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
3.2.1.33
-
RECOMMENDED NAME
GeneOntology No.
amylo-alpha-1,6-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
show the reaction diagram
alpha-(1->6) linkage can be synthesized in the absence of polysaccharide; mechanism
-
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
show the reaction diagram
mechanism; stereochemistry
-
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
show the reaction diagram
mechanism
-
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
show the reaction diagram
regulation of enzyme activity
-
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
show the reaction diagram
mechanism; thermodynamic data
-
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
show the reaction diagram
enzyme hydrolyses an unsubstituted (1->6)-alpha-glucose residue that forms a branch point on an alpha-(1->4)-linked glucose chain
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
endoglycosidic
-
PATHWAY
KEGG Link
MetaCyc Link
glycogen degradation I
-
glycogen degradation II
-
Starch and sucrose metabolism
-
SYSTEMATIC NAME
IUBMB Comments
glycogen phosphorylase-limit dextrin 6-alpha-glucohydrolase
This enzyme hydrolyses an unsubstituted (1->4)-linked 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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
-
-
-
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-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
-
part of the glycogen debranching enzyme
amylo-alpha-1,6-glucosidase
-
-
amylo-alpha-1,6-glucosidase
-
part of the glycogen debranching enzyme
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-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
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)
GlgX
P15067
-
glucosidase, amylo-1,6-
-
-
-
-
glucosidase/transferase
-
-
-
-
glycogen debranching enzyme
-
-
-
-
glycogen debranching enzyme
-
-
glycogen debranching enzyme
-
-
glycogen debranching enzyme
Nostoc punctiforme PCC73102
-
-
-
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
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
-
-
glycogen phosphorylase limit dextrin alpha-1,6-glucohydrolase
-
-
glycogen phosphorylase limit dextrin debranching system
-
-
-
-
indirect debranching enzyme
-
-
-
-
NPDE
Nostoc punctiforme PCC73102
-
-
-
oligo-alpha-1,4-glucan:alpha-1,4-glucan-4-glycosyltransferase-amylo-1,6-glucosidase
-
-
-
-
SSO2094
Q7LX99
locus name
SSO2094
Q7LX99
locus name; locus name
-
transferase-glucosidase
-
-
-
-
TreX
Q7LX99
;
-
CAS REGISTRY NUMBER
COMMENTARY
9012-47-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
member of glycosyl hydrolase 13 family
UniProt
Manually annotated by BRENDA team
healthy and patient with type III glycogen storage disease
-
-
Manually annotated by BRENDA team
patients with Glycogen Storage Disease Type III. Bifunctional amylo-1,6-glucosidase and 4-alpha-glucanotransferase, protein possesses two separate domains for the transferase and glucosidase activities
Uniprot
Manually annotated by BRENDA team
patients with type I and type III glycogen storage disease and control patient
-
-
Manually annotated by BRENDA team
generally present in mammalian tissues
-
-
Manually annotated by BRENDA team
strain PCC73102
-
-
Manually annotated by BRENDA team
Nostoc punctiforme PCC73102
strain PCC73102
-
-
Manually annotated by BRENDA team
2 enzymes: acidic and neutral
-
-
Manually annotated by BRENDA team
bifunctional amylo-1,6-glucosidase and oligo-1,4-1,4 glucanotransferase
-
-
Manually annotated by BRENDA team
D-346, ATCC 56960
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
pacific dogfish
-
-
Manually annotated by BRENDA team
strain ATCC 51178
-
-
Manually annotated by BRENDA team
bifunctional amylo-1,6-glucosidase and 4-alpha-glucanotransferase
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the enzyme may be involved in glycogen metabolism in debranching and rearranging the side chain of the glycogen by both alpha-1,6-hydrolase and alpha-1,6-transferase activity
physiological function
-
the enzyme may be involved in glycogen metabolism in debranching and rearranging the side chain of the glycogen by both alpha-1,6-hydrolase and alpha-1,6-transferase activity
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
show the reaction diagram
-
-
isomaltose
r
2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
show the reaction diagram
-
-
isomaltose
r
2 D-glucose
6-O-alpha-D-glucosyl-D-glucose + H2O
show the reaction diagram
-
-
isomaltose
r
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 cyclodextrin + H2O
D-glucose + cyclodextrin
show the reaction diagram
-
branched
-
?
