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EC Tree
IUBMB Comments The enzyme catalyses the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Thus, for an alpha-glucan containing n (1->4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose are all completely degraded. It does not degrade (1->6)-alpha-glucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin. Other enzymes involved in the anhydrofructose pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 5.3.2.7 (ascopyrone tautomerase).
The enzyme appears in viruses and cellular organisms
Synonyms
glase, alpha-1,4-glucan lyase, ag111,
more
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(1,4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)
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alpha-(1,4)-Glucan 1,5-anhydro-D-fructose eliminase
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alpha-1,4-Glucan exo-lyase
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alpha-1,4-glucan lyase isozyme 1
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Dehydratase, alpha-1,4-glucan
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exo-(1,4)-alpha-D-glucan lyase
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-
-
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Exo-alpha-1,4-glucan lyase
alpha-1,4-Glucan lyase
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-
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alpha-1,4-Glucan lyase
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Exo-alpha-1,4-glucan lyase
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-
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Exo-alpha-1,4-glucan lyase
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GLase
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[(1->4)-alpha-D-glucosyl]n+1 = 1,5-anhydro-D-fructose + [(1->4)-alpha-D-glucosyl]n
[(1->4)-alpha-D-glucosyl]n+1 = 1,5-anhydro-D-fructose + [(1->4)-alpha-D-glucosyl]n
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-
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[(1->4)-alpha-D-glucosyl]n+1 = 1,5-anhydro-D-fructose + [(1->4)-alpha-D-glucosyl]n
reaction mechanism occurred by an acid-catalysed formation of a covalent glycosyl-enzyme intermediate via the nucleophilic aspartic acid residue Asp 553 followed by the E1-like E2 elimination of the enzyme carboxylate to generate 1,5-anhydrofructose
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C-O-bond cleavage
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elimination
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(1->4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)
The enzyme catalyses the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Thus, for an alpha-glucan containing n (1->4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose are all completely degraded. It does not degrade (1->6)-alpha-glucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin. Other enzymes involved in the anhydrofructose pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 5.3.2.7 (ascopyrone tautomerase).
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(1,4-alpha-D-glucosyl)n
1,5-anhydro-D-fructose + (1,4-alpha-D-glucosyl)n-1
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degradation of glycogen and starch in eukaryotes
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-
?
2,4,6-trichlorophenyl alpha-D-glucopyranoside
?
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-
-
?
2,4-dinitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
2,5-dinitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
2-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
3,4-dinitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
3,5-dichlorophenyl alpha-D-glucopyranoside
?
-
-
-
?
3-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-chlorophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-nitrophenyl alpha-D-glucoside
?
-
-
-
-
?
5-fluoro-alpha-D-glucopyranosyl fluoride
?
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-
-
?
alpha-D-glucopyranosyl fluoride
?
amylopectin
?
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barley amylopectin and potato amylopectin
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?
amylopectin
D-glucose + 1,5-anhydro-D-fructose
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-
-
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?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
maltosaccharide
?
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-
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-
?
Maltosaccharides
Glucose + 1,5-anhydro-D-fructose
maltose
D-glucose + 1,5-anhydro-D-fructose
Maltose
Glucose + 1,5-anhydro-D-fructose
p-nitrophenyl alpha-D-glucopyranoside
?
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-
-
?
phenyl alpha-D-glucopyranoside
?
-
-
-
?
starch
1,5-anhydro-D-fructose + ?
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-
-
-
?
additional information
?
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alpha-D-glucopyranosyl fluoride
?
-
-
-
?
alpha-D-glucopyranosyl fluoride
?
-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
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-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
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-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
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-
-
-
?
Glycogen
?
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-
?
Glycogen
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
Glycogen
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
Glycogen
?
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rabbit liver glycogen
-
?
Glycogen
?
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best substrate
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-
?
Glycogen
?
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best substrate
-
-
?
Maltoheptaose
?
-
-
-
?
Maltoheptaose
?
-
-
-
-
?
Maltosaccharides
Glucose + 1,5-anhydro-D-fructose
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-
-
-
?
