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1,4-glucan-4-glucosyltransferase/amylo-1,6-glucosidase
-
-
-
-
4-alpha-glucano-transferase amylo-1,6-glucosidase
-
-
-
-
alpha-(1,6)-glucosidase
-
-
-
-
amylo-1,6-glucosidase-oligo-1,4-1,4-transferase
-
-
-
-
amylo-1,6-glucosidase/1,4-alpha-glucan 4-alpha-glucan 4-alpha-glycosyltransferase
-
-
-
-
amylo-1,6-glucosidase/1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glycosyltransferase
-
-
-
-
amylo-1,6-glucosidase/4-alpha-glucanotransferase
-
-
-
-
amylo-1,6-glucosidase/oligo-1,4-1,4-glucantransferase
-
-
-
-
amylo-alpha-1,6-glucosidase
amylo-alpha-1,6-glucosidase activity
-
-
amylopectin 1,6-glucosidase
-
-
-
-
debrancher enzyme
-
-
-
-
debrancher protein
-
-
-
-
dextrin 6-alpha-D-glucosidase
-
-
-
-
dextrin 6-alpha-glucosidase
dextrin 6-glucanohydrolase
-
-
-
-
dextrin 6-glucohydrolase
-
-
-
-
dextrin-1,6-glucosidase
-
-
-
-
dextrin:6-glucohydrolase
-
-
-
-
GDE amylo-alpha-1,6-glucosidase
-
part of the 170000 Da multifunctional glycogen debranching enzyme (GDE)
glucosidase, amylo-1,6-
-
-
-
-
glucosidase/transferase
-
-
-
-
glycogen debranching enzyme
glycogen debranching system
glycogen phosphorylase dextrin 6-glucanohydrolase
glycogen phosphorylase limit dextrin alpha-1,6-glucohydrolase
glycogen phosphorylase limit dextrin debranching system
-
-
-
-
indirect debranching enzyme
-
-
-
-
oligo-alpha-1,4-glucan:alpha-1,4-glucan-4-glycosyltransferase-amylo-1,6-glucosidase
-
-
-
-
transferase-glucosidase
-
-
-
-
alpha-1,6-glucosidase
-
-
alpha-1,6-glucosidase
-
-
-
amylo-1,6-glucosidase
-
-
-
-
amylo-1,6-glucosidase
part of the multifunctional glycogen debranching enzyme
amylo-1,6-glucosidase
-
part of the putative glycogen-debranching enzyme SSGDE
amylo-1,6-glucosidase
-
-
amylo-alpha-1,6-glucosidase
-
part of the glycogen debranching enzyme
amylo-alpha-1,6-glucosidase
-
part of the glycogen debranching enzyme
amylo-alpha-1,6-glucosidase
-
-
amylo-alpha-1,6-glucosidase
-
part of the glycogen debranching enzyme
amyloglucosidase
-
-
dextrin 6-alpha-glucosidase
-
-
-
-
dextrin 6-alpha-glucosidase
-
-
dextrin 6-alpha-glucosidase
-
part of the glycogen debranching enzyme, hydrolyzes dextrins with the structure Glc-alpha-1,4-(Glc-alpha-1,6)Glc-alpha-1,4-Glc to D-glucose and the corresponding pyridylamino-maltooligosaccharides
GDE
-
-
glycogen debranching enzyme
-
-
-
-
glycogen debranching enzyme
-
-
glycogen debranching enzyme
-
the enzyme shows alpha-1,6-glucosidase activity with the C-terminal domain
glycogen debranching enzyme
-
the enzyme shows alpha-1,6-glucosidase activity with the C-terminal domain
-
glycogen debranching enzyme
-
-
glycogen debranching enzyme
-
exhibits 4-alpha-glucanotransferase and amylo-alpha-1,6-glucosidase activities
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
136428, 136805, 171358, 171360, 171361, 171363, 171364, 171365, 171366, 171367, 171368, 171369, 171372, 171375, 171376, 171377, 171379, 171380, 171381, 171383, 171385, 171386, 171387, 171388, 171389, 171391
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
glycogen debranching system
-
EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system
glycogen phosphorylase dextrin 6-glucanohydrolase
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glycogen phosphorylase dextrin 6-glucanohydrolase
-
-
glycogen phosphorylase limit dextrin alpha-1,6-glucohydrolase
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-
glycogen phosphorylase limit dextrin alpha-1,6-glucohydrolase
-
-
glycogen phosphorylase limit dextrin alpha-1,6-glucohydrolase
-
-
SSO2094
locus name
TreX
-
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2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
2-deoxy-2-fluoro-alpha-D-glucosyl fluoride
?
-
poor substrate
-
-
?
6-O-alpha-D-glucosyl cyclodextrin + H2O
D-glucose + cyclodextrin
6-O-alpha-D-glucosyl cyclomalto-octaose + H2O
D-glucose + cyclomalto-octaose
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
?
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
D-glucose + cyclomaltoheptaose
6-O-alpha-D-glucosyl cyclomaltohexaose + H2O
D-glucose + cyclomaltohexaose
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
?
6-O-alpha-maltosyl-beta-cyclodextrin + H2O
maltose + beta-cyclodextrin
-
-
-
-
?
6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O
?
6-O-alpha-maltotetraosyl-beta-cyclodextrin + H2O
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
?
63-alpha-glucosyl maltopentaose + H2O
maltopentaose + D-glucose
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
63-alpha-maltotriosyl maltotetraose + H2O
?
63-O-alpha-glucosyl-PA-maltotetraose + H2O
maltotetraose + D-glucose
-
-
-
-
?
alpha-(1-6)-glucosyl cycloheptaamylose + H2O
cycloheptaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
alpha-D-glucosyl fluoride
fluoride + D-glucose
alpha-dextrin + H2O
alpha-dextrin + D-glucose
amylopectin + H2O
amylopectin + D-glucose
amylopectin + H2O
maltose + ?
amylopectin beta-dextrin + H2O
?
amylose
cycloamylose
-
-
degree of polymerization between 11 and 50
-
?
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
branched cyclodextrin + H2O
?
D-glucose + maltooligosaccharide
maltooligosaccharide
D-glucose-beta-cyclodextrin + H2O
D-glucose + beta-cyclodextrin
Glc-alpha-1,4-Glc-alpha-1,4-(Glc-alpha-1,6)-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + H2O
Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + D-glucose
Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-(Glc-alpha-1,6)Glc-alpha-1,4-Glc-alpha-1,4-Glc + H2O
Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc + D-glucose
-
the substrate is hydrolyzed most rapidly
-
-
?
Glc1-4Glc-alpha1-4(Glc-alpha1-6)Glc-alpha1-4 Glc-alpha1-4 Glc-alpha1-4Glc-2-aminopyridine + H2O
?
-
-
-
-
?
Glcalpha1-4Glcalpha1-4Glcalpha1-4(Glcalpha1-6)Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol) + H2O
Glcapha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol) + D-glucose
-
-
-
-
?