6-O-alpha-D-glucosyl cyclomalto-octaose + H2O
D-glucose + cyclomalto-octaose
show the reaction diagram
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
D-glucose + cyclomaltoheptaose
show the reaction diagram
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
6-O-alpha-D-glucosyl cyclomaltohexaose + H2O
D-glucose + cyclomaltohexaose
show the reaction diagram
-
poor substrate
-
-
?
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
?
show the reaction diagram
Q7LX99
-
-
-
?
6-O-alpha-maltosyl-beta-cyclodextrin + H2O
maltose + beta-cyclodextrin
show the reaction diagram
-
-
-
-
?
6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O
?
show the reaction diagram
-
very poor substrate
-
-
?
6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
6-O-alpha-maltotetraosyl-beta-cyclodextrin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
very poor substrate
-
-
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
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
-
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
-
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
branched pentasaccharide "fast B5"
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
branched pentasaccharide "fast B5"
-
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
branched pentasaccharide "fast B5"
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
branched pentasaccharide "fast B5"
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
branched pentasaccharide "fast B5"
-
r
63-alpha-glucosyl maltotetraose + H2O
maltotetraose + D-glucose
show the reaction diagram
-
branched pentasaccharide "fast B5"
-
-
r
63-alpha-maltotriosyl maltotetraose + H2O
?
show the reaction diagram
-
branched heptasaccharide B7
-
-
?
63-alpha-maltotriosyl maltotetraose + H2O
?
show the reaction diagram
-
branched heptasaccharide B7
-
-
?
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-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
-
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
-
-
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + 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
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + 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
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + 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
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + 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
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + 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
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-(1-6)-glucosyl cyclohexaamylose + H2O
cyclohexaamylose + D-glucose
show the reaction diagram
-
6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin
alpha-Schardinger dextrin
r
alpha-D-glucosyl fluoride
fluoride + D-glucose
show the reaction diagram
-
-
-
?
alpha-D-glucosyl fluoride
fluoride + D-glucose
show the reaction diagram
-
in absence or presence of glycogen or polysaccharide
-
?
alpha-dextrin + H2O
alpha-dextrin + 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
amylopectin + D-glucose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
very poor substrate
-
-
r
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
very poor substrate
partially debranched
-
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
very poor substrate
partially debranched
r
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
slowly hydrolyzed
-
-
-
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
slowly hydrolyzed
-
-
r
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
slowly hydrolyzed
-
-
-
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
slowly hydrolyzed
-
-
r
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
slowly hydrolyzed, phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
-
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
r
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
-
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
phi-dextrin, beta-dextrin and phi-beta-dextrin from amylopectin
partially debranched
r
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
-
100% activity
-
-
?
amylopectin + H2O
amylopectin + D-glucose
show the reaction diagram
Nostoc punctiforme PCC73102
-
-
-
-
?
amylopectin + H2O
maltose + ?
show the reaction diagram
Q7LX99
-
-
-
?
amylose
cycloamylose
show the reaction diagram
-
-
degree of polymerization between 11 and 50
-
?
amylose + H2O
?
show the reaction diagram
-
-
-
-
r
amylose + H2O
?
show the reaction diagram
-
-
-
-
r
amylose + H2O
?
show the reaction diagram
-
16.9% activity compared to amylopectin
-
-
?
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
beta-dextrin
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
beta-dextrin
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
beta-dextrin
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
beta-dextrin
-
r
beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
beta-dextrin
reverse reaction: glucose incorporation into beta-limit dextrin
r
beta-cyclodextrin-alpha-1,6-linked maltopentaose + H2O
beta-cyclodextrin + maltopentaose
show the reaction diagram
P15067
-
-
-
?
beta-cyclodextrin-alpha-1,6-linked maltotetraose + H2O
beta-cyclodextrin + maltotetraose
show the reaction diagram
P15067
-
-
-
?
beta-cyclodextrin-alpha-1,6-linked maltotriose + H2O
beta-cyclodextrin + maltotriose
show the reaction diagram
P15067
-
-
-
?
branched cyclodextrin + H2O
?
show the reaction diagram
Q7LX99
the TreX protein has a specificity for hydrolysis of chains consisting of 6 glucose residues or longer
-
-
?
