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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 + 2 H2O
Man9GlcNAc2 + 2 D-glucose
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + beta-D-glucopyranose
-
-
-
-
?
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucopyranose
Glc2Man9GlcNAc2 + H2O
GlcMan9GlcNAc2 + D-glucose
Glc2Man9GlcNAc2 + H2O
Man9GlcNAc2 + alpha-D-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 + 1,5-anhydrofructose
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
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 + 2 H2O
Man9GlcNAc2 + 2 D-glucose
-
enzyme expression in Schizosaccharomyces pombe mutants either glucosidase II-alpha or both glucosidase II-alpha and -beta minus after cells transformed with the cDNA sequences of Arabidopsis thaliana glucosidase II-alpha encoding gene
-
?
Glc2Man9GlcNAc2 + 2 H2O
Man9GlcNAc2 + 2 D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + 2 H2O
Man9GlcNAc2 + 2 D-glucose
-
-
-
-
?
Glc2Man9GlcNAc2 + 2 H2O
Man9GlcNAc2 + 2 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
-
-
-
-
?
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-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
2 D-glucose
-
-
-
?
maltose + H2O
2 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
-
-
?
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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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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
-
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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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Rattus norvegicus
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Homo sapiens
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Aspergillus oryzae, Aspergillus oryzae RIB 40
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Rattus norvegicus, Sus scrofa
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Schizosaccharomyces pombe (Q9USH8), Schizosaccharomyces pombe 972 (Q9USH8)
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Rattus norvegicus
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Bombyx mori (L8B8U1 and L8B6C5), Spodoptera frugiperda (L8B8V1)
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Mus musculus
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Mus musculus (Q8BHN3), Mus musculus
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Thermochaetoides thermophila (G0SG42 and G0S9M2), Thermochaetoides thermophila DSM 1495 (G0SG42 and G0S9M2)
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