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0.31
4-nitrobenzaldehyde
-
-
0.05
5-cyano-2,3-ditolyl tetrazolium chloride
-
-
0.0019
azidonitrophenyl-gamma-aminobutyryl-NADPH
-
-
0.000001 - 0.0466
cytochrome c
7.2
ethanol
-
microsomal ethanol oxidizing system
0.0072 - 0.1193
ferricyanide
0.00087 - 5
ferricytochrome c
0.055 - 0.077
oxidized 2,6-dichlorophenolindophenol
0.0018 - 0.011
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
0.0078
oxidized cytochrome c
at pH 7.8 and 25°C
-
additional information
additional information
-
1.4
4-Nitroacetophenone
-
-
1.4
4-Nitroacetophenone
-
electron donor NADH, electron acceptor dichlorophenolindophenol
0.000001
cytochrome c
wild type, cosubstrate FAD, Km below
0.00012
cytochrome c
T491V mutant, cosubstrate FAD
0.0008
cytochrome c
G488L mutant, cosubstrate FAD
0.0015
cytochrome c
W677X mutant, cosubstrate NADPH
0.0028
cytochrome c
W677Y mutant, cosubstrate NADPH
0.0041
cytochrome c
R454E mutant, cosubstrate NADPH
0.0056
cytochrome c
S678X mutant, cosubstrate NADPH
0.0058
cytochrome c
Y456S mutant, cosubstrate NADPH
0.0059
cytochrome c
T491V mutant, cosubstrate NADPH
0.006
cytochrome c
-
spleen
0.0062
cytochrome c
wild type, cosubstrate NADPH
0.0063
cytochrome c
C472T mutant, cosubstrate NADPH
0.0077
cytochrome c
G488L mutant, cosubstrate NADPH
0.0078
cytochrome c
Y456S mutant, cosubstrate FAD
0.0095
cytochrome c
-
kidney
0.0131
cytochrome c
-
Y140F/178F double mutant
0.0135
cytochrome c
deletion mutant T236/G237
0.0138
cytochrome c
pH 7.5, 25°C
0.014
cytochrome c
-
Y178F mutant
0.015
cytochrome c
deletion mutant T236/G237/E238/E239
0.0178
cytochrome c
-
native enzyme, liver
0.0185
cytochrome c
-
Y178D mutant
0.0188
cytochrome c
-
Y140F mutant
0.0191
cytochrome c
-
Y140D mutant
0.0211
cytochrome c
-
wild type
0.0251
cytochrome c
R454E mutant, cosubstrate FAD
0.0466
cytochrome c
-
cosubstrate NADPH
0.0072
ferricyanide
pH 7.4, 25°C
0.0276
ferricyanide
pH 7.4, 25°C
0.1193
ferricyanide
at pH 7.4 and 25°C
0.00087
ferricytochrome c
-
at pH 7.5 and 25°C
0.0012
ferricytochrome c
isozyme CPR1, at 25°C, pH 7.4
0.0016
ferricytochrome c
isozyme CPR1, at 25°C, pH 7.4
0.002
ferricytochrome c
-
wild type enzyme, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0024
ferricytochrome c
-
mutant enzyme E115A/E116A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0025
ferricytochrome c
-
mutant enzyme D113A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0034
ferricytochrome c
-
mitochondrial reductase
0.0036
ferricytochrome c
-
mutant enzyme E115A/E116A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.004
ferricytochrome c
-
wild type enzyme, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0043
ferricytochrome c
-
grown on glycerol
0.00455
ferricytochrome c
-
grown on alkanes
0.0052
ferricytochrome c
-
mutant enzyme D113A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.006
ferricytochrome c
-
mutant enzyme E115A/E116A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0078
ferricytochrome c
-
-
0.0085
ferricytochrome c
-
wild type enzyme, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0098
ferricytochrome c
pH 7.7, 30°C
0.01
ferricytochrome c
-
-
0.0105
ferricytochrome c
-
microsomal reductase
0.011
ferricytochrome c
-
full length enzyme, pH 7.8, 25°C
0.011
ferricytochrome c
-
mutant enzyme D113A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0117
ferricytochrome c
-
pH 7.5, 41°C
0.012
ferricytochrome c
-
truncated enzyme, pH 7.8, 25°C
0.01282
ferricytochrome c
-
at pH 8.0 and 50°C
0.0129
ferricytochrome c
pH 7.4, 25°C
0.013
ferricytochrome c
-
mutant enzyme E115A/E116A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0159
ferricytochrome c
-
pH 7.6, 25°C
0.016
ferricytochrome c
-
mutant enzyme E115A/E116A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0167
ferricytochrome c
-
at pH 7.5 and 25°C
0.017
ferricytochrome c
pH 7.7, 30°C
