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D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 9.1% (reference: D-glucose 100%)
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 11% (reference: D-glucose 100%)
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 18% (reference: D-glucose 100%)
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 35% (reference: D-glucose 100%)
-
-
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
14% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
2-deoxy-D-glucose + NAD+
?
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
best substrate, wild-type and mutant enzymes
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
D-fructose + NAD(P)+
? + NAD(P)H
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-fructose + NAD+
?
weak substrate
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
-
low activity with wild-type and mutant enzymes
-
-
?
D-galactose + NAD+
?
weak substrate
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 2.9% (reference: D-glucose 100%)
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
-
?
D-glucosamine + NAD+
?
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
-
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 3% (reference: D-glucose 100%)
-
-
?
D-glucosamine + NADP+
D-glucosamino-1,5-lactone + NADPH
-
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
75% relative activity
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-mannose + NAD(P)+
? + NAD(P)H
-
wild-type and mutant enzymes
-
-
?
D-mannose + NAD+
?
weak substrate
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 4.8% (reference: D-glucose 100%)
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
-
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
wild-type and mutant enzymes
-
-
?
D-xylose + NAD+
?
weak substrate
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 10% (reference: D-glucose 100%)
-
-
?
additional information
?
-
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
114% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
112% relative activity
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
the enzyme is highly specific for beta-D-glucose
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is highly specific for beta-D-glucose
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% relative activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
100% activity
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
-
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
2% relative activity
-
-
?
additional information
?
-
-
no activity of wild-type and mutant enzymes with sucrose
-
-
?
additional information
?
-
-
no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
-
-
?
additional information
?
-
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
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3.1
D-glucose
pH 6.0, 37°C, wild-tpye
4 - 10
D-glucose
pH 6.0, 37°C, mutant G261A
4.3
D-glucose
pH 6.0, 37°C, mutant A258F
9.8
D-glucose
pH 8.0, 37°C, mutant A258F
12
D-glucose
pH 8.0, 37°C, wild-tpye
81
D-glucose
pH 6.0, 37°C, mutant G259A
380
D-glucose
pH 8.0, 37°C, mutant G259A
1100
D-glucose
pH 6.0, 37°C, mutant DELTAG261
1400
D-glucose
pH 6.0, 37°C, mutant G259V
2000
D-glucose
pH 8.0, 37°C, mutant DELTAG261
2000
D-glucose
pH 8.0, 37°C, mutant G261A
4000
D-glucose
pH 6.0, 37°C, mutant G261V
4000
D-glucose
pH 8.0, 37°C, mutant G259V
5000
D-glucose
pH 8.0, 37°C, mutant G261V
2.7
beta-D-glucose
-
E96K mutant, coenzyme NAD+
4
beta-D-glucose
-
E96K mutant, coenzyme NADP+
4.5
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH IV, coenzyme NADP+
4.6
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH I, coenzyme NAD+
7.9
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH I, coenzyme NADP+
8
beta-D-glucose
-
mutant Q252L, pH 8.0, 25°C
8.5
beta-D-glucose
-
mutant Q252L/E170K, pH 8.0, 25°C
8.7
beta-D-glucose
-
E96A mutant, coenzyme NAD+
9
beta-D-glucose
-
Q252L mutant, coenzyme NAD+
9.2
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH II, coenzyme NAD+
9.5
beta-D-glucose
-
wild type, coenzyme NAD+
9.8
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH IV, coenzyme NAD+
10
beta-D-glucose
-
Q252L mutant, coenzyme NADP+
11
beta-D-glucose
-
wild type, coenzyme NADP+
12.4
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH II, coenzyme NADP+
13
beta-D-glucose
-
E96A mutant, coenzyme NADP+
14
beta-D-glucose
-
wild-type enzyme, pH 8.0, 25°C
16
beta-D-glucose
-
E96G mutant, coenzyme NAD+
18
beta-D-glucose
-
E96G mutant, coenzyme NADP+
44
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH III, coenzyme NAD+
47.5
beta-D-glucose
-
pH 9.0, 25°C
55
beta-D-glucose
-
Y253C mutant, coenzyme NAD+
85
beta-D-glucose
-
Y253C mutant, coenzyme NADP+
135
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH III, coenzyme NADP+
7.5
D-glucose
apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
8
D-glucose
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
8.5
D-glucose
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
11
D-glucose
pH 6.0, 37°C, wild-tpye
14
D-glucose
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
14.8
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P
16
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R
16.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R
17.2
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I
17.3
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R
17.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K
17.5
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
63
D-glucose
pH 8.0, 37°C, wild-tpye
0.018
NAD+
-
E96K mutant
0.081
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH I
0.088
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH IV
0.15
NAD+
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.16
