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Information on EC 1.6.2.4 - NADPH-hemoprotein reductase and Organism(s) Rattus norvegicus and UniProt Accession P00388

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EC Tree
     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.2 With a heme protein as acceptor
                1.6.2.4 NADPH-hemoprotein reductase
IUBMB Comments
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases (e.g. EC 1.14.14.1, unspecific monooxygenase) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. It also reduces cytochrome b5 and cytochrome c. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
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Rattus norvegicus
UNIPROT: P00388
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadph-cytochrome p-450 reductase, cytochrome p450 reductase, p450 reductase, p-450 reductase, nadph-p450 reductase, p450 bm3, p450 oxidoreductase, nadph cytochrome p450 reductase, cytochrome p450 oxidoreductase, cypor, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADPH P450 oxidoreductase
-
NADPH-cytochrome P450 oxidoreductase
-
NADPH-cytochrome P450 reductase
-
P450 oxidoreductase
-
aldehyde reductase (NADPH-dependent)
-
-
-
-
cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent)
-
-
-
-
cytochrome P450 oxidoreductase
-
-
cytochrome P450 reductase
-
-
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase
-
-
-
-
FAD-cytochrome c reductase
-
-
-
-
ferrihemprotein P450 reductase
-
-
-
-
NADP-cytochrome c reductase
-
-
-
-
NADP-cytochrome reductase
-
-
-
-
NADPH cytochrome P450 reductase
-
-
NADPH dependent cytochrome P450 reductase
-
-
NADPH-CYP reductase
-
-
NADPH-cytochrome c oxidoreductase
-
-
-
-
NADPH-cytochrome c reductase
-
-
-
-
NADPH-cytochrome p-450 reductase
-
-
-
-
NADPH-cytochrome P450 (CYP) oxidoreductase
-
-
-
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-dependent cytochrome c reductase
-
-
-
-
NADPH-dependent cytochrome P450 reductase
-
-
NADPH-ferricytochrome c oxidoreductase
-
-
-
-
P450R
reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase
-
-
-
-
reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
TPNH-cytochrome c reductase
-
-
-
-
TPNH2 cytochrome c reductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
show the reaction diagram
catalytic cycle and the rate-limiting step, which is at or after the introduction of the second electron from the reductase to the heme iron
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NADPH:hemoprotein oxidoreductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases (e.g. EC 1.14.14.1, unspecific monooxygenase) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. It also reduces cytochrome b5 and cytochrome c. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-03-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
+ NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
1,4-dioxo-2-(trifluoromethyl)-1lambda5,4lambda5-quinoxaline + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
1,4-dioxo-7-(trifluoromethoxy)-1lambda5,2,4lambda5-benzotriazin-3-amine + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
1-oxo-1lambda5,2,4-benzotriazine + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 oxidized nitroblue tetrazolium + NADPH
2 reduced nitroblue tetrazolium + NADP+ + H+
show the reaction diagram
-
-
-
?
3-amino-1,4-dioxo-1lambda5,4lambda5-quinoxaline-2-carbonitrile + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
methyl (1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)carbamate + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)-1,1,1-trifluoromethanesulfonamide + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)acetamide + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)methanesulfonamide + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
N-(1-oxo-1lambda5,2,4-benzotriazin-3-yl)acetamide + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
show the reaction diagram
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome P450 2B4
NADP+ + 2 reduced cytochrome P450 2B4
show the reaction diagram
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
show the reaction diagram
-
-
-
?
tirapazamine + NADPH + H+
1,2,4-benzotriazin-3-amine + 1-oxo-1lambda5,2,4-benzotriazin-3-amine + NADP+
show the reaction diagram
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
NADPH + 5-cyano-2,3-di-p-tolyltetrazolium chloride
NADP+ + (5-cyano-2,3-di-p-tolyltetrazolium chloride) formazan
show the reaction diagram
-
-
formazan is fluorescent
-
?
NADPH + H+ + 2,4,6-trinitrotoluene
NADP+ + nitrite + ?
show the reaction diagram
-
-
-
-
?
NADPH + H+ + 4-nitroacetophenone
?
show the reaction diagram
-
-
-
-
r
NADPH + H+ + 4-nitrobenzaldehyde
?
show the reaction diagram
-
-
-
-
r
NADPH + H+ + 4-nitroso-2,6-dinitrotoluene
NADP+ + 4-hydroxyamino-2,6-dinitrotoluene
show the reaction diagram
-
-
-
-
?
NADPH + H+ + benzalacetone
?
show the reaction diagram
-
-
-
-
r
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
NADPH + H+ + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
NADP+ + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
show the reaction diagram
-
-
-
-
?