Glcalpha1-6Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4GlcPA + H2O
?
-
-
-
-
?
glycogen + H2O
glycogen + D-glucose
glycogen limit dextrin + H2O
?
-
-
-
-
?
glycogen phosphorylase limit dextrin + H2O
?
glycogen phosphorylase-limit dextrin + H2O
?
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
maltodecaose + H2O
?
-
-
-
-
?
maltodecaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
-
-
-
-
?
maltododecaose + H2O
?
-
-
-
-
?
maltoheptaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
-
-
-
-
?
maltohexaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
-
-
-
-
?
maltononaose + H2O
?
-
-
-
-
?
maltononaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
-
-
-
-
?
maltooctaose + H2O
?
-
-
-
-
?
maltooctaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
-
-
-
-
?
maltopentaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
-
-
-
-
?
maltotetraosyl-alpha-1,6 maltoheptaose + H2O
?
maltoundecaose + H2O
?
-
-
-
-
?
maltoundecaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
-
-
-
-
?
phosphorylase beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
phosphorylase limit dextrin + H2O
?
-
the purified enzyme has both maltooligosaccharide transferase and amylo-1,6-glucosidase activities within a single polypeptide chain, and the combination of these two activities removes the branches of phosphorylase limit dextrin
-
-
?
rice starch + H2O
?
-
82.4% activity compared to amylopectin
-
-
?
additional information
?
-
2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
-
-
isomaltose
r
2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
-
-
isomaltose
r
2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
-
-
isomaltose
r
6-O-alpha-D-glucosyl cyclodextrin + H2O
D-glucose + cyclodextrin
-
branched
-
?
6-O-alpha-D-glucosyl cyclodextrin + H2O
D-glucose + cyclodextrin
-
-
-
?
6-O-alpha-D-glucosyl cyclomalto-octaose + H2O
D-glucose + cyclomalto-octaose
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomalto-octaose + H2O
D-glucose + cyclomalto-octaose
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
D-glucose + cyclomaltoheptaose
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
D-glucose + cyclomaltoheptaose
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltohexaose + H2O
D-glucose + cyclomaltohexaose
-
poor substrate
-
-
?
6-O-alpha-D-glucosyl cyclomaltohexaose + H2O
D-glucose + cyclomaltohexaose
-
poor substrate
-
-
?
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
?
-
-
-
?
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
?
-
-
-
?
6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O
?
-
very poor substrate
-
-
?
6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O
?
-
poor substrate
-
-
?
6-O-alpha-maltotetraosyl-beta-cyclodextrin + H2O
?
the enzyme catalyzes both hydrolysis of alpha-1,6-glycosidic linkages and transglycosylation at relatively high (above 0.5 mM) substrate concentrations
-
-
?
6-O-alpha-maltotetraosyl-beta-cyclodextrin + H2O
?
the enzyme catalyzes both hydrolysis of alpha-1,6-glycosidic linkages and transglycosylation at relatively high (above 0.5 mM) substrate concentrations
-
-
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
?
-
very poor substrate
-
-
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
?
-
poor substrate
-
-
?
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
branched pentasaccharide "fast B5"
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
branched pentasaccharide "fast B5"
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
branched pentasaccharide "fast B5"
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
branched pentasaccharide "fast B5"
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
branched pentasaccharide "fast B5"
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
-
branched pentasaccharide "fast B5"
-
-
r
63-alpha-maltotriosyl maltotetraose + H2O
?
-
branched heptasaccharide B7
-
-
?
63-alpha-maltotriosyl maltotetraose + H2O
?
-
branched heptasaccharide B7
-
-
?
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
-
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
-
-
-
-
?
alpha-D-glucosyl fluoride
fluoride + D-glucose
-
-
-
?
alpha-D-glucosyl fluoride
fluoride + D-glucose
-
in absence or presence of glycogen or polysaccharide
-
?
alpha-dextrin + H2O
alpha-dextrin + D-glucose
-
-
-
-
?
alpha-dextrin + H2O
alpha-dextrin + D-glucose
-
-
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
-
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
slowly hydrolyzed
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
slowly hydrolyzed
-
-
r
amylopectin + H2O
amylopectin + D-glucose
-
-
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
-
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
very poor substrate
-
-
r
amylopectin + H2O
amylopectin + D-glucose
-
very poor substrate
partially debranched
?
amylopectin + H2O
amylopectin + D-glucose
-
very poor substrate
partially debranched
r
amylopectin + H2O
amylopectin + D-glucose
-
phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
?
amylopectin + H2O
amylopectin + D-glucose
-
phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
r
amylopectin + H2O
amylopectin + D-glucose
-
100% activity
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
-
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
slowly hydrolyzed
-
-
?
amylopectin + H2O
amylopectin + D-glucose
-
slowly hydrolyzed
-
-
r
amylopectin + H2O
amylopectin + D-glucose
-
slowly hydrolyzed
partially debranched
?
amylopectin + H2O
amylopectin + D-glucose
-
phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
?
amylopectin + H2O
amylopectin + D-glucose
-
phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
r
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin beta-dextrin + H2O
?
-
-
-
-
?
amylopectin beta-dextrin + H2O
?
-
-
-
-
?
amylose + H2O
?
-
-
-
-
r
amylose + H2O
?
-
16.9% activity compared to amylopectin
-
-
?
amylose + H2O
?
-
-
-
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
reverse reaction: glucose incorporation into beta-limit dextrin
reverse reaction: glucose incorporation into beta-limit dextrin
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
beta-dextrin
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
beta-dextrin
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
beta-dextrin
reverse reaction: glucose incorporation into beta-limit dextrin
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
beta-dextrin
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
beta-dextrin
-
r
branched cyclodextrin + H2O
?
the TreX protein has a specificity for hydrolysis of chains consisting of 6 glucose residues or longer
-
-
?
branched cyclodextrin + H2O
?
the TreX protein has a specificity for hydrolysis of chains consisting of 6 glucose residues or longer
-
-
?
D-glucose + maltooligosaccharide
maltooligosaccharide
-
-
branched
r
D-glucose + maltooligosaccharide
maltooligosaccharide
-
-
branched
r
D-glucose + maltooligosaccharide
maltooligosaccharide
-
-
branched
r
D-glucose + maltooligosaccharide
maltooligosaccharide
-
maltotetraose and maltopentaose
branched
r
D-glucose-beta-cyclodextrin + H2O
D-glucose + beta-cyclodextrin
-
most substrate is hydrolysed at 1 h and completely degraded at 5 h
-
-
?
D-glucose-beta-cyclodextrin + H2O
D-glucose + beta-cyclodextrin
-
most substrate is hydrolysed at 1 h and completely degraded at 5 h
-
-
?
Glc-alpha-1,4-Glc-alpha-1,4-(Glc-alpha-1,6)-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + H2O
Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + D-glucose
-
-
-
-
?
Glc-alpha-1,4-Glc-alpha-1,4-(Glc-alpha-1,6)-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + H2O
Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + D-glucose
-
-
-
-
?