D-glucose + maltooligosaccharide
maltooligosaccharide
show the reaction diagram
-
-
branched
r
D-glucose + maltooligosaccharide
maltooligosaccharide
show the reaction diagram
-
-
branched
r
D-glucose + maltooligosaccharide
maltooligosaccharide
show the reaction diagram
-
maltotetraose and maltopentaose
branched
r
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
Q7LX99
preferred substrate
-
-
?
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 + H2O
?
show the reaction diagram
-
in addition to 1,6-glucosidase activity, also has some 1,4-glucosidase and transferase activities
-
-
?
glycogen + H2O
?
show the reaction diagram
Q7LX99
preferred substrate
-
-
?
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
-
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
slowly hydrolyzed
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
slowly hydrolyzed
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
rabbit liver glycogen: very poor substrate, shellfish glycogen: not a substrate
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
native glycogen from shellfish and rabbit liver
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
liver glycogen and shellfish glycogen: one-tenth of activity compared with glycogen phosphorylase limit dextrin as substrate
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
reverse reaction: incorporation of glucose into glycogen
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
reverse reaction: incorporation of glucose into glycogen
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
reverse reaction: incorporation of glucose into glycogen
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
reverse reaction: incorporation of glucose into glycogen
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
reverse reaction: incorporation of glucose into glycogen
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
slight reversibility
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
rabbit liver glycogen: slowly
-
-
r
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
-
73.5% activity compared to amylopectin
-
-
?
glycogen limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
-
partially debranched glycogen
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
best substrate
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
best substrate
partially debranched glycogen
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
symmetric dextrin
asymmetric dextrin
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
-
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
debranched phi-dextrin
r
glycogen phosphorylase-limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
phi-dextrin
partially debranched glycogen
r
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
symmetric dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
phi-dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
phi-dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
phi-dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
total degradation of glycogen is accomplished by the combined action of glycogen phosphorylase and glycogen debranching enzyme
-
-
-
maltodecaose + H2O
?
show the reaction diagram
Nostoc punctiforme, Nostoc punctiforme PCC73102
-
-
-
-
?
maltodecaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
Nostoc punctiforme, Nostoc punctiforme PCC73102
-
-
-
-
?
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
Nostoc punctiforme, Nostoc punctiforme PCC73102
-
-
-
-
?
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
-
-
-
-
?
phosphorylase beta-amylase limit dextrin + H2O
limit dextrin + D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
limit dextrin, beta-phi-dextrin, derived from the action of beta-amylase on the phosphorylase limit dextrin
-
r
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
-
36.8% activity compared to amylopectin
-
-
?
rice starch + H2O
?
show the reaction diagram
-
82.4% activity compared to amylopectin
-
-
?
maltoundecaosyl-alpha-(1,6)-beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrate specificities
-
-
-
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
?
-
-
panose: not a substrate
-
-
-
additional information
?
-
-
pullulan: not a substrate
-
-
-
additional information
?
-
-
glycogen debranching enzyme might play an important role in the structure of glycogen particles, or the control of its metabolism
-
-
-
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
?
-
-
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
?
-
-
no alpha-glucosidase or alpha-amylase activity
-
-
-
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
-
-
-
additional information
?
-
-
no activity towards G2-beta-cyclodextrin and G5-beta-cyclodextrin
-
-
-
additional information
?
-
Nostoc punctiforme, Nostoc punctiforme PCC73102
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Nostoc punctiforme, Nostoc punctiforme PCC73102
-
-
-
-
?
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
-
-
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
symmetric dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
phi-dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
phi-dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
phi-dextrin
-
-
-
glycogen phosphorylase-limit dextrin + H2O
?
show the reaction diagram
-
total degradation of glycogen is accomplished by the combined action of glycogen phosphorylase and glycogen debranching enzyme
-
-
-
additional information
?
-
-
glycogen debranching enzyme might play an important role in the structure of glycogen particles, or the control of its metabolism
-
-
-
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
?