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
show the reaction diagram
-
-
-
-
?
NADPH + hexadecanal
NADP+ + hexadecanol
show the reaction diagram
-
brain, hexadecanal replaceable by p-nitroacetophenone, or p-pyridinecarboxaldehyde, benzalacetone or p-nitrobenzaldehyde
-
?
NADPH + octanal
NADP+ + octanol
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
NADPH-cytochrome P450 reductase is a unique universal donor of electrons to practically all known microsomal cytochrome P450s and one of the most important components of the monooxygenase system
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
NADH
-
less effective than NADPH
NADPH
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-chloroethyl ethyl sulfide
-
potent inhibitor
diphenylene iodonium sulfate
-
time-dependent and concentration-dependent inhibition of cDNA-expressed liver enzyme as well as aortic and hepatic microsomal enzyme activity
steapsin
-
brain
-
Tannic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001 - 0.0251
cytochrome c
0.000001 - 0.0548
NADPH
1.4
4-Nitroacetophenone
-
-
0.31
4-nitrobenzaldehyde
-
-
0.05
5-cyano-2,3-ditolyl tetrazolium chloride
-
-
2.5
Benzalacetone
-
-
0.013 - 0.0211
cytochrome c
7.2
ethanol
-
microsomal ethanol oxidizing system
0.002 - 0.026
ferricytochrome c
0.03
hexadecanal
-
-
0.001 - 0.0114
NADPH
0.21
octanal
-
-
0.0018 - 0.011
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42
5-cyano-2,3-ditolyl tetrazolium chloride
-
-
20.8 - 50
cytochrome c
14.67 - 65
ferricytochrome c
5.83 - 56.67
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27
1,4-dioxo-2-(trifluoromethyl)-1lambda5,4lambda5-quinoxaline
pH 7.4, 25°C
-
46
1,4-dioxo-7-(trifluoromethoxy)-1lambda5,2,4lambda5-benzotriazin-3-amine
pH 7.4, 25°C
-
17
1-oxo-1lambda5,2,4-benzotriazine
pH 7.4, 25°C
-
4.7
3-amino-1,4-dioxo-1lambda5,4lambda5-quinoxaline-2-carbonitrile
pH 7.4, 25°C
-
80
methyl (1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)carbamate
pH 7.4, 25°C
-
25
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)-1,1,1-trifluoromethanesulfonamide
pH 7.4, 25°C
-
70
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)acetamide
pH 7.4, 25°C
-
2.7
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)methanesulfonamide
pH 7.4, 25°C
-
8.7
N-(1-oxo-1lambda5,2,4-benzotriazin-3-yl)acetamide
pH 7.4, 25°C
-
1500 - 10500
ferricytochrome c
2700 - 7200
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9
2-chloroethyl ethyl sulfide
Rattus norvegicus
-
in 10 mM phosphate buffer (pH 7.4), at 37°C
0.0118
Tannic acid
Rattus norvegicus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.17
R454E mutant, electron acceptor: cytochrome c
0.23
Y456S mutant, electron acceptor: cytochrome c
1.35
G488L mutant, electron acceptor: cytochrome c
1.7
W677X mutant, electron acceptor: cytochrome c
32.7
T491V mutant, electron acceptor: cytochrome c
36
W677Y mutant, electron acceptor: cytochrome c
57.4
wild type, electron acceptor: cytochrome c
62.5
S678X mutant, electron acceptor: cytochrome c
65.4
C472T mutant, electron acceptor: cytochrome c
0.0104
-
aortic microsomal preparation
0.02
-
brain
0.021
-
riboflavin-deficient animals, feeding period 7 weeks, electron acceptor: cytochrome c
0.025
-
electron donor: NADH, electron acceptor: dichlorophenolindophenol
0.03
-
electron donor: NADPH, electron acceptor: cytochrome b5
0.034
-
beta-naphthoflavone-treated animals
0.036
-
control microsomes
0.055
-
electron donor: NADH, electron acceptor: cytochrome c
0.06572
-
purified microsomal ethanol-oxidizing system fraction
0.066
-
riboflavin-deficient animals, feeding period 6 weeks, electron acceptor: cytochrome c
0.075
-
riboflavin deficient animals, feeding period 7 weeks, electron acceptor: ferricyanide
0.08572
-
microsomes
0.097
-
riboflavin-deficient-animals, feeding period 6 weeks, electron acceptor: ferricyanide
0.157
-
control animals, feeding period 6 weeks, electron acceptor: ferricyanide
0.165
-
control animals, feeding period 6 weeks, electron acceptor: cytochrome c
0.171
-
nuclear envelope
0.189
-
electron acceptor: formylated cytochrome c
0.211
-
brain, electron acceptor: hexadecanal
0.28
-
Y140D/178D double mutant, electron acceptor: cytochrome c
0.333
-
microsomes
0.44
-
Y178D mutant, electron acceptor: cytochrome c
0.58
-
peroxidation of microsomes for 18 min
0.676
-
purified enzyme, liver
0.72
-
control microsomes
0.928
-
electron acceptor: cytochrome c
11
-
Y140D mutant, electron acceptor: cytochrome c
113
-
Y178F mutant, electron acceptor: ferricyanide
16.5
-
cDNA-expressed liver enzyme
17.9
-