Glc-alpha-1,4-Glc-alpha-1,4-(Glc-alpha-1,6)-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + H2O
Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-1-deoxy-1-[(2-pyridylamino)-D-glucitol] + D-glucose
-
-
-
-
?
glycogen + H2O
?
-
total degradation of glycogen requires combined actions of glycogen phosphorylase and glucosidase/transferase. Glucosidase/transferase: regulatory role of glycogen metabolism in liver
-
-
?
glycogen + H2O
?
preferred substrate
-
-
?
glycogen + H2O
?
preferred substrate
-
-
?
glycogen + H2O
?
-
in addition to 1,6-glucosidase activity, also has some 1,4-glucosidase and transferase activities
-
-
?
glycogen + H2O
glycogen + D-glucose
-
-
-
r
glycogen + H2O
glycogen + D-glucose
-
reverse reaction: incorporation of glucose into glycogen
-
r
glycogen + H2O
glycogen + D-glucose
-
reverse reaction: incorporation of glucose into glycogen
-
-
r
glycogen + H2O
glycogen + D-glucose
-
-
-
-
r
glycogen + H2O
glycogen + D-glucose
-
slowly hydrolyzed
-
-
r
glycogen + H2O
glycogen + D-glucose
-
reverse reaction: incorporation of glucose into glycogen
-
-
r
glycogen + H2O
glycogen + D-glucose
-
slowly hydrolyzed
-
-
r
glycogen + H2O
glycogen + D-glucose
-
rabbit liver glycogen: very poor substrate, shellfish glycogen: not a substrate
-
-
r
glycogen + H2O
glycogen + D-glucose
-
reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide
-
-
r
glycogen + H2O
glycogen + D-glucose
-
reverse reaction: incorporation of glucose into glycogen
136805, 171367, 171371, 171372, 171375, 171378, 171380, 171385, 171386, 171387, 171388, 171389 -
-
r
glycogen + H2O
glycogen + D-glucose
-
slight reversibility
-
-
r
glycogen + H2O
glycogen + D-glucose
-
rabbit liver glycogen: slowly
-
-
r
glycogen + H2O
glycogen + D-glucose
-
73.5% activity compared to amylopectin
-
-
?
glycogen + H2O
glycogen + D-glucose
-
slowly hydrolyzed
-
-
r
glycogen + H2O
glycogen + D-glucose
-
reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide
-
-
r
glycogen + H2O
glycogen + D-glucose
-
native glycogen from shellfish and rabbit liver
-
-
r
glycogen + H2O
glycogen + D-glucose
-
reverse reaction: incorporation of glucose into glycogen
-
-
r
glycogen + H2O
glycogen + D-glucose
-
liver glycogen and shellfish glycogen: one-tenth of activity compared with glycogen phosphorylase limit dextrin as substrate
-
r
glycogen phosphorylase limit dextrin + H2O
?
-
-
-
-
?
glycogen phosphorylase limit dextrin + H2O
?
-
-
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
-
phi-dextrin
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
-
-
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
-
symmetric dextrin
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
-
phi-dextrin
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
-
total degradation of glycogen is accomplished by the combined action of glycogen phosphorylase and glycogen debranching enzyme
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
-
-
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
-
phi-dextrin
-
-
?
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
best substrate
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
partially debranched glycogen
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
best substrate
partially debranched glycogen
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
symmetric dextrin
asymmetric dextrin
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
debranched phi-dextrin
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
partially debranched glycogen
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
best substrate
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
-
-
-
r
maltotetraosyl-alpha-1,6 maltoheptaose + H2O
?
-
-
-
?
maltotetraosyl-alpha-1,6 maltoheptaose + H2O
?
-
-
-
?
phosphorylase beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
limit dextrin, beta-phi-dextrin, derived from the action of beta-amylase on the phosphorylase limit dextrin
-
r
phosphorylase beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
limit dextrin, beta-phi-dextrin, derived from the action of beta-amylase on the phosphorylase limit dextrin
-
r
phosphorylase beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
limit dextrin, beta-phi-dextrin, derived from the action of beta-amylase on the phosphorylase limit dextrin
-
r
phosphorylase beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
-
limit dextrin, beta-phi-dextrin, derived from the action of beta-amylase on the phosphorylase limit dextrin
-
r
pullulan + H2O
?
-
36.8% activity compared to amylopectin
-
-
?
additional information
?
-
-
no alpha-glucosidase or alpha-amylase activity
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
pullulan: not a substrate
-
-
?
additional information
?
-
-
glycogen debranching system may be regarded as an integral part of the overall phosphorolytic pathway for the degradation of glycogen
-
-
?
additional information
?
-
-
glycogen debranching system, indirect debranching enzymes, is the dominant type of glycogen debranching mechanism, where glycogen is stored
-
-
?
additional information
?
-
-
NPDE exhibits hydrolysis activity toward both alpha-(1,6)- and alpha-(1,4)-glucosidic linkages, NPDE specifically liberates glucose from the reducing end, the catalytic efficiency of NPDE increases considerably upon using substrates that can occupy at least eight glycone subsites. Side chains shorter than maltooctaose in amylopectin are resistant to hydrolysis by NPDE
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
6-O-alpha-maltosyl cyclomaltoheptaose: not a substrate
-
-
?
additional information
?
-
-
63-alpha-glucosyl maltotriose: not a substrate
-
-
?
additional information
?
-
-
glycogen debranching system may be regarded as an integral part of the overall phosphorolytic pathway for the degradation of glycogen
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
substrate specificities
-
-
?
additional information
?
-
-
6-O-alpha-maltosyl cyclomaltoheptaose: not a substrate
-
-
?
additional information
?
-
-
panose: not a substrate
-
-
?
additional information
?
-
-
glycogen debranching system may be regarded as an integral part of the overall phosphorolytic pathway for the degradation of glycogen
-
-
?
additional information
?
-
-
in vivo degradation of glycogen requires the presence of both glycogen hydrolase and the enzyme
-
-
?
additional information
?
-
-
cyclization reaction also occurs with starch
-
-
?
additional information
?
-
-
glycogen debranching enzyme might play an important role in the structure of glycogen particles, or the control of its metabolism
-
-
?
additional information
?
-
-
activity with glycogen, soluble starch, amylopektin and pullulan is less than 1% of the activity with phosphorylase limit dextrin
-
-
?
additional information
?
-
-
the alpha-1,6-glycosidic linkage of dextrins (Glc-alpha-1,4)m-(Glc-alpha-1,6)Glc-alpha-1,4-(Glc-alpha-1,4)n-1-deoxy-1-[2(pyridyl)amino]-D-glucitol with m equal 0 or n equal 0 can not be hydrolyzed by the enzyme, indicating that at least the two glycosyl residues sandwiching the isomaltosyl moiety are indispensable for hydrolysis by the GDE amylo-alpha-1,6-glucosidase activity
-
-
?
additional information
?