Maltosaccharides
Glucose + 1,5-anhydro-D-fructose
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-
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?
maltose
D-glucose + 1,5-anhydro-D-fructose
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-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
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-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
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-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
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-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
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the enzyme degrades alpha-maltose and beta-maltose at different rates
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?
Maltose
Glucose + 1,5-anhydro-D-fructose
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-
-
-
?
Maltose
Glucose + 1,5-anhydro-D-fructose
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-
-
-
?
Maltose
Glucose + 1,5-anhydro-D-fructose
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-
-
-
?
Maltotetraose
?
-
-
-
?
Maltotetraose
?
-
-
-
-
?
starch
?
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-
-
?
starch
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
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?
starch
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
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?
additional information
?
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the enzyme is highly specific for alpha-1,4-glucosidic bonds found in starch-type substrates and shows low or no activity towards other types of glucosidic bonds and other types of polysaccharides
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?
additional information
?
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the enzyme catalyzes the breakdown of alpha-1,4-glucans via a mechanism involving the formation of a covalent glycosyl-enzyme intermediate which then undergoes a syn-elimination
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?
additional information
?
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no activity towards glucans with alpha-1,1-linkages, alpha-1,3-linkages or alpha-1,6-linkages
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?
additional information
?
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no activity towards glucans with alpha-1,1-linkages, alpha-1,3-linkages or alpha-1,6-linkages
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-
?
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(1,4-alpha-D-glucosyl)n
1,5-anhydro-D-fructose + (1,4-alpha-D-glucosyl)n-1
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degradation of glycogen and starch in eukaryotes
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-
?
Glycogen
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
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?
Glycogen
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
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?
starch
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
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?
starch
?
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the enzyme catalyzes the first step of the anhydrofructose pathway
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?
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Ca2+
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1.3fold activation
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1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide hydrochloride
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2,4,6-trinitrobenzene-sulfonyl acid
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4-chloromercuribenzoic acid
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5-fluoro-beta-L-idopyranosyl fluoride
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Cu2+
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10 mM, complete inactivation
glucose
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with amylopectin as substrate. No effect with glycogen as substrate
Hg2+
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1 mM, complete inactivation
hydroximinogluconolactam
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poor
maltitol
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with amylopectin or glycogen as substrate
methyl alpha-glucoside
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with glycogen as substrate
PCMB
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with amylopectin or glycogen as substrate
additional information
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no effect with 1 mM Mg2+, Zn2+, Fe2+ or Co2+
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acarbose
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deoxynojirimycin
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deoxynojirimycin
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with amylopectin or glycogen as substrate
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Abscess
The use of radioactive silver for the detection of abscesses and tumors; the concentration of Ag111 in spontaneous and experimentally induced abscesses.
Hyperopia
Noncontact thermokeratoplasty to correct hyperopia induced by laser in situ keratomileusis.
Leukemia
Video-Rate Bioluminescence Imaging of Degranulation of Mast Cells Attached to the Extracellular Matrix.
Neoplasms
The use of radioactive silver for the detection of abscesses and tumors; the concentration of Ag111 in spontaneous and experimentally induced abscesses.