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH III
0.17
NAD+
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.22
NAD+
apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.33
NAD+
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.99
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH II
0.0051
NADP+
-
E96K mutant
0.0076
NADP+
-
E96G mutant
0.0093
NADP+
-
E96A mutant
0.018
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH II
0.02
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH I
0.026
NADP+
-
Q252L mutant
0.037
NADP+
-
Y253C mutant
1.9
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH IV
18.9
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH III
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18
beta-D-glucose
-
E96K mutant, coenzyme NADP+
23
beta-D-glucose
-
E96K mutant, coenzyme NAD+
92
beta-D-glucose
-
E96G mutant, coenzyme NADP+
97
beta-D-glucose
-
E96A mutant, coenzyme NAD+
98
beta-D-glucose
-
E96A mutant, coenzyme NADP+
114
beta-D-glucose
-
E96G mutant, coenzyme NAD+
120
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP+, isoenzyme GlcDH I
140
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP+, isoenzyme GlcDH II
186
beta-D-glucose
-
Y253C mutant, coenzyme NADP+
190
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NAD+, isoenzymes GlcDH I and GlcDH II
200
beta-D-glucose
-
Y253C mutant, coenzyme NAD+
260
beta-D-glucose
-
wild type, coenzyme NADP+
300
beta-D-glucose
-
Q252L mutant, coenzyme NADP+
317
beta-D-glucose
-
mutant Q252L, pH 8.0, 25°C
334
beta-D-glucose
-
mutant Q252L/E170K, pH 8.0, 25°C
390
beta-D-glucose
-
wild type, coenzyme NAD+
395
beta-D-glucose
-
wild-type enzyme, pH 8.0, 25°C
420
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NAD+, isoenzyme GlcDH IV
430
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NAD+, isoenzyme GlcDH III
462
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP, isoenzyme GlcDH IV
802
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP+, isoenzyme GlcDH III
81.9
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R
82.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
82.6
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P
84.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K
89.6
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R
112
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I
119
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R
190
D-glucose
isozyme GlcDH-I
190
D-glucose
isozyme GlcDH-II
317
D-glucose
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
334
D-glucose
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
352
D-glucose
apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
390
D-glucose
isozyme GlcDH-IWG3
395
D-glucose
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
23
NAD+
-
E96K mutant
390
NAD+
-
wild type, coenzyme NAD+
18
NADP+
-
E96K mutant
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A258F
Km (D-glucose) increased at pH 6 compared to wild-type, decreased at pH 8 compared to wild-type. Mutant shows higher substrate specificity with D-xylose, D-mannose, D-galactose and D-glucosamine compared to wild-type. Mutant shows a markedly deteriorated thermostability
DELTAG261
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type.Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Mutant shows a markedly deteriorated thermostability
G259A
Km (D-glucose) increased at pH 6 and pH 8 compared to wild-type. Specific activity of the G259A mutant is slightly lower, but is still comparable with wild-type BmGlcDH-IV. Thermostability comparable to wild-type
G259V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261A
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
E170K
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH
E96K
-
mutation increases thermostability by about 15°C at pH 6.5
E96K/D108N/P194Q/E210K
mutant enzyme has higher stability at 60°C and 97% remaining activity compared to the wild type enzyme
E96K/V112A/E133K/Y217H
mutant enzyme has higher stability at 60°C and 85% remaining activity compared to the wild type enzyme
E96K/V183I
mutant enzyme has higher stability at 60°C and 72% remaining activity compared to the wild type enzyme
Q252L/A258G
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
Q252L/E170K/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/K137R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I/K137R
the mutant enzyme exhibits a 9.2fold increase in tolerance against 10% (v/v) 1-phenylethanol and is more stable than mutant enzyme Q252L/E170K (BmGDHM0) when exposed to hydrophobic and enzyme-inactivating compounds such as acetophenone, ethyl 2-oxo-4-phenylbutyrate, and ethyl (R)-2-hydroxy-4-phenylbutyrate
E96A
-
mutation increases thermostability at pH 6.5
E96A
mutant enzyme has higher stability at 60°C and 90% remaining activity compared to the wild type enzyme
E96G
-
mutation increases thermostability at pH 6.5
E96G
mutant enzyme has higher stability at 60°C and 47% remaining activity compared to the wild type enzyme
Q252L
-
mutation increases thermostability at pH 6.5
Q252L
-
natural mutant strain IWG3, Leu252 increases enzyme stability, slightly increased activity compared to the wild-type enzyme
Q252L
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
Q252L
mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH
Q252L/E170K
-
site-directed mutagenesis of the mutant strain IWG3, the mutant is insensitive against NaCl concentration and pH value, slightly increased activity compared to the wild-type enzyme
Q252L/E170K
mutant exhibits increased pH stability (95% residual activity at pH 8-10.5) in the absence of NaCl
Q252L/E170K
kinetic parameters of the mutant enzyme are determined
Y253C
-
mutation increases thermostability at pH 6.5
