BRENDA - Enzyme Database

Preparative use of isolated CYP102 monooxygenases - a critical appraisal

Eiben, S.; Kaysser, L.; Maurer, S.; Kuehnel, K.; Urlacher, V.B.; Schmid, R.D.; J. Biotechnol. 124, 662-669 (2006)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
1.14.14.1
synthesis
the enzyme is intersting for regioselective production of compounds
Bacillus subtilis
1.14.14.1
synthesis
the enzyme is intersting for regioselective production of compounds
Bacillus megaterium
Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
1.14.14.1
expression in Escherichia coli in fed-batch fermentation
Bacillus subtilis
1.14.14.1
expression in Escherichia coli in fed-batch fermentation
Bacillus megaterium
Crystallization (Commentary)
EC Number
Crystallization (Commentary)
Organism
1.14.14.1
crystallization of the wild-type and mutant CYP102A1 with and without bound substrates and one including theFMNbinding domain
Bacillus megaterium
Engineering
EC Number
Protein Variants
Commentary
Organism
1.14.14.1
A74E/F87V/P386S
site-directed mutagenesis, the mutant shows altered regioselectivity and activity, and cofactor specificity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/R966D
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/R966M
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/S965D
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/W1046A
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/W1046S
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
F87G
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
F87GA
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
additional information
construction of an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
Bacillus megaterium
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.14.14.1
H2O2
at high concentrations
Bacillus megaterium
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14.14.1
0.002
-
NADPH
mutants A74G/F87V/L188Q/W1046A and A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
0.0025
-
NADPH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
0.004
-
NADH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
0.004
-
NADH
mutant enzyme A74G/F87V/L188Q/W1046A/S965D, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.01
-
NADH
mutant A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
0.01
-
NADH
mutant enzyme A74G/F87V/L188Q/W1046S, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.02
-
NADPH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
0.02
-
NADH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
0.02
-
NADH
mutant enzyme A74G/F87V/L188Q/W1046A, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.05
-
NADPH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
0.13
-
NADPH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
0.33
-
NADH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
0.33
-
NADH
mutant enzyme A74G/F87V/L188Q/R966D, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.54
-
NADH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
0.54
-
NADH
mutant enzyme A74G/F87V/L188Q/R966M, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
1.43
-
NADH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
1.43
-
NADH
mutant enzyme A74G/F87V/L188Q, pH and temperature not specified in the publication
Bacillus megaterium
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.14.1
Fe2+
a heme-containing P450 monooxygenase
Bacillus subtilis
1.14.14.1
Fe2+
a heme-containing P450 monooxygenase
Bacillus megaterium
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.14.14.1
Bacillus megaterium
-
-
-
1.14.14.1
Bacillus subtilis
-
-
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
1.14.14.1
several purification protocols are published, based on ion exchange chromatography, hydrophobic interaction chromatography or metal affinity chromatography, resulting in high levels of purity depending on the further application of the enzymes
Bacillus subtilis
1.14.14.1
several purification protocols are published, based on ion exchange chromatography, hydrophobic interaction chromatography or metal affinity chromatography, resulting in high levels of purity depending on the further application of the enzymes
Bacillus megaterium
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.14.14.1
beta-ionone + [reduced NADPH-hemoprotein reductase] + O2
-
674972
Bacillus megaterium
4-hydroxy-beta-ionone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
1.14.14.1
cytochrome c + NADH + H+ + O2
-
674972
Bacillus megaterium
?
-
-
-
r
1.14.14.1
cytochrome c + O2 + NADH
-
674972
Bacillus megaterium
?
-
-
-
r
1.14.14.1
additional information
activity involves cytochrome c reduction, CYP102A1 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions, an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor
674972
Bacillus megaterium
?
-
-
-
?
1.14.14.1
additional information
activity involves cytochrome c reduction, CYP102A3 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions
674972
Bacillus subtilis
?
-
-
-
?
1.14.14.1
styrene + O2 + H2O2
engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
674972
Bacillus megaterium
(R)-styrene oxide + (S)-styrene oxide + H2O
-
-
-
?
