Information on EC 3.2.1.33 - amylo-alpha-1,6-glucosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.2.1.33
-
RECOMMENDED NAME
GeneOntology No.
amylo-alpha-1,6-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
endoglycosidic
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycogen degradation II
-
-
glycogen metabolism
-
-
Starch and sucrose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
glycogen phosphorylase-limit dextrin 6-alpha-glucohydrolase
This enzyme hydrolyses an unsubstituted glucose unit linked by an alpha(1->6) bond to an alpha(1->4) glucose chain. The enzyme activity found in mammals and yeast is in a 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 then hydrolyse. Together, these two activities constitute the glycogen debranching system.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-47-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PCC73102
-
-
Manually annotated by BRENDA team
strain PCC73102
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pacific dogfish
-
-
Manually annotated by BRENDA team
strain ATCC 51178
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
show the reaction diagram
2-deoxy-2-fluoro-alpha-D-glucosyl fluoride
?
show the reaction diagram
-
poor substrate
-
-
?
6-O-alpha-D-glucosyl cyclodextrin + H2O
D-glucose + cyclodextrin
show the reaction diagram
6-O-alpha-D-glucosyl cyclomalto-octaose + H2O
D-glucose + cyclomalto-octaose
show the reaction diagram
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
D-glucose + cyclomaltoheptaose
show the reaction diagram
6-O-alpha-D-glucosyl cyclomaltohexaose + H2O
D-glucose + cyclomaltohexaose
show the reaction diagram
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
?
show the reaction diagram
6-O-alpha-maltosyl-beta-cyclodextrin + H2O
maltose + beta-cyclodextrin
show the reaction diagram
-
-
-
-
?
6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O
?
show the reaction diagram
6-O-alpha-maltotetraosyl-beta-cyclodextrin + H2O
?
show the reaction diagram
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
?
show the reaction diagram
63-alpha-glucosyl maltopentaose + H2O
maltopentaose + D-glucose
show the reaction diagram
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
63-alpha-maltotriosyl maltotetraose + H2O
?
show the reaction diagram
63-O-alpha-glucosyl-PA-maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
-
-
-
?
alpha-(1-6)-glucosyl cycloheptaamylose + H2O
cycloheptaamylose + D-glucose
show the reaction diagram
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
alpha-D-glucosyl fluoride
fluoride + D-glucose
show the reaction diagram
alpha-dextrin + H2O
alpha-dextrin + D-glucose
show the reaction diagram
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
amylopectin + H2O
maltose + ?
show the reaction diagram
amylose
cycloamylose
show the reaction diagram
-
-
degree of polymerization between 11 and 50
-
?
amylose + H2O
?
show the reaction diagram
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
beta-cyclodextrin-alpha-1,6-linked maltopentaose + H2O
beta-cyclodextrin + maltopentaose
show the reaction diagram
-
-
-
?
beta-cyclodextrin-alpha-1,6-linked maltotetraose + H2O
beta-cyclodextrin + maltotetraose
show the reaction diagram
-
-
-
?
beta-cyclodextrin-alpha-1,6-linked maltotriose + H2O
beta-cyclodextrin + maltotriose
show the reaction diagram
-
-
-
?
branched cyclodextrin + H2O
?
show the reaction diagram
D-glucose + maltooligosaccharide
maltooligosaccharide
show the reaction diagram
D-glucose-beta-cyclodextrin + H2O
D-glucose + beta-cyclodextrin
show the reaction diagram
G3-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
G4-beta-cyclodextrin + H2O
?
show the reaction diagram
-
GlgX shows substrate specificity for G4 phosphorylase-limit dextrin
-
-
?
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
show the reaction diagram
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Glcalpha1-6Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4GlcPA + H2O
?
show the reaction diagram
-
-
-
-
?
glycogen + H2O
?
show the reaction diagram
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
glycogen limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
maltodecaose + H2O
?
show the reaction diagram
maltodecaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
maltododecaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltoheptaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
maltohexaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
maltononaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltononaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
maltooctaose + H2O
?
show the reaction diagram
maltooctaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
maltopentaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
maltotetraosyl-alpha-1,6 maltoheptaose + H2O
?
show the reaction diagram
maltoundecaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltoundecaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
phosphorylase beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
phosphorylase limit dextrin + H2O
?
show the reaction diagram
-
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
-
-
?
pullulan + H2O
-
show the reaction diagram
pullulan + H2O
?
show the reaction diagram
-
36.8% activity compared to amylopectin
-
-
?
rice starch + H2O
?
show the reaction diagram
-
82.4% activity compared to amylopectin
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
glycogen + H2O
?
