. USA
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Arabidopsis thaliana
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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
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