1.14.14.1
styrene + O2 + NAD(P)H
-
674972
Bacillus megaterium
(R)-styrene oxide + (S)-styrene oxide + H2O + NAD(P)+
enantioselective styrene oxidation with different CYP102A1 mutants, 25% S-isomer for the wild-type enzyme, 58% S-isomer for mutant A74E/F87V/P386S, 49% R-isomer for mutant F87A, 65% R-isomer for mutant A74G/F87V/L188Q, and 92% R-isomer for mutant F87G
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.14.14.1
More
the enzyme is a natural fusion enzyme composed of an N-terminal heme monooxygenase linked to the C-terminal diflavin reductase domain
Bacillus subtilis
1.14.14.1
More
the enzyme is a natural fusion enzyme composed of an N-terminal heme monooxygenase linked to the C-terminal diflavin reductase domain
Bacillus megaterium
Synonyms
EC Number
Synonyms
Commentary
Organism
1.14.14.1
CYP102 monooxygenase
-
Bacillus subtilis
1.14.14.1
CYP102 monooxygenase
-
Bacillus megaterium
1.14.14.1
CYP102A1
-
Bacillus megaterium
1.14.14.1
CYP102A3
-
Bacillus subtilis
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.14.14.1
additional information
-
melting temperatures of the CYP102A1 monooxygenase and the CYP102A1 reductase domain differ by about 15°C: whereas Tm for the monooxygenase domain is 63°C, it is only 48°C for the reductase domain
Bacillus megaterium
1.14.14.1
46
-
10 min, half-life, wild-type CYP102A1
Bacillus megaterium
1.14.14.1
61
-
10 min, half-life, engineered CYP102A1 heme domain which utilizes H2O2 as electron donor
Bacillus megaterium
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.14.14.1
0.016
-
NADH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
0.43
-
NADPH
mutant F87A
Bacillus megaterium
1.14.14.1
0.45
-
NADPH
wild-type enzyme
Bacillus megaterium
1.14.14.1
0.5
-
NADPH
mutant F87G
Bacillus megaterium
1.14.14.1
0.83
-
NADPH
mutant A74E/F87V/P386S
Bacillus megaterium
1.14.14.1
1.7
-
NADPH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
5.67
-
NADPH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
6.5
-
NADPH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
7
-
NADH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
9.3
-
NADPH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
9.83
-
NADPH
mutant A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
32
-
NADH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
37.83
-
NADH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
46.83
-
NADH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
89
-
NADH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
105.2
-
NADH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
132.2
-
NADPH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
156
-
NADH
mutant A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
183
-
NADPH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
362.8
-
NADPH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.14.14.1
cytochrome c
-
Bacillus subtilis
1.14.14.1
cytochrome c
-
Bacillus megaterium
1.14.14.1
FAD
bound
Bacillus subtilis
1.14.14.1
FAD
bound, binding structure, overview
Bacillus megaterium
1.14.14.1
FMN
bound
Bacillus subtilis
1.14.14.1
FMN
bound, binding structure, overview
Bacillus megaterium
1.14.14.1
additional information
engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
Bacillus megaterium
1.14.14.1
additional information
residues S965, R966 and Y974 are important in the Rossman fold-like binding motif for the cofactor binding and discrimination, overview
Bacillus megaterium
1.14.14.1
NAD(P)H
-
Bacillus megaterium
1.14.14.1
NADPH
-
Bacillus subtilis
Application (protein specific)
EC Number
Application
Commentary
Organism
1.14.14.1
synthesis
the enzyme is intersting for regioselective production of compounds
Bacillus subtilis
1.14.14.1
synthesis
the enzyme is intersting for regioselective production of compounds
Bacillus megaterium
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.14.1
expression in Escherichia coli in fed-batch fermentation
Bacillus subtilis
1.14.14.1
expression in Escherichia coli in fed-batch fermentation
Bacillus megaterium
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.14.14.1
cytochrome c
-
Bacillus subtilis
1.14.14.1
cytochrome c
-
Bacillus megaterium
1.14.14.1
FAD
bound
Bacillus subtilis
1.14.14.1
FAD
bound, binding structure, overview
Bacillus megaterium
1.14.14.1
FMN
bound
Bacillus subtilis
1.14.14.1
FMN
bound, binding structure, overview
Bacillus megaterium
1.14.14.1
additional information
engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
Bacillus megaterium
1.14.14.1
additional information
residues S965, R966 and Y974 are important in the Rossman fold-like binding motif for the cofactor binding and discrimination, overview
Bacillus megaterium
1.14.14.1
NAD(P)H
-
Bacillus megaterium
1.14.14.1
NADPH
-
Bacillus subtilis
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.14.14.1
crystallization of the wild-type and mutant CYP102A1 with and without bound substrates and one including theFMNbinding domain
Bacillus megaterium
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
1.14.14.1
A74E/F87V/P386S
site-directed mutagenesis, the mutant shows altered regioselectivity and activity, and cofactor specificity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/R966D
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/R966M
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/S965D
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/W1046A
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
A74G/F87V/L188Q/W1046S
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
Bacillus megaterium
1.14.14.1
F87G
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
F87GA
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
Bacillus megaterium
1.14.14.1
additional information
construction of an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
Bacillus megaterium
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.14.14.1
H2O2
at high concentrations