-
-
in vivo degradation of glycogen requires the presence of both glycogen hydrolase and the enzyme
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
1 mM, 154% of initial activity
Ba2+
-
41.7% increase of activity at 5 mM
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,4-diaminobutane
-
putrescine, glycogen debranching enzyme, slight inhibition
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
-
-
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)
-
50% inhibition, reversed by glycogen
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTNB
5-amino-D-glucose
-
nojirimycin, potent inhibitor, noncompetitive
5-thio-D-glucose
-
slight inhibition
7-O-beta-D-glucopyranosyl-homonojirimycin
-
-
alpha-homonojirimycin
-
-
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
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
-
competitive
D-glucose
-
10 mM, 89% of initial activity
D-glucose
-
10% inhibition by 10 mM, 50% inhibition by 50 mM
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)
ethylamine
-
slight inhibition
Fe2+
-
1 mM, 7% of initial activity
-
glucooligosaccharides
-
containing one, two, or three glucose, competitive inhibitors
-
glycogen
-
competitive
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
Hg2+
-
1 mM, 3% of initial activity
imidazole
-
buffer, 50% inhibition
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)
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
-
0.3 mM: completely
p-hydroxymercuribenzoate
-
-
phosphate
-
buffer, inhibits at neutral pH
SDS
-
irreversible inhibition by less than 0.1% SDS
Taurine
-
slight inhibition
triethylamine
-
very poor inhibitor
Tris
-
buffer, strong inhibition
Tris
-
0.02 M Tris: 50-60% inhibition
Tris
-
15 mM: 75% inhibition
Tris
-
noncompetitive; Tris analogues
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
Zn2+
-
1 mM, 4% of initial activity
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
additional information
-
unaffected by hormone administration
-
additional information
-
-
-
additional information
-
inhibition mechanism
-
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
-
additional information
-
inhibition mechanism; no inhibition by dithioerythritol, dithiothreitol, cadaverine, spermidine, spermine, D,L-threitol, 1-thio-beta-D-glucose
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
unaffected by hormone administration
-
additional information
-
mechanism of activation
-
additional information
-
no activating by usual sugar phosphates or nucleotide effectors of glycolysis such as AMP, ADP, ATP, uridine diphosphoglucose, glucose-1-phosphate, glucose-6-phosphate and phosphate
-
additional information
-
no activating substance
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
15.9
-
6-O-alpha-D-glucosyl cyclomaltoheptaose
-
mutant E564Q, pH 6.5, 37C
16.3
-
6-O-alpha-D-glucosyl cyclomaltoheptaose
-
wild type, pH 6.5, 37C
16.6
-
6-O-alpha-D-glucosyl cyclomaltoheptaose
-
mutant D535N, pH 6.5, 37C
19.3
-
6-O-alpha-D-glucosyl cyclomaltoheptaose
-
mutant D670N, pH 6.5, 37C
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
-
63-alpha-glucosyl maltotetraose
-
branched pentasaccharide B5, pH 6.6
-
4.45
-
63-alpha-glucosyl maltotetraose
-
branched pentasaccharide 'fast B5', muscle enzyme
-
5.6
-
63-alpha-maltotriosyl maltotetraose
-
branched heptasaccharide B7, muscle enzyme
-
2.8
-
alpha-glucosyl fluoride
-
-
-
4.3
-
amylopectin beta-dextrin
-
-
-
11
-
amylopectin beta-dextrin
-
-
-
3.8
-
beta-amylase limit dextrin
-
beta-dextrin from shellfish glycogen
-
7.2
-
beta-amylase limit dextrin
-
beta-dextrin from shellfish glycogen
-
0.15
-
beta-cyclodextrin-alpha-1,6-linked maltotetraose
P15067
pH 7, 37C
-
1.5
-
beta-cyclodextrin-alpha-1,6-linked maltotriose
P15067
pH 7, 37C
-
32
-
D-glucose
-
in the presence of glycogen
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
-
glycogen phosphorylase limit dextrin
-
-
-
0.063
-
glycogen phosphorylase limit dextrin
-
phi-dextrin
-
0.74
-
glycogen phosphorylase limit dextrin
-
phi-dextrin from shellfish glycogen
-
0.74
-
glycogen phosphorylase limit dextrin
-
-
-
1.6
-
glycogen phosphorylase limit dextrin
-
phi-dextrin from shellfish glycogen
-
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
8.1
-
alpha-glucosyl fluoride
-
with 9.6% glycogen
-
additional information
-
Amylopectin
-