show the reaction diagram
-
total degradation of glycogen requires combined actions of glycogen phosphorylase and glucosidase/transferase. Glucosidase/transferase: regulatory role of glycogen metabolism in liver
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
27.3% increase of activity at 5 mM
Co2+
-
15% increase of activity at 5 mM
Fe2+
-
40.6% increase of activity at 5 mM
Mg2+
-
17.2% increase of activity at 5 mM
Mn2+
-
62.2% increase of activity at 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-diaminobutane
-
putrescine, glycogen debranching enzyme, slight inhibition
1-deoxynojirimycin
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
ATP
-
10 mM, no activity
cationic buffer
-
-
-
Cd2+
-
1 mM, no 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
D-glucose-1-phosphate
-
10 mM, 82% of initial activity
D-Glucose-6-phosphate
-
10 mM, 89% of initial activity
D-isofagomine
-
-
deoxynojirimycin
-
reversible, specific inhibitor
diethanolamine
-
-
DMSO
-
80.8% residual activity at 10% (v/v)
ethanol
-
83.3% residual activity at 10% (v/v)
ethanolamine
-
-
ethylamine
Fe2+
-
1 mM, 7% of initial activity
glucooligosaccharides
-
containing one, two, or three glucose, competitive inhibitors
-
glycogen
-
competitive
glycylglycine
guanidine
Hg2+
-
1 mM, 3% of initial activity
hydroxylamine
-
-
imidazole
m-erythritol
-
noncompetitive
maltose
-
competitive
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
NH4+
-
slight inhibition
Ni2+
-
1 mM, 25% of initial activity
organic arsenites
-
-
-
p-hydroxymercuribenzoate
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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-cyclodextrin
-
20 mM: 2.3fold activation
amylopectin
-
potent activator
DMSO
-
catalytic activity is promoted in the presence of DMSO. DMSO affects the oligomerization state, causing the enzyme dimers to associate into tetramers
Glcalpha1-6Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4GlcPA
-
-
glucooligosaccharides
-
with four or more glucose units, uncompetitive activation
-
glycogen
-
potent activator
maltohexaose
-
20 mM: 1.86fold activation
maltopentaose
-
20 mM: 1.45fold activation
maltotetraose
-
20 mM: 1.15fold activation
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.9 - 19.3
6-O-alpha-D-glucosyl cyclomaltoheptaose
12.23
6-O-alpha-maltosyl-beta-cyclodextrin
-
at 70C in 50 mM sodium acetate buffer (pH 5.5)
0.206
6-O-alpha-maltotetraosyl-beta-cyclodextrin
-
pH 5.5, 75C
1.8 - 4.45
63-alpha-glucosyl maltotetraose
5.6
63-alpha-maltotriosyl maltotetraose
-
branched heptasaccharide B7, muscle enzyme
-
2.8 - 8.1
alpha-glucosyl fluoride
4.3 - 11
amylopectin beta-dextrin
3.8 - 7.2
beta-amylase limit dextrin
0.15
beta-cyclodextrin-alpha-1,6-linked maltotetraose
pH 7, 37C
1.5
beta-cyclodextrin-alpha-1,6-linked maltotriose
pH 7, 37C
32 - 43
D-glucose
1.51
G3-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
0.15
G4-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
0.063 - 1.6
glycogen phosphorylase limit dextrin
0.64
maltodecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.62
maltododecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.81
maltononaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.51
maltoundecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
additional information
amylopectin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2570
6-O-alpha-maltotetraosyl-beta-cyclodextrin
Sulfolobus solfataricus
-
pH 5.5, 75C
0.48 - 17.35
amylopectin
41.7
beta-cyclodextrin-alpha-1,6-linked maltotetraose
Escherichia coli
P15067
pH 7, 37C
38
beta-cyclodextrin-alpha-1,6-linked maltotriose
41.7
G4-beta-cyclodextrin
Escherichia coli
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
0.045
maltodecaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.0478
maltododecaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.0205
maltononaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.0452
maltoundecaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
300
beta-cyclodextrin-alpha-1,6-linked maltotetraose
Escherichia coli
P15067
pH 7, 37C
41692
26
beta-cyclodextrin-alpha-1,6-linked maltotriose
300
G4-beta-cyclodextrin
Escherichia coli
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
40103
0.07
maltodecaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
13345
0.177
maltodecaosyl-alpha-(1,6)-beta-cyclodextrin
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
156527
0.077
maltododecaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
40105
0.0145
maltoheptaosyl-alpha-(1,6)-beta-cyclodextrin
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
156529
0.003
maltohexaosyl-alpha-(1,6)-beta-cyclodextrin
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
156530
0.025
maltononaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
5991
0.117
maltononaosyl-alpha-(1,6)-beta-cyclodextrin
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
156526
0.0027
maltooctaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
3083
0.103
maltooctaosyl-alpha-(1,6)-beta-cyclodextrin
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
156525
0.0027
maltopentaosyl-alpha-(1,6)-beta-cyclodextrin
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
156531
0.09
maltoundecaose
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
12601
0.173