0.018
ferricytochrome c
pH 7.7, 30°C
0.0182
ferricytochrome c
-
determined on the basis of a sequential mechanism
0.0189
ferricytochrome c
-
at pH 8.5 and 23°C
0.019
ferricytochrome c
-
wild type enzyme, pH not specified in the publication, at 25°C
0.02
ferricytochrome c
-
wild type enzyme, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.023
ferricytochrome c
-
wild type enzyme, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0239
ferricytochrome c
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C
0.025
ferricytochrome c
-
mutant enzyme D113A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.026
ferricytochrome c
-
mutant enzyme D113A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0372
ferricytochrome c
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0439
ferricytochrome c
-
at pH 7.5 and 23°C
0.048
ferricytochrome c
-
pH 7.7
0.0514
ferricytochrome c
at pH 7.4 and 25°C
0.057
ferricytochrome c
-
-
0.06289
ferricytochrome c
-
-
0.0732
ferricytochrome c
pH 7.4, 25°C
0.0746
ferricytochrome c
-
at pH 9.5 and 23°C
0.081
ferricytochrome c
isoform CPR1, at pH 7.6 and 25°C
0.0924
ferricytochrome c
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.39
ferricytochrome c
-
mutant enzyme R600W
0.92
ferricytochrome c
-
mutant enzyme P452L
0.99
ferricytochrome c
-
mutant enzyme A503V
1.15
ferricytochrome c
-
mutant enzyme P284T
1.19
ferricytochrome c
-
wild-type enzyme
1.37
ferricytochrome c
-
mutant enzyme V472M
1.61
ferricytochrome c
-
mutant enzyme G213E
1.84
ferricytochrome c
-
mutant enzyme A485T
1.86
ferricytochrome c
-
mutant enzyme E300K
2.07
ferricytochrome c
-
mutant enzyme R406H
2.09
ferricytochrome c
-
mutant enzyme A462T
2.16
ferricytochrome c
-
mutant enzyme delE53
2.25
ferricytochrome c
-
mutant enzyme P284L
2.31
ferricytochrome c
-
mutant enzyme P55L
2.5 - 5
ferricytochrome c
-
mutant enzyme D211L
0.0084
NADH
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0108
NADH
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0133
NADH
-
microsomal reductase
4
NADH
-
wild type enzyme, pH not specified in the publication, at 25°C
4.3
NADH
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C
20
NADH
-
mitochondrial reductase
26.76
NADH
-
at pH 7.5 and 25°C
0.000001
NADPH
wild type, cosubstrate FAD, Km below
0.00012
NADPH
T491V mutant, cosubstrate FAD
0.00014
NADPH
mutant enzyme D634N, at pH 7.5 and 25°C
0.00019
NADPH
mutant enzyme D634A, at pH 7.5 and 25°C
0.00031
NADPH
-
mutant enzyme H322A, at pH 7.5 and 25°C
0.00058
NADPH
-
mutant enzyme H322Q, at pH 7.5 and 25°C
0.0007
NADPH
wild type enzyme, at pH 7.5 and 25°C
0.00071
NADPH
-
wild type enzyme, at pH 7.5 and 25°C
0.00071
NADPH
-
at pH 7.5 and 25°C
0.0008
NADPH
G488L mutant, cosubstrate FAD
0.00102
NADPH
-
at pH 7.5 and 25°C
0.00106
NADPH
mutant enzyme A635G, at pH 7.5 and 25°C
0.00106
NADPH
mutant enzyme R636S, at pH 7.5 and 25°C
0.00122
NADPH
-
at pH 7.5 and 25°C
0.0016
NADPH
mutant enzyme R636A, at pH 7.5 and 25°C
0.0017
NADPH
-
mitochondrial reductase
0.0018
NADPH
mutant enzyme A635G/R636S, at pH 7.5 and 25°C
0.0019
NADPH
-
full length enzyme, pH 7.8, 25°C
0.0022
NADPH
pH 7.4, 25°C
0.0022
NADPH
-
truncated enzyme, pH 7.8, 25°C
0.0027
NADPH
deletion mutant T236/G237/E238/E239
0.003
NADPH
deletion mutant T236/G237
0.0037
NADPH
pH 7.4, 25°C
0.0046
NADPH
isozyme CPR1, at 25°C, pH 7.4
0.00506
NADPH
purified recombinant enzyme, pH 7.8, 25°C
0.005208
NADPH
-
at pH 8.0 and 50°C
0.0055
NADPH
-
microsomal reductase
0.0056
NADPH
isozyme CPR1, at 25°C, pH 7.4
0.00577
NADPH
pH 7.7, 30°C
0.0064
NADPH
-
wild type, cosubstrate cytochrome c
0.00648
NADPH
purified recombinant enzyme, pH 7.8, 25°C
0.0066
NADPH
-
native enzyme, liver, cosubstrate cytochrome c
0.0066
NADPH
-
Y140D mutant, cosubstrate cytochrome c
0.0071
NADPH
-
Y178F mutant, cosubstrate cytochrome c
0.0078
NADPH
-
Y140F mutant, cosubstrate cytochrome c
0.0078
NADPH
