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2-amino-2-deoxy-D-mannose + NADP+
2-amino-2-deoxy-D-mannono-1,5-lactone + NADPH
-
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
the enzyme has a strong preference for NADP+ over NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
D-glucose + 1,N6-ethanoadenine-NADP+
D-glucono-1,5-lactone + 1,N6-ethanoadenine-NADPH
D-glucose + N1-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N1-(2-aminoethyl)-NADPH
D-glucose + N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N6-(2-aminoethyl)-NADPH
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
D-glucose + polyethylene glycol(MW 20000)-N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + polyethylene glycol(MW 20000)-N6-(2-aminoethyl)-NADPH + H+
-
-
-
-
r
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
additional information
?
-
-
reduction of C=N bonds with good levels of conversion (more than 50%) and excellent enantioselectivity (up to more than 99% enantiomeric excess) by glucose dehydrogenase represents a promiscuous catalytic activity of this enzyme
-
-
-
beta-D-glucose + NAD+
?
activity with NAD+ is 26% of the activity with NADP+
-
-
?
beta-D-glucose + NAD+
?
activity with NAD+ is 26% of the activity with NADP+
-
-
?
beta-D-glucose + NADP+
?
activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
-
-
?
beta-D-glucose + NADP+
?
activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
the enzyme has a strong preference for NADP+ over NAD+
-
-
?
D-glucose + 1,N6-ethanoadenine-NADP+
D-glucono-1,5-lactone + 1,N6-ethanoadenine-NADPH
-
-
-
r
D-glucose + 1,N6-ethanoadenine-NADP+
D-glucono-1,5-lactone + 1,N6-ethanoadenine-NADPH
-
-
-
r
D-glucose + N1-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N1-(2-aminoethyl)-NADPH
-
-
-
r
D-glucose + N1-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N1-(2-aminoethyl)-NADPH
-
-
-
r
D-glucose + N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N6-(2-aminoethyl)-NADPH
-
-
-
r
D-glucose + N6-(2-aminoethyl)-NADP+
D-glucono-1,5-lactone + N6-(2-aminoethyl)-NADPH
-
-
-
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
4% of the reverse reaction when assayed with D-glucono-1,5-lactone and NADPH at neutral or weak alkaline pH
-
-
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
unphosphorylated glucose as substrate
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80°C. At 25°C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
the enzyme prefers NADP+ over NAD+ as the cofactor. It shows a larger Km value for NAD+ (4.5 mM) than for NADP+ (0.12 mM) at 80°C. At 25°C the Km values are 0.069 mM for NAD+ and 0.0059 mM for NADP+
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
-
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
-
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
-
-
-
?
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0.05
1,N6-ethanoadenine-NADP+
-
-
29
2-amino-2-deoxy-D-mannose
-
-
0.07
N1-(2-aminoethyl)-NADP+
-
-
0.03
N6-(2-aminoethyl)-NADP+
-
-
0.09
polyethylene glycol(MW 20000)-N6-(2-aminoethyl)-NADP+
-
-
-
3.9
beta-D-glucose
pH 8.8, 40°C
12.9
beta-D-glucose
wild type enzyme, using NAD+ as cosubstrate
15
beta-D-glucose
mutant enzyme G206D, using NAD+ as cosubstrate
24
beta-D-glucose
mutant enzyme R207I, using NADP+ as cosubstrate
31.1
beta-D-glucose
wild type enzyme, using NADP+ as cosubstrate
32
beta-D-glucose
mutant enzyme R207I, using NAD+ as cosubstrate
52
beta-D-glucose
mutant enzyme G206D, using NADP+ as cosubstrate
57
beta-D-glucose
mutant enzyme G206D/R207I/R208N, using NAD+ as cosubstrate