-
-
fluorogenic dextrins with non-reducing-end isomaltosyl residues, Glcalpha1-6Glcalpha1-4(Glcalpha1-4)nGlcPA, are not hydrolysed by the GDE amylo-alpha-1,6-glucosidase found in porcine liver
-
-
?
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1,4-diaminobutane
-
putrescine, glycogen debranching enzyme, slight inhibition
1-S-dimethylarsino-1-thio-beta-D-glucanopyranoside
2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol
2-(2-hydroxyethylamino)-2-hydroxymethyl-1,3-propanediol
-
hydroxyethyltris
2-(N-morpholino)ethanesulfonic acid
-
-
2-amino-1,3-propandiol
-
-
2-amino-2-methyl-1,3-propanediol
-
-
2-deoxy-2-fluoro-alpha-glucosyl fluoride
-
very poor inhibitor, 56 mM: 17% inhibition
2-hydroxyethyl-3-hydroxypropylamine
-
HEPA, glycogen debranching enzyme
3-aminopropyl-2-hydroxyethylamine
-
DAPH, glycogen debranching enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
5-amino-D-glucose
-
nojirimycin, potent inhibitor, noncompetitive
5-thio-D-glucose
-
slight inhibition
7-O-beta-D-glucopyranosyl-homonojirimycin
-
-
alpha-homonojirimycin
-
-
aminophenyl arsenoxide
-
-
AMP
-
10 mM, 86% of initial activity
choline
-
very poor inhibitor
Co2+
-
1 mM, 15% of initial activity
Cu2+
-
1 mM, 6% of initial activity
cyclohexaamylose
-
alpha-Schardinger dextrin, debranching enzyme, competitive inhibitor
D-glucono-1,5-lactone
-
glycogen debranching enzyme, noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose
D-glucose-1-phosphate
-
10 mM, 82% of initial activity
D-Glucose-6-phosphate
-
10 mM, 89% of initial activity
deoxynojirimycin
-
reversible, specific inhibitor
DMSO
-
80.8% residual activity at 10% (v/v)
ethanol
-
83.3% residual activity at 10% (v/v)
Fe2+
-
1 mM, 7% of initial activity
glucooligosaccharides
-
containing one, two, or three glucose, competitive inhibitors
-
Hg2+
-
1 mM, 3% of initial activity
m-erythritol
-
noncompetitive
maltotriose
-
competitive
methanediimine
-
carbodiimide in the presence of an amine inhibits glycogen debranching enzyme, transferase activity is inhibited, amylo-1,6-glucosidase , hydrolysis of alpha-glucosyl fluoride, is unaffected by carbodiimide. Slow inactivation of glucosidase activity as measured by [14C]glucose incorporation into glycogen
methanol
-
91.6% residual activity at 10% (v/v)
mono-(2-ethylhexyl)phthalate
-
inhibits the activity of oligo-1,4-1,4 glucanotransferase in bifunctional amylo-1,6-glucosidase oligo-1,4-1,4 glucanotransferase, but not that of amylo-1,6-glucosidase
N,N'-bis(tris[hydroxymethyl]methyl)-1,3-diaminopropane
-
bis(tris)propane, noncompetitive
N-2-Hydroxyethylpiperazine-N'-2-ethanesulfonic acid
-
slight inhibition
N-Tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid
-
slight inhibition
Ni2+
-
1 mM, 25% of initial activity
phosphate
-
buffer, inhibits at neutral pH
SDS
-
irreversible inhibition by less than 0.1% SDS
taurine
-
slight inhibition
triethylamine
-
very poor inhibitor
Zn2+
-
1 mM, 4% of initial activity
1-deoxynojirimycin
-
-
1-deoxynojirimycin
-
in primary rat hepatocytes, the inhibition of glycogen breakdown reaches plateau at 100 microM with 25% inhibition and then remains unchanged
1-S-dimethylarsino-1-thio-beta-D-glucanopyranoside
-
DATG, active site-directed irreversible inhibitor, inhibition: mechanism. Inactivation occurs with significant conformational change
1-S-dimethylarsino-1-thio-beta-D-glucanopyranoside
-
DATG, active site-directed irreversible inhibitor, inhibition: mechanism. Inactivation occurs with significant conformational change; glycogen phosphorylase limit dextrin and Bis-Tris protect from inactivation
2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol
-
Bis-Tris, reversible inhibitor
2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol
-
10 mM: 97% inhibition; Bis-Tris, reversible inhibitor
2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol
-
Bis-Tris, reversible inhibitor; noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose
2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTNB
5,5'-dithiobis(2-nitrobenzoic acid)
-
50% inhibition, reversed by glycogen
Amine
-
protonated, hydroxylalkyl-substituted, noncompetitive, mechanism of inhibition
Amine
-
noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose; polyhydroxyamines, mechanism of inhibition; protonated, hydroxylalkyl-substituted, noncompetitive, mechanism of inhibition
D-glucose
-
10 mM, 89% of initial activity
D-glucose
-
10% inhibition by 10 mM, 50% inhibition by 50 mM
ethylamine
-
-
ethylamine
-
slight inhibition
glycylglycine
-
slight inhibition
glycylglycine
-
inhibits at acidic pH
glycylglycine
-
no inhibition at 0.01 or 0.05 M
guanidine
-
muscle and liver enzyme: inhibition at very low concentrations
guanidine
-
at 0.05 M: 20% inhibition, at 0.15 M: 50% inhibition
imidazole
-
buffer, 50% inhibition
p-hydroxymercuribenzoate
-
0.3 mM: completely
p-hydroxymercuribenzoate
-
-
Tris
-
buffer, strong inhibition
Tris
-
0.02 M Tris: 50-60% inhibition
Tris
-
noncompetitive; Tris analogues
Tris
-
15 mM: 75% inhibition
Urea
-
muscle enzyme: reversible 95% inhibition by 2 M urea, with higher concentration, 3 M urea: time-dependent irreversible denaturation, liver enzyme: reversible 57% inhibition by 2 M urea
Urea
-
muscle enzyme: reversible 95% inhibition by 2 M urea, with higher concentration, 3 M urea: time-dependent irreversible denaturation, liver enzyme: reversible 57% inhibition by 2 M urea; reversible inhibitor below 2 M, 90% inhibition by 2.6 M urea
Urea
-
glucosidase-transferase: 31% inhibition at 0.21 M, 72% at 1.6 M, 98% at 3.2 M
additional information
-
unaffected by hormone administration
-
additional information
-
inhibition mechanism
-
additional information
-
-
-
additional information
-
inhibition mechanism
-
additional information
-
inhibition mechanism; no inhibition by dithioerythritol, dithiothreitol, cadaverine, spermidine, spermine, D,L-threitol, 1-thio-beta-D-glucose
-
additional information
-
no inhibition by usual sugar phosphates or nucleotide effectors of glycolysis such as AMP, ADP, ATP, uridine diphosphoglucose, glucose-1-phosphate, glucose-6-phosphate and phosphate
-
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6-phosphofructokinase deficiency
Myopathies due to enzyme deficiencies.