Y456S mutant, cosubstrate FAD
0.0085
NADPH
W677X mutant, cosubstrate cytochrome c
0.0086
NADPH
-
at pH 7.5 and 25°C
0.0094
NADPH
-
pH 7.5, 41°C
0.0095
NADPH
-
Y178D mutant, cosubstrate cytochrome c
0.0114
NADPH
-
Y140F/178F double mutant, cosubstrate cytochrome c
0.0116
NADPH
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C
0.0125
NADPH
-
wild type enzyme, pH not specified in the publication, at 25°C
0.0129
NADPH
-
pH 7.6, 25°C
0.0134
NADPH
G488L mutant, cosubstrate cytochrome c
0.0143
NADPH
W677Y mutant, cosubstrate cytochrome c
0.0163
NADPH
wild type, cosubstrate cytochrome c
0.0166
NADPH
R454E mutant, cosubstrate cytochrome c
0.0187
NADPH
at pH 7.4 and 25°C
0.0192
NADPH
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0199
NADPH
S678X mutant, cosubstrate cytochrome c
0.0201
NADPH
T491V mutant, cosubstrate cytochrome c
0.0217
NADPH
C472T mutant, cosubstrate cytochrome c
0.025
NADPH
-
mutant enzyme Y607C
0.0251
NADPH
R454E mutant, cosubstrate FAD
0.029
NADPH
-
grown on alkanes
0.0308
NADPH
-
determined on the basis of a sequential mechanism
0.033
NADPH
-
grown on glycerol
0.0341
NADPH
-
cosubstrate cytochrome c
0.0425
NADPH
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.05
NADPH
Coleus scutellarioides
-
0.05
NADPH
Coleus scutellarioides
recombinant yeast microsomal CPR, pH 7.5, 35°C
0.0511
NADPH
pH 7.7, 30°C
0.0548
NADPH
Y456S mutant, cosubstrate cytochrome c
0.05488
NADPH
pH 7.7, 30°C
0.066
NADPH
-
mutant enzyme P284T
0.084
NADPH
-
mutant enzyme R600W
0.125
NADPH
-
mutant enzyme P452L
0.144
NADPH
-
wild-type enzyme
0.144
NADPH
-
mutant enzyme A485T
0.146
NADPH
-
mutant enzyme P55L
0.151
NADPH
-
mutant enzyme delE53
0.153
NADPH
-
mutant enzyme D211L
0.155
NADPH
-
mutant enzyme A503V
0.157
NADPH
-
mutant enzyme P284L
0.169
NADPH
-
mutant enzyme V472M
0.177
NADPH
-
mutant enzyme R406H
0.196
NADPH
-
mutant enzyme G213E
0.215
NADPH
Coleus scutellarioides
recombinant yeast internal CPR, pH 7.5, 35°C
0.222
NADPH
-
mutant enzyme E300K
0.276
NADPH
-
mutant enzyme A462T
0.055
oxidized 2,6-dichlorophenolindophenol
-
grown on glycerol
0.077
oxidized 2,6-dichlorophenolindophenol
-
grown on alkanes
0.0018
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0021
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0022
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0026
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0026
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0031
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0038
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0039
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0041
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0062
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0063
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0065
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0087
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.01
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.011
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
additional information
additional information
-
-
-
additional information
additional information
-
cosubstrate NADH, biphasic kinetic
-
additional information
additional information
-
O2-generation
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
kinetic mechanism, overview
-
additional information
additional information
-
kinetic mechanism, overview
-
additional information
additional information
CsCPR displays Michaelis-Menten behavior with respect to both cytochrome c and NADPH
-
additional information
additional information
-
kinetics by stopped-flow spectroscopy
-
additional information
additional information
steady-state kinetics of P450 enzyme reactions supported by Malassezia globosa NPR, overview
-
additional information
additional information
-
steady-state kinetics of P450 enzyme reactions supported by Malassezia globosa NPR, overview
-