80
beta-D-glucose
mutant enzyme G206D/R207I, using NAD+ as cosubstrate
0.0286
D-glucose
pH 9.0, 25°C, wild-type enzyme
0.0286
D-glucose
wild type enzyme, at pH 9.0 and 25°C
0.0293
D-glucose
pH 9.0, 25°C, mutant enzyme I189V
0.0293
D-glucose
mutant enzyme I189V, at pH 9.0 and 25°C
0.0391
D-glucose
pH 9.0, 25°C, mutant enzyme V254I
0.0391
D-glucose
mutant enzyme V254I, at pH 9.0 and 25°C
0.287
D-glucose
pH 9.0, 80°C, wild-type enzyme
0.287
D-glucose
wild type enzyme, at pH 9.0 and 80°C
0.314
D-glucose
pH 9.0, 80°C, mutant enzyme I189V
0.314
D-glucose
mutant enzyme I189V, at pH 9.0 and 80°C
0.457
D-glucose
pH 9.0, 80°C, mutant enzyme V254I
0.457
D-glucose
mutant enzyme V254I, at pH 9.0 and 80°C
1.8
D-glucose
-
mutant D344K
2.2
D-glucose
-
mutant D216K
2.4
D-glucose
-
mutant D172K
2.8
D-glucose
-
wild-type
2.8
D-glucose
with NADP+ as coenzyme
2.8
D-glucose
wild-type, pH 8.8, 40°C
3.2
D-glucose
-
mutant D172K/D216K/D344K
12.9
D-glucose
with NAD+ as coenzyme
12.9
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C
15
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
24
D-glucose
mutant R207I, pH 8.8, 40°C
32
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
52
D-glucose
mutant G206D, pH 8.8, 40°C
57
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
80
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
1.8
D-mannose
-
in 0.1 M Tris-buffer pH 8.0
5.6
D-mannose
-
in 0.1 M potassium phosphate pH 6.2
0.035
NAD(P)+
with NADP+ as coenzyme
0.4
NAD(P)+
with NAD+ as coenzyme
0.4
NAD+
wild type enzyme
0.4
NAD+
wild-type, pH 8.8, 40°C
0.49
NAD+
mutant enzyme G206D
0.49
NAD+
mutant G206D, pH 8.8, 40°C
1.3
NAD+
mutant enzyme G206D/R207I/R208N
1.3
NAD+
mutant enzyme R207I
1.3
NAD+
mutant G206D/R207I/R208N, pH 8.8, 40°C
1.3
NAD+
mutant R207I, pH 8.8, 40°C
2.7
NAD+
mutant enzyme G206D/R207I
2.7
NAD+
mutant G206D/R207I, pH 8.8, 40°C
0.00588
NADP+
pH 9.0, 25°C, wild-type enzyme
0.00588
NADP+
wild type enzyme, at pH 9.0 and 25°C
0.00876
NADP+
pH 9.0, 25°C, mutant enzyme V254I
0.00876
NADP+
mutant enzyme V254I, at pH 9.0 and 25°C
0.00927
NADP+
pH 9.0, 25°C, mutant enzyme I189V
0.00927
NADP+
mutant enzyme I189V, at pH 9.0 and 25°C
0.035
NADP+
wild type enzyme
0.035
NADP+
-
mutant D216K
0.035
NADP+
wild-type, pH 8.8, 40°C
0.036
NADP+
-
mutant D172K
0.046
NADP+
-
mutant D172K/D216K/D344K
0.056
NADP+
-
mutant D344K
0.109
NADP+
pH 9.0, 80°C, mutant enzyme I189V
0.109
NADP+
mutant enzyme I189V, at pH 9.0 and 80°C
0.117
NADP+
pH 9.0, 80°C, wild-type enzyme
0.118
NADP+
wild type enzyme, at pH 9.0 and 80°C
0.132
NADP+
pH 9.0, 80°C, mutant enzyme V254I
0.132
NADP+
mutant enzyme V254I, at pH 9.0 and 80°C
1.7
NADP+
mutant enzyme R207I
1.7
NADP+
mutant R207I, pH 8.8, 40°C
2.6
NADP+
mutant enzyme G206D
2.6
NADP+
mutant G206D, pH 8.8, 40°C
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0.00041
D-glucose
-
mutant D216K
0.00041
D-glucose
-
mutant D344K
0.00045
D-glucose
-
mutant D172K
0.00045
D-glucose
-
mutant D172K/D216K/D344K
0.00051
D-glucose
-
wild-type
0.0097
D-glucose
mutant enzyme I189V, at pH 9.0 and 80°C
0.0101
D-glucose
wild type enzyme, at pH 9.0 and 80°C
0.0167
D-glucose
mutant enzyme V254I, at pH 9.0 and 80°C
0.047
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
0.072
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
0.085
D-glucose
pH 9.0, 25°C, mutant enzyme I189V
0.085
D-glucose
mutant enzyme I189V, at pH 9.0 and 25°C
0.11
D-glucose
pH 9.0, 25°C, wild-type enzyme
0.11
D-glucose
wild type enzyme, at pH 9.0 and 25°C
0.2
D-glucose
mutant R207I, pH 8.8, 40°C
0.205
D-glucose