electron donor: NADPH, electron acceptor: dichlorophenolindophenol
37.6
-
purified enzyme
41.2
-
electron donor: NADPH, electron acceptor: cytochrome c
46
-
Y140F/178F double mutant, electron acceptor: cytochrome c
47.4
-
Y178F mutant, electron acceptor: cytochrome c
48.1
-
Y178D mutant, electron acceptor: ferricyanide
5.9
-
brain, electron acceptor: p-nitrobenzaldehyde
51
-
Y140D/178D double mutant, electron acceptor: ferricyanide
51.5
-
bacterially expressed reductase protein, electron acceptor: cytochrome c
52.9
-
electron acceptor: ferricyanide
53.3
-
electron acceptor: cytochrome c
55.2
-
Y140F mutant, electron acceptor: cytochrome c
60
-
purified enzyme, microsomes
62.5
-
purification by affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate
63.8
-
purification by n-octylamino-Sepharose 4B and 2',5'-ADP column chromatography
94.2
-
Y140F/178F double mutant, electron acceptor: ferricyanide
94.8
-
Y140F mutant, electron acceptor: ferricyanide
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.7
assay at
6.9 - 7.5
-
microsomal ethanol-oxidizing system
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
assay at
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
beta-naphtoflavone-treated animals
Manually annotated by BRENDA team
additional information
-
CPR activity in 28-day-old male offspring in only the LM76 group (low protein diet based on the modified version of the AIN76A purified diet) but not in the L93 group (low protein diet based on the AIN93G purified diet) is significantly greater than its purified control. CPR activity in 28-day-old male offspring of the M76 group is lower than that in the NP group (nonpurified diet). CPR activities in 65- and 150-day-old male offspring in all five groups are similar. CPR activities in 28-day-old female offspring of the LPD groups are similar to those of their respective purified control groups. However, CPR activities in 28-day-old female offspring in both the purified control groups are lower than that in the NP group. These differences disappeare by day 65, and the lack of differences persisted on day 150. Gender differences (activity in males greater than that in females) are present in all five groups on day 150 but not on days 28 and 65 (the 28-day-old NP group being an exception)
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug target
the cytotoxicity of heteroaromatic N-oxides in murine hepatoma MH22a and human colon carcinoma HCT-116 cells increases with the geometric average of their reactivity towards NADPH:cytochrome P-450 reductase and and Plasmodium falciparum ferredoxin:NADP+ oxidoreductase, and with their reactivity towards rat NQO1
physiological function
evolution
-
the enzyme is a member of the diflavin oxidoreductase family. They are multi-domain enzymes containing distinct FAD and FMN domains connected by a flexible hinge. The protein has evolved by fusing two ancestral genes that encode proteins related to a FMN-containing flavodoxin and a FAD-containing ferredoxin-NADP+ oxidoreductase
metabolism
-
microsomal P450 systems, overview
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NCPR_RAT
678
1
76963
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78000
78000
78000 - 79000
-
liver
80000
-
wild type, x * 80000, SDS-PAGE
85000
-
x * 85000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
domain-domain interactions, structure-activity analysis and structure comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
deletion mutants
purified mutant CYPOR with an engineered disulfide bond between the FAD and FMN domains, with or without complexed NADP+, hanging drop vapour diffusion method, mixing of 0.002 ml of 15 mg/ml protein solution with 0.002 ml of reservoir solution containing 100 mM HEPES, pH 7.2, 150 mM MgCl2, and 17% PEG 335, purified protein is treated with 2 and 20 times molar excess of FMN and NADP+, respectively, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C136A
site-directed mutagenesis
C228A
site-directed mutagenesis
C363T
site-directed mutagenesis
C445L
site-directed mutagenesis
C472T
C566A
site-directed mutagenesis, the mutant shows full catalytic activity and a 2.5fold increased Km for NADPH compared to the wild-type enzyme
E238A/E239A
hinge region connecting the FMN domain to the rest of the protein
G237/+AA/E238
hinge region connecting the FMN domain to the rest of the protein
G237/+AAAA/238
hinge region connecting the FMN domain to the rest of the protein
G488L