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0.77
2,4,6-trichlorophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
3.8
2,4-dinitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
9.9
2,5-dinitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
11
2-nitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
0.59
3,4-dinitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
3.1
3,5-dichlorophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
2.2
3-nitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
2.7
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
2.1
4-chlorophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
2.1
4-nitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
10.7
5-fluoro-alpha-D-glucopyranosyl fluoride
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pH 6.0, 30°C
27.9 - 28
alpha-D-glucopyranosyl fluoride
0.03
amylopectin
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pH 5.0, 35°C, barley amylopectin or potato amylopectin
0.03
glycogen
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pH 5.0, 35°C, rabbit liver glycogen
0.1
maltoheptaose
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pH 5.0, 35°C
0.1
maltohexaose
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pH 5.0, 35°C
0.1
maltopentaose
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pH 5.0, 35°C
2.3
maltose
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pH 5.0, 35°C
0.1
maltotetraose
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pH 5.0, 35°C
0.4
maltotriose
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pH 5.0, 35°C
2
p-nitrophenyl alpha-D-glucopyranoside
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-
4.4
phenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
27.9
alpha-D-glucopyranosyl fluoride
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pH 6.0, 30°C
28
alpha-D-glucopyranosyl fluoride
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-
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1
2,4,6-trichlorophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
27
2,4-dinitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
11
2,5-dinitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
5.3
2-nitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
1.7
3,4-dinitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
1.5
3,5-dichlorophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
0.66 - 6.08
3-nitrophenyl alpha-D-glucopyranoside
6.3
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
0.44
4-chlorophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
0.4
4-nitrophenyl alpha-D-glucopyranoside
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pH 6.0, 30°C
0.131
5-fluoro-alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30°C
505
alpha-D-glucopyranosyl fluoride
0.38
p-nitrophenyl alpha-D-glucopyranoside
-
-
0.11
phenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
0.66
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
6.08
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
505
alpha-D-glucopyranosyl fluoride
-
-
505
alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30°C
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28.3
5-fluoro-beta-L-idopyranosyl fluoride
-
-
0.00013
deoxynojirimycin
-
pH 6.0, 30°C
1.33
hydroximinogluconolactam
-
pH 6.0, 30°C
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2.5 - 7
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maltose as substrate
3.5 - 7.5
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amylopectin as substrate
6.5
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-
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3 - 6.5
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pH 3: about 50% of maximal activity, pH 6.5: about 60% of maximal activity
4.5 - 8
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pH 4.5: about 40% of maximal activity, pH 8.0: about 55% of maximal activity
5 - 8
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pH 5.0: about 60% of maximal activity, pH 8.0: about 50% of maximal activity
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37
-
amylopectin as substrate
40
-
glycogen as substrate
43
-
amylopectin as substrate
45
-
optimal activity without addition of any salt
48
-
glycogen as substrate
50
-
optimal activity in presence of 1 mM calcium chloride
50
-
maltose or amylopectin as substrate
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25 - 55
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25°C: about 60% of maximal activity, 55°C: about 55% of maximal activity, glycogen as substrate
25 - 60
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25°C: about 40% of maximal activity, 60°C: about 40% of maximal activity, glycogen as substrate
33 - 65
-
about 50% of maximal activity at 33°C and 65°C
35 - 50
-
35°C: about 70% of maximal activity, 50°C: about 70% of maximal activity, activity without addition of any salt
35 - 55
-
35°C: about 50% of maximal activity, 55°C: about 80% of maximal activity, optimal activity in presence of 1 mM calcium chloride
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CBS 293.54
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brenda
CBS 293.54
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brenda
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brenda
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-
brenda
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-
-
brenda
-
-
-
brenda
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-
-
brenda
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-
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brenda
-
UniProt
brenda
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brenda
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Q9STC2_GRALE
1092
0
123169
TrEMBL
Secretory Pathway (Reliability: 3 )
Q9STB9_GRALE
180
0
20427
TrEMBL
other Location (Reliability: 2 )
Q9STC0_GRALE
1091
0
123255
TrEMBL
Mitochondrion (Reliability: 3 )
Q9UVY7_9PEZI
163
0
18055
TrEMBL
other Location (Reliability: 2 )
Q9STB8_GRALE
571
0
65149
TrEMBL
other Location (Reliability: 2 )
Q9UVZ1_9PEZI
1070
0
121924
TrEMBL
other Location (Reliability: 1 )
Q9STC1_GRALE
1088
0
122338
TrEMBL
Mitochondrion (Reliability: 5 )
Q9UVZ2_9PEZI
1066
0
121536
TrEMBL
other Location (Reliability: 1 )
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100000
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x * 100000, SDS-PAGE
111000
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1 * 111000, SDS-PAGE
116700
-
martix-assisted laser desorption mass spectrometry
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monomer
-
1 * 111000, SDS-PAGE
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no glycoprotein
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no detectable amount of carbohydrate
no glycoprotein
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no detectable amount of carbohydrate
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