pH 9.0, 25°C, mutant enzyme V254I
0.205
D-glucose
mutant enzyme V254I, at pH 9.0 and 25°C
0.26
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C
0.26
D-glucose
mutant G206D, pH 8.8, 40°C
0.5
D-glucose
wild-type, pH 8.8, 40°C
0.57
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
0.9
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
9.7
D-glucose
pH 9.0, 80°C, mutant enzyme I189V
10.1
D-glucose
pH 9.0, 80°C, wild-type enzyme
16.7
D-glucose
pH 9.0, 80°C, mutant enzyme V254I
0.0097
NADP+
mutant enzyme I189V, at pH 9.0 and 80°C
0.0101
NADP+
wild type enzyme, at pH 9.0 and 80°C
0.0167
NADP+
mutant enzyme V254I, at pH 9.0 and 80°C
0.085
NADP+
pH 9.0, 25°C, mutant enzyme I189V
0.0857
NADP+
mutant enzyme I189V, at pH 9.0 and 25°C
0.11
NADP+
pH 9.0, 25°C, wild-type enzyme
0.11
NADP+
wild type enzyme, at pH 9.0 and 25°C
0.205
NADP+
pH 9.0, 25°C, mutant enzyme V254I
0.205
NADP+
mutant enzyme V254I, at pH 9.0 and 25°C
9.7
NADP+
pH 9.0, 80°C, mutant enzyme I189V
10.1
NADP+
pH 9.0, 80°C, wild-type enzyme
16.7
NADP+
pH 9.0, 80°C, mutant enzyme V254I
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0.0000008 - 5.25
D-glucose
0.0000008
D-glucose
cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C
0.000002
D-glucose
cosubstrate NAD+, mutant R207I, pH 8.8, 40°C
0.000005
D-glucose
mutant G206D, pH 8.8, 40°C
0.000008
D-glucose
mutant R207I, pH 8.8, 40°C
0.000012
D-glucose
cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C
0.00002
D-glucose
cosubstrate NAD+, wild-type, pH 8.8, 40°C
0.000038
D-glucose
cosubstrate NAD+, mutant G206D, pH 8.8, 40°C
0.00019
D-glucose
wild-type, pH 8.8, 40°C
0.31
D-glucose
pH 9.0, 80°C, mutant enzyme I189V
0.31
D-glucose
mutant enzyme I189V, at pH 9.0 and 80°C
0.351
D-glucose
pH 9.0, 80°C, wild-type enzyme
0.351
D-glucose
wild type enzyme, at pH 9.0 and 80°C
0.365
D-glucose
pH 9.0, 80°C, mutant enzyme V254I
0.365
D-glucose
mutant enzyme V254I, at pH 9.0 and 80°C
2.91
D-glucose
pH 9.0, 25°C, mutant enzyme I189V
2.91
D-glucose
mutant enzyme I189V, at pH 9.0 and 25°C
3.82
D-glucose
pH 9.0, 25°C, wild-type enzyme
3.82
D-glucose
wild type enzyme, at pH 9.0 and 25°C
5.25
D-glucose
pH 9.0, 25°C, mutant enzyme V254I
5.25
D-glucose
mutant enzyme V254I, at pH 9.0 and 25°C
0.000035
NAD+
mutant G206D/R207I/R208N, pH 8.8, 40°C
0.000055
NAD+
mutant R207I, pH 8.8, 40°C
0.00033
NAD+
mutant G206D/R207I, pH 8.8, 40°C
0.00073
NAD+
wild-type, pH 8.8, 40°C
0.00112
NAD+
mutant G206D, pH 8.8, 40°C
0.0001
NADP+
mutant G206D, pH 8.8, 40°C
0.00012
NADP+
mutant R207I, pH 8.8, 40°C
0.015
NADP+
wild-type, pH 8.8, 40°C
0.092
NADP+
pH 9.0, 25°C, mutant enzyme I189V
0.092
NADP+
mutant enzyme I189V, at pH 9.0 and 25°C
0.126
NADP+
pH 9.0, 80°C, mutant enzyme V254I
0.126
NADP+
mutant enzyme V254I, at pH 9.0 and 80°C
0.186
NADP+
pH 9.0, 25°C, wild-type enzyme
0.186
NADP+
wild type enzyme, at pH 9.0 and 25°C
0.234
NADP+
pH 9.0, 25°C, mutant enzyme V254I
0.234
NADP+
mutant enzyme V254I, at pH 9.0 and 25°C
0.863
NADP+
pH 9.0, 80°C, wild-type enzyme
0.863
NADP+
wild type enzyme, at pH 9.0 and 80°C
0.893
NADP+
pH 9.0, 80°C, mutant enzyme I189V
0.893
NADP+
mutant enzyme I189V, at pH 9.0 and 80°C
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D172K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D172K/D216K/D344K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D216K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D344K
-
mutation in surface residue, mutant protein is slightly less halotolerant than wild-type
D38C
crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein
D38C
-