amylo-alpha-1,6-glucosidase deficiency
Amylo-1,60glucosidase deficiency (glycogenosis type III) in the Faroe Islands.
amylo-alpha-1,6-glucosidase deficiency
Facial appearance in glycogen storage disease type III.
amylo-alpha-1,6-glucosidase deficiency
Glycogen Debrancher Enzyme Deficiency Myopathy.
amylo-alpha-1,6-glucosidase deficiency
Glycogen storage disease type III presenting with secondary diabetes and managed with insulin: a case report.
amylo-alpha-1,6-glucosidase deficiency
Glycogen storage disease: clinical, biochemical, and molecular heterogeneity.
amylo-alpha-1,6-glucosidase deficiency
Improvement of Cardiomyopathy After High-Fat Diet in Two Siblings with Glycogen Storage Disease Type III.
amylo-alpha-1,6-glucosidase deficiency
Myopathies due to enzyme deficiencies.
amylo-alpha-1,6-glucosidase deficiency
Myopathy and growth failure in debrancher enzyme deficiency: improvement with high-protein nocturnal enteral therapy.
amylo-alpha-1,6-glucosidase deficiency
Myopathy in debrancher enzyme deficiency.
amylo-alpha-1,6-glucosidase deficiency
Pathological characteristics of glycogen storage disease III in skeletal muscle.
amylo-alpha-1,6-glucosidase deficiency
Pregnancy associated with amylo-1,6-glucosidase deficiency (Forbe's disease). Case report.
amylo-alpha-1,6-glucosidase deficiency
[Glycogenosis caused by amylo-1,6-glucosidase deficiency. Myopathy as a lead finding in adults]
Cardiomyopathies
Facial appearance in glycogen storage disease type III.
carnitine o-palmitoyltransferase deficiency
Neonatal metabolic myopathies.
Cytochrome-c Oxidase Deficiency
Neonatal metabolic myopathies.
Genetic Diseases, Inborn
[The determination of amylo-1,6-glucosidase in biopsy specimens from human chorion]
glucan 1,4-alpha-glucosidase deficiency
A hypotonic infant with complete deficiencies of acid maltase and debrancher enzyme.
Glycogen Storage Disease
A c.3216_3217delGA mutation in AGL gene in Tunisian patients with a glycogen storage disease type III: evidence of a founder effect.
Glycogen Storage Disease
A lower energetic, protein and uncooked cornstarch intake is associated with a more severe outcome in glycogen storage disease type III: an observational study of 50 patients.
Glycogen Storage Disease
A simple assay for amylo-1,6-glucosidase to detect heterozygotes for glycogenosis type III in erythrocytes.
Glycogen Storage Disease
Accumulation of glycogen in sural nerve axons in adult-onset type III glycogenosis.
Glycogen Storage Disease
ACTION OF AMYLO-1,6-GLUCOSIDASE ON LOW MOLECULAR WEIGHT SUBSTRATES AND THE ASSAY OF THIS ENZYME IN GLYCOGEN STORAGE DISEASE.
Glycogen Storage Disease
Amylo-1,6-glucosidase activity and glycogen content of the erythrocytes of normal subjects, patients with glycogen storage disease and heterozygotes.
Glycogen Storage Disease
Amylo-1,6-glucosidase activity in cultured cells: a deficiency in type III glycogenosis with prenatal studies.
Glycogen Storage Disease
AMYLO-1,6-GLUCOSIDASE ACTIVITY IN LEUCOCYTES FROM PATIENTS WITH GLYCOGEN STORAGE DISEASE.
Glycogen Storage Disease
Amylo-1,6-glucosidase in human fibroblasts: studies 3 glycogen storage disease.
Glycogen Storage Disease
Amylo-1,60glucosidase deficiency (glycogenosis type III) in the Faroe Islands.
Glycogen Storage Disease
Case report: rupture of a gastric varix in liver cirrhosis associated with glycogen storage disease type III.
Glycogen Storage Disease
Clinical and genetic variability of glycogen storage disease type IIIa: seven novel AGL gene mutations in the Mediterranean area.
Glycogen Storage Disease
Clinical, biochemical and genetic features of glycogen debranching enzyme deficiency.
Glycogen Storage Disease
Debrancher enzyme activity in blood cells of families with type III glycogen storage disease. A method for diagnosis of heterozygotes.
Glycogen Storage Disease
Glycogen debranching enzyme: purification, antibody characterization, and immunoblot analyses of type III glycogen storage disease.
Glycogen Storage Disease
Glycogen storage disease type III in Egyptian children: a single centre clinico-laboratory study.
Glycogen Storage Disease
Glycogen storage disease type III in the Irish population.
Glycogen Storage Disease
Glycogen storage disease type IIIa presenting as non-ketotic hypoglycemia: use of a newly approved commercially available mutation analysis to non-invasively confirm the diagnosis.
Glycogen Storage Disease
History of settlement of villages from Central Tunisia by studying families sharing a common founder Glycogenosis type III mutation.
Glycogen Storage Disease
Improvement of Cardiomyopathy After High-Fat Diet in Two Siblings with Glycogen Storage Disease Type III.
Glycogen Storage Disease
Liver transplantation in patients with type IIIa glycogen storage disease, cirrhosis and hepatocellular carcinoma.
Glycogen Storage Disease
Metabolic myopathies.
Glycogen Storage Disease
Molecular and biochemical characterization of Tunisian patients with glycogen storage disease type III.
Glycogen Storage Disease
Molecular characterisation of GSD III subjects and identification of six novel mutations in AGL.
Glycogen Storage Disease
Mutational analysis of the AGL gene: five novel mutations in GSD III patients.
Glycogen Storage Disease
Neonatal metabolic myopathies.
Glycogen Storage Disease
Possible prenatal diagnosis of type III glycogenosis.
Glycogen Storage Disease
Reduction in bone mineral density in glycogenosis type III may be due to a mixed muscle and bone deficit.
Glycogen Storage Disease
Studies in glycogen storage disease type 3: kinetics of amylo-1,6-glucosidase in human erythrocytes.
Glycogen Storage Disease
Studies on a patient with in vivo evidence of type I glycogenosis and normal enzyme activities in vitro.
Glycogen Storage Disease
The ischemic exercise test in normal adults and in patients with weakness and cramps.
Glycogen Storage Disease
Type III glycogen storage disease: an adult case with mild disease but complete absence of debrancher protein.
Glycogen Storage Disease
[A case of glycogen storage myopathy with acute heart failure]
Glycogen Storage Disease
[Evaluation of a fluorimetric for determining the activity of amylo-1,6-glucosidase in leukocytes for confirming the diagnosis of glycogen storage disease type III].
Glycogen Storage Disease
[Glycogen storage disease caused by absence of amylo-1,6-glucosidase. Hepatomuscular and isolated hepatic forms.]