Y253C
mutant enzyme has higher stability at 60°C and 1% remaining activity compared to the wild type enzyme
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4
-
30 min, about 50% loss of activity
639125
4 - 10
-
30°C, 20 min, mutant enzymes E96K and E95A, less than 20% loss of activity
639105
4 - 8
-
30°C, 20 min, mutant enzyme Q252L is stable
639105
5
-
30°C, 20 min, about 55% loss of activity of mutant enzyme Y253C, about 35% loss of activity of mutant enzyme E96G and wild-type enzyme
639105
5 - 10
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-III is stable
639101
5 - 6.5
-
30 min, stable
639125
5.5 - 10
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-V is stable
639101
6 - 7
-
30°C, 20 min, wild-type and mutant enzyme Y253C are stable
639105
6 - 9
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-IWG3 is stable
639101
6.5 - 7
-
20 min, without NaCl, isoenzyme GlcDH-IWG3 and GlcDH-III are stable
639101
6.5 - 9
-
the enzyme is stable and active at pH 6.5, by shifting the pH to 9.0 the enzyme is completely and irreversibly dissociated into four inactive protomers
639108
7 - 9
wild type GlcDH shows reversible dissociation-association between inactive monomers and active tetramers when the pH is shifted between 9 and 7
677657
7.3
-
30 min, about 50% loss of activity
639125
7.5
-
30 min, about 95% loss of activity
639125
8
-
30°C, 20 min, about 50% loss of activity of mutant enzyme Y253C, about 80% loss of wild-type enzyme, about 30% loss of activity of mutant enzyme E96G and E96, about 15% loss of activity of mutant enzyme E96K
639105
9
-
-
639125
9
-
the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9 the enzyme is completely and reversibly dissociated into four inactive protomers
639108, 639112
9
after dissociation of the tetrameric enzyme into its inactive monomers at pH 9 two tyrosine residues (Tyr-254 and Tyr-160) become susceptible to nitration which are unable to reassociate to the tetramer
679608
additional information
-
-
639125
additional information
-
isoenzyme GlcDHIII has no stable pH-region without NaCl
639101
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65
wild-type enzyme retains 70% activity after 40 min at 65°C
30
-
20 min, isoenzyme GlcDH-III, without NaCl, about 55% loss of activity
40
-
pH 6.5, 20 min, wild-type enzyme is stable
45
-
20 min, isoenzyme GlcDH-IV, without NaCl, about 35% loss of activity, isoenzyme IWG3, without NaCl, about 10% loss of activity
55
-
pH 6.5, 20 min, about 65% loss of acticity of mutant enzyme Y253C, about 20% loss of activity of mutant enzyme Y252L, mutant enzyme E96K, E96G and E96A are stable
60
-
pH 6.5, 20 min, complete loss of activity of enzyme Y253C about 95% loss of activity of mutant enzyme Y252L, about 30% loss of activity of mutant enzyme E96G, mutant enzymes E96K and E95A are stable
66
-
half-life: mutant Q252L 1.3 min, mutant Q252L/E170K 540 min
70
-
20 min, presence of 2 mM NaCl, complete inactivation of isoenzyme GlcDH-III and GlcDH-IV, isoenzyme GlcDH-IWG3 loses 30% of initial activity
additional information
-
thermostability is highly increased by addition of NaCl
50
-
20 min, isoenzyme GlcDH-IWG3, without NaCl, complete loss of activity, isoenzymes GlcDH-II and GlcDH-IWG3 are stable in presence of 2 M NaCl
50
-
pH 6.5, 20 min, complete inactivation of wild-type enzyme, mutant enzyme E96K, E96G, E96A, Q252L and Y253C are stable
50
GlcDH-I1 is the most resistant isozyme against heat inactivation at 50°C (pH 6.5)
65
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-III loses about 30% of initial activity, isoenzyme GlcDH-IV loses about 10% of initial activity, isoenzyme IWG2 is stable
65
-
pH 6.5, 20 min, complete loss of activity of mutant enzyme Q252L, about 50% loss of activity of mutant enzyme E96K, about 10% loss of activity of mutant enzyme E96A
65
wild-type enzyme retains 20% activity after 20 min at 65°C
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Priestia megaterium
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Priestia megaterium
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Priestia megaterium
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61
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71
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2005
Priestia megaterium (P40288), Priestia megaterium IGW3 (P40288)
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1983
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1984
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1987
Priestia megaterium, Priestia megaterium MI286
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Heilmann, H.J.; Maegert, H.J.; Gassen, H.G.
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Priestia megaterium, Priestia megaterium M1286
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2007
Priestia megaterium, Priestia megaterium AS1.223
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Priestia megaterium, Priestia megaterium (P39485)
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NAD(P)-dependent glucose dehydrogenase applications for biosensors, bioelectrodes, and biofuel cells
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2020
Aspergillus niger, Priestia megaterium, Thermoplasma acidophilum
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brenda
Qian, W.; Ou, L.; Li, C.; Pan, J.; Xu, J.; Chen, Q.; Zheng, G.
Evolution of glucose dehydrogenase for cofactor regeneration in bioredox processes with denaturing agents
ChemBioChem
21
2680-2688
2020
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Plz, M.; Petrovicova, T.; Rebros, M.
Semi-continuous flow biocatalysis with affinity co-immobilized ketoreductase and glucose dehydrogenase
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25
4278
2020
Priestia megaterium
brenda