Km-values: 31.1 mg/ml at pH 5.5, 75C, in absence of DMSO. 88.0 mg/ml at pH 5.5, 75C, in presence of DMSO. 92.3 mg/ml at pH 6.5, 75C, in absence of DMSO. 345 mg/ml at pH 5.5, 75C, in presence of DMSO
0.51
-
maltoundecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
additional information
-
additional information
-
kinetic mechanism
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data
-
additional information
-
additional information
-
kinetic data; kinetic mechanism
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2570
-
6-O-alpha-maltotetraosyl-beta-cyclodextrin
-
pH 5.5, 75C
-
0.48
-
Amylopectin
-
pH 6.5, 75C, calculated as microMol maltose released from the substrate, in absence of DMSO
0.923
-
Amylopectin
-
pH 5.5, 75C, calculated as microMol maltose released from the substrate, in absence of DMSO
7.57
-
Amylopectin
-
pH 5.5, 75C, calculated as microMol maltose released from the substrate, in presence of DMSO
17.35
-
Amylopectin
-
pH 5.5, 75C, calculated as microMol maltose released from the substrate, in presence of DMSO
41.7
-
beta-cyclodextrin-alpha-1,6-linked maltotetraose
P15067
pH 7, 37C
-
38
-
beta-cyclodextrin-alpha-1,6-linked maltotriose
P15067
pH 7, 37C
-
38
-
G3-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
41.7
-
G4-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
0.045
-
maltodecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.0478
-
maltododecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.0205
-
maltononaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
0.0452
-
maltoundecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
300
-
beta-cyclodextrin-alpha-1,6-linked maltotetraose
P15067
pH 7, 37C
0
26
-
beta-cyclodextrin-alpha-1,6-linked maltotriose
P15067
pH 7, 37C
0
26
-
G3-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
293262
300
-
G4-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH7.0) at 37C
293261
0.07
-
maltodecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
139983
0.177
-
maltodecaosyl-alpha-(1,6)-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293839
0.077
-
maltododecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293263
0.0145
-
maltoheptaosyl-alpha-(1,6)-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293841
0.003
-
maltohexaosyl-alpha-(1,6)-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293842
0.025
-
maltononaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
12851
0.117
-
maltononaosyl-alpha-(1,6)-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293838
0.0027
-
maltooctaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
12852
0.103
-
maltooctaosyl-alpha-(1,6)-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293837
0.0027
-
maltopentaosyl-alpha-(1,6)-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293843
0.09
-
maltoundecaose
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
12861
0.173
-
maltoundecaosyl-alpha-(1,6)-beta-cyclodextrin
-
in 50 mM sodium phosphate buffer (pH 7.5) at 30C
293840
additional information
-
additional information
-
catalytic efficiency (the kcat/Km ratio) increases as the degree of polymerization of branch chains rises
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0015
-
guanidine
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00019
-
1-deoxynojirimycin
-
-
0.0061
-
7-O-beta-D-glucopyranosyl-homonojirimycin
-
-
0.00011
-
alpha-homonojirimycin
-
-
0.48
-
D-isofagomine
-
-
0.0021
-
fagomine
-
-
0.00039
-
miglitol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.82
-
-
substrate: 63-alpha-glucosyl maltotetraose
3
-
-
maleate buffer, pH 6.0, 19C
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
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
-
imidazole buffer, about 50% inhibition
5.5
-
-
assay at
6
-
-
substrate: glycogen phosphorylase limit dextrin, citrate /phosphate buffer
6
-
-
phosphate-citrate buffer
6
-
-
substrate: glycogen phosphorylase limit dextrin, citrate /phosphate buffer
6
-
-
-
6
-
-
-
6.1
6.4
-
sodium citrate/mercaptoethanol buffer
6.6
-
-
anionic buffer, substrate: glycogen phosphorylase limit dextrin
6.6
-
-
anionic buffer, substrate: glycogen phosphorylase limit dextrin; imidazole buffer
7.2
-
-
cationic buffer, substrate: glycogen phosphorylase limit dextrin
7.6
-
-
citrate buffer
additional information
-
-
pH-optimum depends on substrate and type of buffer, overview; pH-optimum depends on type of buffer