Bacillus megaterium
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14.14.1
0.002
-
NADPH
mutants A74G/F87V/L188Q/W1046A and A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
0.0025
-
NADPH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
0.004
-
NADH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
0.004
-
NADH
mutant enzyme A74G/F87V/L188Q/W1046A/S965D, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.01
-
NADH
mutant A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
0.01
-
NADH
mutant enzyme A74G/F87V/L188Q/W1046S, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.02
-
NADPH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
0.02
-
NADH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
0.02
-
NADH
mutant enzyme A74G/F87V/L188Q/W1046A, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.05
-
NADPH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
0.13
-
NADPH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
0.33
-
NADH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
0.33
-
NADH
mutant enzyme A74G/F87V/L188Q/R966D, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
0.54
-
NADH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
0.54
-
NADH
mutant enzyme A74G/F87V/L188Q/R966M, pH and temperature not specified in the publication
Bacillus megaterium
1.14.14.1
1.43
-
NADH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
1.43
-
NADH
mutant enzyme A74G/F87V/L188Q, pH and temperature not specified in the publication
Bacillus megaterium
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.14.1
Fe2+
a heme-containing P450 monooxygenase
Bacillus subtilis
1.14.14.1
Fe2+
a heme-containing P450 monooxygenase
Bacillus megaterium
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.14.1
several purification protocols are published, based on ion exchange chromatography, hydrophobic interaction chromatography or metal affinity chromatography, resulting in high levels of purity depending on the further application of the enzymes
Bacillus subtilis
1.14.14.1
several purification protocols are published, based on ion exchange chromatography, hydrophobic interaction chromatography or metal affinity chromatography, resulting in high levels of purity depending on the further application of the enzymes
Bacillus megaterium
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.14.14.1
beta-ionone + [reduced NADPH-hemoprotein reductase] + O2
-
674972
Bacillus megaterium
4-hydroxy-beta-ionone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
1.14.14.1
cytochrome c + NADH + H+ + O2
-
674972
Bacillus megaterium
?
-
-
-
r
1.14.14.1
cytochrome c + O2 + NADH
-
674972
Bacillus megaterium
?
-
-
-
r
1.14.14.1
additional information
activity involves cytochrome c reduction, CYP102A1 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions, an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor
674972
Bacillus megaterium
?
-
-
-
?
1.14.14.1
additional information
activity involves cytochrome c reduction, CYP102A3 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions
674972
Bacillus subtilis
?
-
-
-
?
1.14.14.1
styrene + O2 + H2O2
engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
674972
Bacillus megaterium
(R)-styrene oxide + (S)-styrene oxide + H2O
-
-
-
?
1.14.14.1
styrene + O2 + NAD(P)H
-
674972
Bacillus megaterium
(R)-styrene oxide + (S)-styrene oxide + H2O + NAD(P)+
enantioselective styrene oxidation with different CYP102A1 mutants, 25% S-isomer for the wild-type enzyme, 58% S-isomer for mutant A74E/F87V/P386S, 49% R-isomer for mutant F87A, 65% R-isomer for mutant A74G/F87V/L188Q, and 92% R-isomer for mutant F87G
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.14.14.1
More
the enzyme is a natural fusion enzyme composed of an N-terminal heme monooxygenase linked to the C-terminal diflavin reductase domain
Bacillus subtilis
1.14.14.1
More
the enzyme is a natural fusion enzyme composed of an N-terminal heme monooxygenase linked to the C-terminal diflavin reductase domain
Bacillus megaterium
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.14.14.1
additional information
-
melting temperatures of the CYP102A1 monooxygenase and the CYP102A1 reductase domain differ by about 15°C: whereas Tm for the monooxygenase domain is 63°C, it is only 48°C for the reductase domain
Bacillus megaterium
1.14.14.1
46
-
10 min, half-life, wild-type CYP102A1
Bacillus megaterium
1.14.14.1
61
-
10 min, half-life, engineered CYP102A1 heme domain which utilizes H2O2 as electron donor
Bacillus megaterium
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.14.14.1
0.016
-
NADH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
0.43
-
NADPH
mutant F87A
Bacillus megaterium
1.14.14.1
0.45
-
NADPH
wild-type enzyme
Bacillus megaterium
1.14.14.1
0.5
-
NADPH
mutant F87G
Bacillus megaterium
1.14.14.1
0.83
-
NADPH
mutant A74E/F87V/P386S
Bacillus megaterium
1.14.14.1
1.7
-
NADPH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
5.67
-
NADPH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
6.5
-
NADPH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
7
-
NADH
mutant A74G/F87V/L188Q/S965D
Bacillus megaterium
1.14.14.1
9.3
-
NADPH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
9.83
-
NADPH
mutant A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
32
-
NADH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
37.83
-
NADH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium
1.14.14.1
46.83
-
NADH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
89
-
NADH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
105.2
-
NADH
mutant A74G/F87V/L188Q/W1046A
Bacillus megaterium
1.14.14.1
132.2
-
NADPH
mutant A74G/F87V/L188Q
Bacillus megaterium
1.14.14.1
156
-
NADH
mutant A74G/F87V/L188Q/W1046S
Bacillus megaterium
1.14.14.1
183
-
NADPH
mutant A74G/F87V/L188Q/R966D
Bacillus megaterium
1.14.14.1
362.8
-
NADPH
mutant A74G/F87V/L188Q/R966M
Bacillus megaterium