maltoundecaosyl-alpha-(1,6)-beta-cyclodextrin
Nostoc punctiforme
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
156528
additional information
additional information
Sulfolobus solfataricus
-
catalytic efficiency (the kcat/Km ratio) increases as the degree of polymerization of branch chains rises
2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
guanidine
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00019
1-deoxynojirimycin
Oryctolagus cuniculus
-
-
0.0061
7-O-beta-D-glucopyranosyl-homonojirimycin
Oryctolagus cuniculus
-
-
0.00011
alpha-homonojirimycin
Oryctolagus cuniculus
-
-
0.48
D-isofagomine
Oryctolagus cuniculus
-
-
0.0021
fagomine
Oryctolagus cuniculus
-
-
0.00039
miglitol
Oryctolagus cuniculus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.82
-
substrate: 63-alpha-glucosyl maltotetraose
3.9
-
substrate: limit dextrin
4
-
substrate: glycogen phosphorylase-limit dextrin
4.5
-
liver enzyme
4.91
-
pH 6.5, 37C
8 - 10
-
muscle enzyme
3100
-
37C, pH 6.5
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
imidazole buffer, about 50% inhibition
5.5 - 6.3
-
-
6.1 - 6.4
-
sodium citrate/mercaptoethanol buffer
7.6
-
citrate buffer
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 9
-
inactive below pH 4.6 and above pH 9
5 - 6.5
-
pH 5.0: about 20% of maximal activity, pH 6.5: about 85% of maximal activity, pH 7.0: about 15% of maximal activity
5 - 7
-
pH 5.0: about 25% of maximal activity, pH 5.5: about 70% of maximal activity, pH 6.5: about 60% of maximal activity, pH 7.0: about 20% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 80
-
65C: about 45% of maximal activity, 80C: about 80% of maximal activity
additional information
-
the activity of glycogen debranching enzyme decreases strongly when the temperature decreases from values of 39C and 42C, found just after slaughter to values of 4 and 15C. The activity begins to fall at temperatures below 39C and is almost zero when the temperature decreases to below 15C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cultivated
Manually annotated by BRENDA team
-
from skin biopsies
Manually annotated by BRENDA team
-
primary culture
Manually annotated by BRENDA team
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of hepatocyte
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
protein-glycogen particle from skeletal muscle, glycogen debranching enzyme component of
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
141000
-
dimeric enzyme form, analytical ultracentrfugation
160000 - 170000
160000
162000
-
glycogen debranching enzyme, carboxymethylation prior to sedimentation equilibrium
164000
-
glycogen debranching enzyme, sedimentation equilibrium
166000
-
glycogen debranching enzyme, PAGE and SDS-PAGE
169200
-
glycogen debranching enzyme, muscle enzyme, equilibrium ultracentrifugation
170000
172600
-
glycogen debranching enzyme, calculated from cDNA-derived amino acid sequence
177500
-
glycogen debranching enzyme, calculated from cDNA-derived amino acid sequence
179300
-
glycogen debranching enzyme, liver enzyme, sucrose density gradient centrifugation
190000
-
gel filtration
210000
-
glycogen debranching enzyme, gel filtration and PAGE
250000
-
glycogen debranching enzyme, low-speed sedimentation equilibrium centrifugation, enzyme has tendency to associate from monomeric form, about 160000 Da, to higher molecular weight species at a protein concentration greater than about 5 mg/ml
267000 - 279000
280000
355000
-
tetrameric enzyme form, analytical ultracentrfugation
640000
-
gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
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no covalently bound phosphate or carbohydrate, method would not have detected less than 5% carbohydrate
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M sodium citrate, 47% (v/v) MPD, 4% (v/v) PEG 3350, and HEPES (pH 8.0) buffer
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to 2.25 A resolution. Structure reveals a monomer consisting of three major domains with high structural similarity to the subunit of TreX, the oligomeric bifunctional glycogen debranching enzyme from Sulfolobus. In the overlapping substrate binding groove, conserved residues Leu270, Asp271, and Pro208 block the cleft, yielding a shorter narrow GlgX cleft compared to that of TreX. Residues 207-213 form a unique helical conformation that is observed in both GlgX and TreX, possibly distinguishing GDEs from isoamylases and pullulanases
3.0 A resolution; glycogen debranching enzyme
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glycogen debranching enzyme
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native dimer, native tetramer and the tetramer in complex with acarbose ligand covalently bound to residue D363, occupying subsites -1 to -3. Protein exhibits two different active-site configurations depending on its oligomeric state. The N-terminus of one subunit is located at the active site of the other molecule, resulting in a reshaping of the active site in the tetramer. This is accompanied by a large shift in the flexible loop of amino acids 399-416, creating connected holes inside the tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6.5
-
-
681359
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
unstable above
25
-