additional information
-
-
pH-optimum depends on type of buffer
additional information
-
-
reverse action of amylo-1,6-glucosidase: pH optimum depends on different acceptor substrates
additional information
-
-
pH optimum is the same in both degradative and synthetic directions and optimum is shifted and inhibited by Tris in the same manner in both directions
additional information
-
-
pH-optimum depends on type of buffer; pH optimum is the same in both degradative and synthetic directions and optimum is shifted and inhibited by Tris in the same manner in both directions
additional information
-
-
2 enzymes: one with an acid and one with a neutral pH-optimum
additional information
-
-
2 enzymes: one with an acid and one with a neutral pH-optimum; pH-optimum depends on type of buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
5
8
-
pH 5.0: about 25% of maximum activity, pH 8.0: about 40% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
cerebrum
Manually annotated by BRENDA team
-
from skin biopsies
Manually annotated by BRENDA team
-
primary culture
Manually annotated by BRENDA team
-
pectoralis
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
masseter and longissimus dorsi
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
protein-glycogen particle from skeletal muscle, glycogen debranching enzyme component of
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
141000
-
-
dimeric enzyme form, analytical ultracentrfugation
160000
170000
-
glycogen debranching enzyme, analytical gel chromatography under denaturing, with 6 M guanidine HCl and 1% 2-mercaptoethanol and non-denaturing conditions
160000
170000
-
-
160000
-
-
glycogen debranching enzyme, linear density gradient column
160000
-
-
glycogen debranching enzyme, calculation on Stokes' radius using Svedberg equation
160000
-
-
glycogen debranching enzyme, PAGE and SDS-PAGE
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
-
-
glycogen debranching enzyme, SDS-PAGE
170000
-
-
glycogen debranching enzyme, muscle enzyme, sucrose density gradient centrifugation
170000
-
-
gel filtration
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
-
glycogen debranching enzyme, equilibrium ultracentrifugation
267000
279000
-
glycogen debranching enzyme can probably form a complex with one or more other soluble proteins
267000
279000
-
glycogen debranching enzyme, equilibrium ultracentrifugation
267000
279000
-
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
-
-
; glycogen debranching enzyme, sedimentation equilibrium
280000
-
-
glycogen debranching enzyme, SDS-PAGE
280000
-
-
glycogen debranching enzyme, sedimentation equilibrium
280000
-
-
; glycogen debranching enzyme, sedimentation equilibrium
355000
-
-
tetrameric enzyme form, analytical ultracentrfugation
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 160000, SDS-PAGE
dimer
-
2 * 83000, the enzyme is mainly dimeric at pH 7.0, SDS-PAGE; 2 * 93091, the enzyme is mainly dimeric at pH 7.0, calculated from sequence
dimer
-
2 * 83000, the enzyme is mainly dimeric at pH 7.0, SDS-PAGE; 2 * 93091, the enzyme is mainly dimeric at pH 7.0, calculated from sequence
-
monomer
-
1 * 166000, glycogen debranching enzyme, SDS-PAGE
monomer
-
glycogen debranching enzyme, SDS-PAGE
monomer
-
1 * 170000, glycogen debranching enzyme, SDS-PAGE, alkylated enzyme
monomer
-
1 * 170000, glycogen debranching enzyme, SDS-PAGE
monomer
-
1 * 160000, glycogen debranching enzyme, carboxymethylation prior to SDS-PAGE
monomer
-
1 * 155000, glycogen debranching enzyme, sedimentation equilibrium with 6 M guanidinium chloride; 1 * 166000, glycogen debranching enzyme, SDS-PAGE
tetramer
-
4 * 83000, the enzyme is mainly dimeric at pH 5.5-6.5, SDS-PAGE; 4 * 93091, the enzyme is mainly dimeric at pH 5.5-6.5, calculated from sequence
tetramer
-
4 * 83000, the enzyme is mainly dimeric at pH 5.5-6.5, SDS-PAGE; 4 * 93091, the enzyme is mainly dimeric at pH 5.5-6.5, calculated from sequence
-
trimer
-
; glycogen debranching enzyme, three basic subunits, 1 * 122000, 1 * 85000, 1 * 70000, carboxymethylation prior to SDS-PAGE and gel electrophoresis in the presence of urea
trimer
-
glycogen debranching enzyme, three basic subunits, 1 * 122000, 1 * 85000, 1 * 70000, carboxymethylation prior to SDS-PAGE and gel electrophoresis in the presence of urea