crystallization of a range of binary and ternary complexes of the wild-type and a D38C mutant protein
-
I189V
the mutant has decreased kcat and kcat/Km values at both 25°C and 80°C compared to the wild type enzyme
G206D
less efficient with NADP+ than the wild type, 1.6fold increase in ratio kcat/Km for NAD+
G206D
prefers NAD+ over NADP+
G206D
the mutant is less efficient with NADP+ than the wild type enzyme, the relation kcat/KNAD+ is 1.6times higher than in the wild type, resulting in an enzyme that prefers NAD+ over NADP+
G206D/R207I
active only with NAD+
G206D/R207I
no activity with NADP+, highest reaction rate with cofactor NAD+ of all mutants tested
G206D/R207I
the mutant shows no activity with NADP+, when the coenzyme NAD+ is incubated with this double mutant, it reaches the highest kcat value, between 1.5 and 2times higher than the kcat of the wild type enzyme with NADP+, and between 3 and 4times higher than the kcat of the wild type with NAD+
G206D/R207I/R208N
active only with NAD+
G206D/R207I/R208N
no activity with NADP+
G206D/R207I/R208N
the mutant shows no activity with NADP+
R207I
less efficient with NAD+ or NADP+ than the wild-type enzyme
R207I
less efficient with NADP+ than the wild type
R207I
the mutant is less efficient with NADP+ than the wild type enzyme, shows an increase of 48times in Km value with NADP+ when compared with the wild type accompanied by a decrease in kcat, which clearly makes the R207I mutant less efficient in catalysis with NADP+, the R207I substitution also makes the enzyme less efficient with NAD+, with a decrease of 4 times in kcat/Km, this substitution also increases the Km for glucose
V254I
mutant has improved kcat and kcat/Km values at both 25°C and 80°C. The thermal stability of the mutant enzyme was comparable to that of the wild-type enzyme. Calculation of the energetic contribution of the V254I mutation for the dehydrogenase reaction reveals that the mutation destabilizes the enzyme-NADPD-glucose ternary complex and reduces the transition-state energy, thus enhancing catalysis
V254I
the mutant has improved kcat and kcat/Km values at both 25°C and 80°C compared to the wild type enzyme
V254I
-
mutant has improved kcat and kcat/Km values at both 25°C and 80°C. The thermal stability of the mutant enzyme was comparable to that of the wild-type enzyme. Calculation of the energetic contribution of the V254I mutation for the dehydrogenase reaction reveals that the mutation destabilizes the enzyme-NADPD-glucose ternary complex and reduces the transition-state energy, thus enhancing catalysis
-
additional information
-
Escherichia coli strain expressing both recombinant glucose 1-dehydrogenase and a glucose facilitator for uptake of unphosphorylated glucose shows a nine times higher initial alpha-pinene oxide formation rate corresponding to a sixfold higher yield of 20 mg per g cell dry weight after 1.5 h and to a sevenfold increased alpha-pinene oxide yield in the presence of glucose compared to glucose-free conditions
additional information
-
introduction of both, GLF and GlcDH, in P450-overexpressing Escherichia coli should enable the cell to carry out a straightforward intracellular cofactor regeneration driven by externally added glucose. For the generation of recombinant Escherichia coli strains carrying two plasmids, these are transformed successively. Firstly, pZY507glf is transformed into Escherichia coli BL21 (DE3). Subsequently, competent cells are prepared from a positive transformant, and then pETDUETbm-3qm glcdh is transformed.
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