Glycogen Storage Disease
[Glycogenosis caused by amylo-1,6-glucosidase deficiency. Myopathy as a lead finding in adults]
Glycogen Storage Disease
[Mutation analysis of glycogen debrancher enzyme gene in five Chinese patients with glycogen storage disease type III]
Glycogen Storage Disease
[Nine cases of debrancher deficiency (glycogen storage disease type III) presenting muscle weakness--study on clinicobiochemical analysis]
Glycogen Storage Disease
[Serum lipoproteins in the generalized form of type III glycogenosis]
Glycogen Storage Disease Type II
A hypotonic infant with complete deficiencies of acid maltase and debrancher enzyme.
Glycogen Storage Disease Type III
A c.3216_3217delGA mutation in AGL gene in Tunisian patients with a glycogen storage disease type III: evidence of a founder effect.
Glycogen Storage Disease Type III
A lower energetic, protein and uncooked cornstarch intake is associated with a more severe outcome in glycogen storage disease type III: an observational study of 50 patients.
Glycogen Storage Disease Type III
Case report: rupture of a gastric varix in liver cirrhosis associated with glycogen storage disease type III.
Glycogen Storage Disease Type III
Clinical and genetic variability of glycogen storage disease type IIIa: seven novel AGL gene mutations in the Mediterranean area.
Glycogen Storage Disease Type III
Glycogen storage disease type III in Egyptian children: a single centre clinico-laboratory study.
Glycogen Storage Disease Type III
Glycogen storage disease type III in the Irish population.
Glycogen Storage Disease Type III
Glycogen storage disease type IIIa presenting as non-ketotic hypoglycemia: use of a newly approved commercially available mutation analysis to non-invasively confirm the diagnosis.
Glycogen Storage Disease Type III
History of settlement of villages from Central Tunisia by studying families sharing a common founder Glycogenosis type III mutation.
Glycogen Storage Disease Type III
Molecular and biochemical characterization of Tunisian patients with glycogen storage disease type III.
Glycogen Storage Disease Type III
Molecular characterisation of GSD III subjects and identification of six novel mutations in AGL.
Glycogen Storage Disease Type III
Mutational analysis of the AGL gene: five novel mutations in GSD III patients.
Glycogen Storage Disease Type III
Pathological characteristics of glycogen storage disease III in skeletal muscle.
Glycogen Storage Disease Type III
Reduction in bone mineral density in glycogenosis type III may be due to a mixed muscle and bone deficit.
Glycogen Storage Disease Type III
Studies in glycogen storage disease type 3: kinetics of amylo-1,6-glucosidase in human erythrocytes.
Glycogen Storage Disease Type III
[Mutation analysis of glycogen debrancher enzyme gene in five Chinese patients with glycogen storage disease type III]
Glycogen Storage Disease Type III
[Nine cases of debrancher deficiency (glycogen storage disease type III) presenting muscle weakness--study on clinicobiochemical analysis]
Hepatomegaly
Facial appearance in glycogen storage disease type III.
Hepatomegaly
[Glycogenosis caused by amylo-1,6-glucosidase deficiency. Myopathy as a lead finding in adults]
Hypoglycemia
[Glycogenosis caused by amylo-1,6-glucosidase deficiency. Myopathy as a lead finding in adults]
Muscle Hypotonia
Neonatal metabolic myopathies.
Muscle Weakness
Myopathies due to enzyme deficiencies.
Muscle Weakness
[Nine cases of debrancher deficiency (glycogen storage disease type III) presenting muscle weakness--study on clinicobiochemical analysis]
Muscular Diseases
Debrancher deficiency neuromuscular disorder with pseudohypertrophy in two brothers.
Muscular Diseases
Facial appearance in glycogen storage disease type III.
Muscular Diseases
Glycogen Debrancher Enzyme Deficiency Myopathy.
Muscular Diseases
Myopathy and growth failure in debrancher enzyme deficiency: improvement with high-protein nocturnal enteral therapy.
Muscular Diseases
Myopathy in debrancher enzyme deficiency.
Muscular Diseases
[Glycogenosis caused by amylo-1,6-glucosidase deficiency. Myopathy as a lead finding in adults]
Myoglobinuria
Metabolic myopathies.
Myoglobinuria
Neonatal metabolic myopathies.
Polyneuropathies
Accumulation of glycogen in sural nerve axons in adult-onset type III glycogenosis.
Protein Deficiency
Neonatal metabolic myopathies.
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Scopes, R.K.; Stoter, A.
Purification of all glycolytic enzymes from one muscle extract
Methods Enzymol.
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479-490
1982
Oryctolagus cuniculus
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Properties of yeast debranching enzyme and its specificity toward branched cyclodextrins
Eur. J. Biochem.
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1992
Saccharomyces cerevisiae, Oryctolagus cuniculus
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Lee, E.Y.C.; Whelan, W.J.
Glycogen and starch debranching enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
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Saccharomyces cerevisiae, Oryctolagus cuniculus, Homo sapiens, Mammalia
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Crystallization of glycogen debranching enzyme
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Oryctolagus cuniculus
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Palmer, T.N.; Ryman, B.E.
The regulatory role of amylo-1,6-glucosidase/oligo-1,4->1,4-glucantransferase in liver glycogen metabolism
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1971
Canis lupus familiaris
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White, R.C.; Ruff, C.J.; Nelson, T.E.
Purification of glycogen debranching enzyme from rabbit muscle using omega-aminoalkyl agarose chromatography
Anal. Biochem.
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1981
Oryctolagus cuniculus
brenda
Gillard, B.K.; White, R.C.; Zingaro, R.A.; Nelson, T.E.
Amylo-1,6-glucosidase/4-alpha-glucanotransferase. Reaction of rabbit muscle debranching enzyme with an active site-directed irreversible inhibitor, 1-S-dimethylarsino-1-thio-beta-D-glucopyranoside
J. Biol. Chem.
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1980
Oryctolagus cuniculus, Mammalia
brenda
Heizmann, C.W.; Eppenberger, H.M.
Glycogen debranching enzyme from chicken pectoralis muscle. Comparison with a 165 000 mol. wt myofibrillar protein
FEBS Lett.
105
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1979
Gallus gallus
brenda
White, R.C.; Nelson, T.E.
Analytical gel chromatography of rabbit muscle amylo-1,6-glucosidase/4-alpha-glucanotransferase under denaturing and non-denaturing conditions
Biochim. Biophys. Acta
400
154-161
1975
Oryctolagus cuniculus
brenda
White, R.C.; Nelson, T.E.
Re-evaluation of the subunit structure and molecular weight of rabbit muscle amylo-1,6-glucosidase/4-alpha-glucanotransferase
Biochim. Biophys. Acta
365
274-280
1974
Oryctolagus cuniculus
brenda
Lee, E.Y.C.; Carter, J.H.
Subunit structure of yeast and rabbit-muscle glucosidase-transferases
FEBS Lett.
32
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1973
Saccharomyces cerevisiae, Oryctolagus cuniculus, Mammalia
brenda
Brown, D.H.; Gordon, R.B.; Illingworth Brown, B.