additional information
-
evidence for a subunit of 120000
additional information
-
transferase and glucosidase activities are independent and located at different sites of the polypeptide chain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
no covalently bound phosphate or carbohydrate, method would not have detected less than 5% carbohydrate
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
P15067
3.0 A resolution; glycogen debranching enzyme
-
glycogen debranching enzyme
-
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
P95868
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
30
-
-
up to, in the presence of Tris and urea
30
-
-
rapid inactivation
45
-
-
complete loss of activity
100
-
-
about 20% of the enzyme activity remains after 60 min of incubation at 100C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
glucosidase: rather resistant to proteolytic attack: very little inactivation after prolonged incubation with 1% trypsin or 1% chymotrypsin
-
stable in 2 M urea, irreversible denaturation with higher concentrations, 3 M, of urea
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
stable in ethanol precipitation with final concentration of 23% ethanol
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 50 mM glycerol-1-phosphate, 2 mM EDTA, 1 mM dithiothreitol, pH 7
-
0C, 50 mM glycerophosphate, 2 mM EDTA, 1 mM dithiothreitol, pH 7.0, 2 months, without loss of activity
-
4C, 50 mM glycerol-1-phosphate, 2 mM EDTA, 1 mM dithiothreitol, pH 7.0, 1 month, little or no loss of activity
-
4C, 50 mM Tris, 5 mM EDTA, 1 mM dithiothreitol, pH 7.2
-
5C, crystalline suspension, ammonium sulfate, retains activity for many months or years
-
frozen, concentrated solution without salt, retains activity for many months or years
-
frozen, solution in Tris-glycerol buffer, 3 months, without loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
Ni-NTA column chromatography and Superdex 200 gel filtration
-
glycogen debranching enzyme
-
glycogen debranching enzyme
-
Ni-NTA column chromatography
-
glycogen debranching enzyme; muscle and liver
-
glycogen debranching enzyme; omega-aminoalkyl agarose chromatography
-
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
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recombinant enzyme, expression in Escherichia coli, purification method via beta-cyclodextrin-immobilized sepharose 6B
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glycogen debranching enzyme
-
Ni-NTA affinity chromatography
-
glycogen debranching enzyme
-
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli MC1061 cells
-
glycogen debranching enzyme, cDNA
-
expressed in Escherichia coli MC1061 cells
-
glycogen debranching enzyme, cDNA
-
expressed in Escherichia coli strain MC 1061
-
expressed in Eschericha coli MC1061
-
expressed in Escherichia coli as a His-tagged protein
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
G1448R
P35573
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
P35573
mutation detected in patient with Glycogen Storage Disease Type III. Mutation abolishes transferase activity
R1147G
P35573
mutation detected in patient with Glycogen Storage Disease Type III. Mutation impairs glucosidase function
Y1445ins
P35573
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
-
loss of glucosidase activity
D1147N
-
loss of glucosidase activity
D535N
-
loss of transferase activity
D670N
-
loss of transferase activity
E564Q
-
loss of transferase activity
D318A
P95868
sharp increasein alpha-1,4-transferase activity
E94A
P95868
minor change in the amylo-1,6-glucosidase activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
diagnosis, even prenatal, of type III glycogen storage disease: marked decrease or absence of amylo-1,6-glucosidase, glycogen debranching enzyme
medicine
P35573
study on patients with Glycogen Storage Disease Type III. Inactivation of either enzymatic activity is sufficient to cause Glycogen Storage Disease Type III disease. The carbohydrate binding domain of amylo-1,6-glucosidase,4-alpha-glucanotransferase plays a major role to coordinate its functions and regulation by the ubiquitin-proteasome system
analysis
-
useful in structural determination of glycogen and amylopectin
synthesis
-
use of enzyme for industrial production of cycloamylose
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