completely stable for 20 h at 25C in 50 mM glycerophosphate, 2 mM EDTA, 1 mM dithiothreitol, pH 7.0
45
-
complete loss of activity
100
-
about 20% of the enzyme activity remains after 60 min of incubation at 100C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glucosidase-transferase stable in 0.05 M Tris and 2 M urea, up to 30C
-
glucosidase-transferase stable in 2 M urea, 2 M urea for prolonged periods of time: no loss in activity
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glucosidase: rather resistant to proteolytic attack: very little inactivation after prolonged incubation with 1% trypsin or 1% chymotrypsin
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stable in 2 M urea, irreversible denaturation with higher concentrations, 3 M, of urea
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
-
stable in ethanol precipitation with final concentration of 23% ethanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 50 mM glycerophosphate, 2 mM EDTA, 1 mM dithiothreitol, pH 7.0, 2 months, without loss of activity
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4C, 50 mM glycerol-1-phosphate, 2 mM EDTA, 1 mM dithiothreitol, pH 7
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4C, 50 mM glycerol-1-phosphate, 2 mM EDTA, 1 mM dithiothreitol, pH 7.0, 1 month, little or no loss of activity
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4C, 50 mM Tris, 5 mM EDTA, 1 mM dithiothreitol, pH 7.2
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5C, crystalline suspension, ammonium sulfate, retains activity for many months or years
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frozen, concentrated solution without salt, retains activity for many months or years
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frozen, solution in Tris-glycerol buffer, 3 months, without loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycogen debranching enzyme
glycogen debranching enzyme; muscle and liver
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glycogen debranching enzyme; omega-aminoalkyl agarose chromatography
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Ni-NTA affinity chromatography
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Ni-NTA column chromatography
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Ni-NTA column chromatography and gel filtration
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Ni-NTA column chromatography and Superdex 200 gel filtration
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partial
partially purified with ammonium sulfate precipitation, DEAE-Sephacryl gel filtration, Sephacryl S-300 gel filtration, and Super Q anion exchange column high performance liquid chromatography
recombinant enzyme, expression in Escherichia coli, purification method via beta-cyclodextrin-immobilized sepharose 6B
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Eschericha coli MC1061
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expressed in Escherichia coli as a His-tagged protein
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expressed in Escherichia coli BL21(DE3-RIL) cells
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expressed in Escherichia coli MC1061 cells
expressed in Escherichia coli strain MC 1061
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glycogen debranching enzyme, cDNA
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G1448R
mutation detected in patient with Glycogen Storage Disease Type III. Significant loss in both enzymatic activites and carbohydrate binding ability, as well as enhancing targeting for proteasomal degradation
L620P
mutation detected in patient with Glycogen Storage Disease Type III. Mutation abolishes transferase activity
R1147G
mutation detected in patient with Glycogen Storage Disease Type III. Mutation impairs glucosidase function
Y1445ins
mutation detected in patient with Glycogen Storage Disease Type III. Significant loss in both enzymatic activites and carbohydrate binding ability, as well as enhancing targeting for proteasomal degradation
D1086N
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loss of glucosidase activity
D1147N
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loss of glucosidase activity
D535N
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loss of transferase activity
D670N
-
loss of transferase activity
E564Q
-
loss of transferase activity
D318A
sharp increasein alpha-1,4-transferase activity
E94A
minor change in the amylo-1,6-glucosidase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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useful in structural determination of glycogen and amylopectin
medicine
nutrition
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the activity of the glycogen debranching enzyme may control the rate of glycogenolysis and glycolysis, but does not block rapid glycolysis and pH decrease when the temperature is high. This may be important in PSE (pale, soft, exudative) meat, where the pH decreases rapidly at high temperatures, but rapid cooling could limit the activity of glycogen debranching enzyme and thus glycogenolysis
synthesis
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use of enzyme for industrial production of cycloamylose
Show AA Sequence (124 entries)
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