Studies on the structure and mechanism of action of the glycogen debranching enzymes of muscle and liver
Ann. N. Y. Acad. Sci.
210
238-253
1973
Oryctolagus cuniculus
brenda
Lee, E.Y.C.; Carter, J.H.
Amylo-1,6-glucosidase/1,4-alpha-glucan: 1,4-alpha-glucan 4-alpha-glycosyltransferase: specificity toward polysaccharide substrates
Arch. Biochem. Biophys.
154
636-641
1973
Saccharomyces cerevisiae, Oryctolagus cuniculus
brenda
Gordon, R.B.; Brown, D.H.; Illingworth Brown, B.
Preparation and properties of the glycogen-debranching enzyme from rabbit liver
Biochim. Biophys. Acta
289
97-107
1972
Oryctolagus cuniculus
brenda
Watts, T.E.; Nelson, T.E.
Improved purification procedure for rabbit muscle amylo-1,6-glucosidase/oligo-1,4 -> 1,4-glucantransferase
Anal. Biochem.
49
479-491
1972
Oryctolagus cuniculus
brenda
Manners, D.J.
Specificity of debranching enzymes
Nature New Biol.
234
150-151
1971
Saccharomyces cerevisiae, Mammalia
brenda
Stark, J.R.; Thambyrajah, V.
Studies on the reverse action of amylo-1,6-glucosidase
Biochem. J.
120
17P-18P
1970
Oryctolagus cuniculus
brenda
Huijing, F.; Lee, E.Y.C.; Carter, J.H.; Whelan, W.J.
Branching action of amylo-1,6-glucosidase/oligo-1,4->1,4-glucantransferase
FEBS Lett.
7
251-254
1970
Saccharomyces cerevisiae, Oryctolagus cuniculus, Mammalia
brenda
Justice, P.; Ryan, C.; Hsia, D.Y.Y.; Krmpotik, E.
Amylo-1,6-glucosidase in human fibroblasts: studies in type III glycogen storage disease
Biochem. Biophys. Res. Commun.
39
301-306
1970
Homo sapiens
brenda
Lee, E.Y.C.; Carter, J.H.; Nielsen, L.D.; Fischer, E.H.
Purification and properties of yeast amylo-1,6-glucosidase-oligo-1,4 -> 1,4-glucantransferase
Biochemistry
9
2347-2355
1970
Saccharomyces cerevisiae
brenda
Nelson, T.E.; Larner, J.
Studies on the action of amylo-I,6-glucosidase
Biochim. Biophys. Acta
198
538-545
1970
Oryctolagus cuniculus
brenda
Nelson, T.E.; Kolb, E.; Larner, J.
Reinvestigation of the pH optimum in terms of the action and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4 -> 1,4-transferase
Biochim. Biophys. Acta
167
212-215
1968
Oryctolagus cuniculus
brenda
Brown, D.H.; Illingworth Brown, B.
Enzymes of glycogen debranching: amylo-1,6-glucosidase (I) and oligo-1,4 -> 1,4-glucantransferase (II)
Methods Enzymol.
8
515-524
1966
Oryctolagus cuniculus
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brenda
Taylor, P.M.; Whelan, W.J.
Rabbit muscle amylo-1,6-glucosidase: properties and evidence of heterogeneity
Control of Glycogen Metabolism, Proc. FEBS 4th Meeting, Oslo, 1967 (Whelan, W. J. , ed. )
101-114
1968
Oryctolagus cuniculus
-
brenda
Nelson, T.E.; Kolb, E.; Larner, J.
Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4->1,4-transferase
Biochemistry
8
1419-1428
1969
Oryctolagus cuniculus
brenda
Liu, W.; Madsen, N.B.; Braun, C.; Withers, S.G.
Reassessment of the catalytic mechanism of glycogen debranching enzyme
Biochemistry
30
1419-1424
1991
Oryctolagus cuniculus
brenda
Liu, W.; Madsen, N.B.; Fan, B.; Zucker, K.A.; Glew, R.H.; Fry, D.E.
Effects of oligosaccharide binding on glycogen debranching enzyme activity and conformation
Biochemistry
34
7056-7061
1995
Oryctolagus cuniculus
brenda
Liu, W.; De Castro, M.L.; Takrama, J.; Bilous, P.T.; Vinayagamoorthy, T.; Madsen, N.B.; Bleackley, R.C.
Molecular cloning, sequencing, and analysis of the cDNA for rabbit muscle glycogen debranching enzyme
Arch. Biochem. Biophys.
306
232-239
1993
Oryctolagus cuniculus
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Becker, J.U.; Long, T.J.; Fischer, E.H.
Purification and properties of debranching enzyme from dogfish muscle
Biochemistry
16
291-297
1977
Squalus acanthias
brenda
Takrama, J.; Madsen, N.B.
Binding of glycogen, oligosaccharides, and glucose to glycogen debranching enzyme
Biochemistry
27
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1988
Oryctolagus cuniculus
brenda
Gillard, B.K.; Nelson, T.E.
Amylo-1,6-glucosidase/4-alpha-glucanotransferase: use of reversible substrate model inhibitors to study the binding and active sites of rabbit muscle debranching enzyme
Biochemistry
16
3978-3987
1977
Oryctolagus cuniculus
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Taylor, C.; Cox, A.J.; Kernohan, J.C.; Cohen, P.
Debranching enzyme from rabbit skeletal muscle. Purification, properties and physiological role
Eur. J. Biochem.
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1975
Oryctolagus cuniculus
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Bates, E.J.; Heaton, G.M.; Taylor, C.; Kernohan, J.C.; Cohen, P.
Debranching enzyme from rabbit skeletal muscle: evidence for the location of two active centres on a single polypeptide chain
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1975
Oryctolagus cuniculus
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Ryman, B.E.; Whelan, W.J.
New aspects of glycogen metabolism
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1971
Saccharomyces cerevisiae, Oryctolagus cuniculus, Mammalia
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Yang, B.Z.; Ding, J.H.; Enghild, J.J.; Bao, Y.; Chen, Y.T.
Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme
J. Biol. Chem.
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Homo sapiens, Sus scrofa
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Fitzgerald, P.M.D.; Madsen, N.B.
Improvement of limit of diffraction and useful x-ray lifetime of crystals of glycogen debranching enzyme
J. Crystal Growth
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Oryctolagus cuniculus
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Nakayama, A.; Yamamoto, K.; Tabata, S.
High expression of glycogen-debranching enzyme in Escherichia coli and its competent purification method
Protein Expr. Purif.
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Saccharomyces cerevisiae
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Glycogen debranching enzyme is associated with rat skeletal muscle sarcoplasmic reticulum
Acta Physiol. Scand.
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Rattus norvegicus
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Yanase, M.; Takata, H.; Takaha, T.; Kuriki, T.; Smith, S.M.; Okada, S.
Cyclization reaction catalyzed by glycogen debranching enzyme (EC 2.4.1.25/EC 3.2.1.33) and its potential for cycloamylose production
Appl. Environ. Microbiol.
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2002
Saccharomyces cerevisiae
brenda
Teste, M.A.; Enjalbert, B.; Parrou, J.L.; Francois, J.M.
The Saccharomyces cerevisiae YPR184w gene encodes the glycogen debranching enzyme
FEMS Microbiol. Lett.
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Saccharomyces cerevisiae
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Narahara, E.; Makino, Y.; Omichi, K.
Glycogen debranching enzyme in bovine brain
J. Biochem.
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2001
Bos taurus
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Nakayama, A.; Yamamoto, K.; Tabata, S.
Identification of the catalytic residues of bifunctional glycogen debranching enzyme
J. Biol. Chem.
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2001
Saccharomyces cerevisiae
brenda
Kylae-Puhju, M.; Ruusunen, M.; Puolanne, E.
Activity of porcine muscle glycogen debranching enzyme in relation to pH and temperature
Meat Sci.
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2004
Sus scrofa
brenda
Makino, Y.; Omichi, K.
Purification of glycogen debranching enzyme from porcine brain: evidence for glycogen catabolism in the brain
Biosci. Biotechnol. Biochem.
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Sus scrofa
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Watanabe, Y.; Makino, Y.; Omichi, K.
Activation of 4-alpha-glucanotransferase activity of porcine liver glycogen debranching enzyme with cyclodextrins
J. Biochem.
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Sus scrofa
brenda
Herszberg, B.; Mata, X.; Giulotto, E.; Decaunes, P.; Piras, F.M.; Chowdhary, B.P.; Chaffaux, S.; Guerin, G.
Characterization of the equine glycogen debranching enzyme gene (AGL): Genomic and cDNA structure, localization, polymorphism and expression
Gene
404
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2007
Equus caballus (A8BQB4)
brenda
Makino, Y.; Omichi, K.
Acceptor specificity of 4-alpha-glucanotransferases of mammalian glycogen debranching enzymes
J. Biochem.
139
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2006
Bos taurus, Oryctolagus cuniculus, Sus scrofa
brenda
Yamamoto, E.; Makino, Y.; Omichi, K.
Active site mapping of amylo-alpha-1,6-glucosidase in porcine liver glycogen debranching enzyme using fluorogenic 6-O-alpha-glucosyl-maltooligosaccharides
J. Biochem.
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2007
Sus scrofa
brenda
Van, T.T.; Ryu, S.I.; Lee, K.J.; Kim, E.J.; Lee, S.B.
Cloning and characterization of glycogen-debranching enzyme from hyperthermophilic archaeon Sulfolobus shibatae
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Saccharolobus shibatae
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Park, J.; Park, H.; Kang, H.; Hong, J.; Cha, H.; Woo, E.; Kim, J.; Kim, M.; Boos, W.; Lee, S.; Park, K.
Oligomeric and functional properties of a debranching enzyme (TreX) from the archaeon Sulfolobus solfataricus P2
Biocatal. Biotransform.
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2008
Saccharolobus solfataricus (Q7LX99), Saccharolobus solfataricus P2 (Q7LX99)
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Woo, E.J.; Lee, S.; Cha, H.; Park, J.T.; Yoon, S.M.; Song, H.N.; Park, K.H.
Structural Insight into the Bifunctional Mechanism of the Glycogen-debranching Enzyme TreX from the Archaeon Sulfolobus solfataricus
J. Biol. Chem.
283
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2008
Saccharolobus solfataricus (P95868)
brenda
Kuriyama, C.; Kamiyama, O.; Ikeda, K.; Sanae, F.; Kato, A.; Adachi, I.; Imahori, T.; Takahata, H.; Okamoto, T.; Asano, N.
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures
Bioorg. Med. Chem.
16
7330-7336
2008
Oryctolagus cuniculus, Rattus norvegicus
brenda
Cheng, A.; Zhang, M.; Okubo, M.; Omichi, K.; Saltiel, A.R.
Distinct mutations in the glycogen debranching enzyme found in Glycogen Storage Disease Type III lead to impairment in diverse cellular functions
Hum. Mol. Genet.
18
2045-2052
2009
Homo sapiens (P35573)
brenda
Kuramori, C.; Hase, Y.; Hoshikawa, K.; Watanabe, K.; Nishi, T.; Hishiki, T.; Soga, T.; Nashimoto, A.; Kabe, Y.; Yamaguchi, Y.; Watanabe, H.; Kataoka, K.; Suematsu, M.; Handa, H.
Mono-(2-ethylhexyl)phthalate targets glycogen debranching enzyme and affects glycogen metabolism in rat testis
Toxicol. Sci.
109
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2009
Rattus norvegicus
brenda
Choi, J.; Lee, H.; Kim, Y.; Park, J.; Woo, E.; Kim, M.; Lee, B.; Park, K.
Characterization of a novel debranching enzyme from Nostoc punctiforme possessing a high specificity for long branched chains
Biochem. Biophys. Res. Commun.
378
224-229
2009
Nostoc punctiforme
brenda
Yamamoto, E.; Watanabe, Y.; Makino, Y.; Omichi, K.
Ispection of the activator binding site for 4-alpha-glucanotransferase in porcine liver glycogen debranching enzyme with fluorogenic dextrins
J. Biochem.
145
585-590
2009
Sus scrofa
brenda
Doi, S.; Makino, Y.; Omichi, K.
Discrimination of porcine glycogen debranching enzyme isozymes by the ratios of their 4-alpha-glucanotransferase and amylo-alpha-1,6-glucosidase activities
J. Biochem.
147
851-856
2010
Sus scrofa
brenda
Nguyen, D.H.; Park, J.T.; Shim, J.H.; Tran, P.L.; Oktavina, E.F.; Nguyen, T.L.; Lee, S.J.; Park, C.S.; Li, D.; Park, S.H.; Stapleton, D.; Lee, J.S.; Park, K.H.
The reaction kinetics and the effect of substrate transglycosylation catalyzed by TreX of Sulfolobus solfataricus on glycogen breakdown
J. Bacteriol.
196
1941-1949
2014
Saccharolobus solfataricus (Q7LX99), Saccharolobus solfataricus P2 (Q7LX99)
brenda
Min-Ho, L.; Hyung-Nam, S.; Ji-Eun, C.; Lan, T.P.; Sunghoon, P.; Jong-Tae, P.; Eui-Jeon, W.
Association of bi-functional activity in the N-terminal domain of glycogen debranching enzyme
Biochem. Biophys. Res. Commun.
445
107-112
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae D349
brenda
Sottnik, J.L.; Mallaredy, V.; Chauca-Diaz, A.; Ritterson Lew, C.; Owens, C.; Dancik, G.M.; Pagliarani, S.; Lucchiari, S.; Moggio, M.; Ripolone, M.; Comi, G.P.; Frierson, H.F.; Clouthier, D.; Theodorescu, D.
Elucidating the role of Agl in bladder carcinogenesis by generation and characterization of genetically engineered mice
Carcinogenesis
40
194-201
2019
Mus musculus
brenda