substitution decreases FAD binding by approximately 80% but does not affect FMN incorporation, 42fold decrease in catalytic activity compared to wild type, substitution does not affect either Km for NADPH or Km for cytochrome c, addition of FAD to the mutant results in partial restoration of catalytic activity
R454E
substitution decreases both FAD binding and FMN incorporation, suggesting interaction between the two flavin domains and/or the interconnecting region, FAD content ranged from undetectable to approximately 0.1 mol of FAD/mol of enzyme, 338fold decrease in catalytic activity compared to wild type, substitution does not affect either Km for NADPH or Km for cytochrome c, addition of FAD to the mutant resulted in partial restoration of catalytic activity
S457A/C630A/D675N
site-directed mutagenesis, catalytically inactive mutant possessing a structure almost identical to that of the wild-type
S678X
substitution does not affect FAD or FMN incorporation, substitution has no effect on the catalytic activity or kinetic properties
T236A/G237A/E238A/E239A
hinge region connecting the FMN domain to the rest of the protein
T491V
substitution decreases FAD binding by approximately 50% but does not affect FMN incorporation, 2fold decrease in catalytic activity compared to wild type, substitution does not affect either Km for NADPH or Km for cytochrome c, addition of FAD to the mutant results in full restoration of catalytic activity
W677X
substitution does not affect FAD or FMN incorporation, 34fold decrease in catalytic activity compared to wild type, substitution does not alter significantly Km for cytochrome c but decreases Km for NADPH
W677Y
substitution does not affect FAD or FMN incorporation, 2fold decrease in catalytic activity compared to wild type, substitution does not alter significantly Km for cytochrome c but decreases Km for NADPH
Y456S
substitution decreases FAD binding but did not affect FMN incorporation, 250fold decrease in catalytic activity compared to wild type, substitution increases Km for cytochrome c, addition of FAD to the mutant results in full restoration of catalytic activity
D113A
-
the mutation increases kcat approximately 2fold, but does not affect Km at the lowest ionic strength (10 mM), the mutant displays no change in catalytic efficiency compared to the wild type enzyme
E115A/E116A
-
the mutations increase kcat approximately 2fold, but does not affect Km at the lowest ionic strength (10 mM), the mutant displays a slight decrease in catalytic efficiency at higher ionic strengths due to a larger increase in Km than observed for kcat
K56Q
-
the full-length mutant enzyme is stable to spontaneopus proteolysis but possesses spectral and catzalytic properties of the wild-type flavoprotein
Y140D
-
substitution does not eliminate FMN binding but reduces cytochrome c reductase activity, Km value for cytochrome c or NADPH similar to wild type
Y140D/178D
-
substitution abolishes FMN binding and cytochrome c reductase activity
Y140F
-
substitution has no effect on FMN content or catalytic activity, Km value for cytochrome c or NADPH similar to wild type
Y140F/178F
-
substitution has no effect on FMN content or catalytic activity, slightly decreases Km for cytochrome c, NADPH Km value slightly higher than wild type
Y178D
-
substitution abolishes FMN binding and cytochrome c reductase activity, Km value for cytochrome c similar to wild type, NADPH Km value slightly higher than wild type
Y178F
-
substitution has no effect on FMN content or catalytic activity, slightly decreases Km for cytochrome c, NADPH Km value similar to wild type
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
-
diluted solutions: gradual loss of activity
50
-
40% activity remaining after 3 min
60
-
brain, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to multiple freeze-thaw cycles, FAD-depleted enzyme
-
the activity of the CPR-CYP3A4 enzyme complex in Nanodiscs gradually decreases over time
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C or -20°C, 10 mM phosphate buffer, pH 7.5, several months
-
-20°C, several weeks
-
-78°C, 30 mM potassium phosphate buffer, pH 7.7, 0.1 mM EDTA, 20% glycerol, 0.4 mM PMSF
-
0°C, some days
-
4°C or room temperature, at both low and high ionic strength, in the presence or absence of NADP, FAD-depleted enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, using Ni2+-affinity chromatography
recombinant truncated mutant from Escherichia coli strain C41(DE3) by aanion exchange and 2',5'-ADP-Sepharose
2',5'-ADP agarose affinity column chromatography and DEAE resin column chromatography
-
chromatography on 2',5'-ADP agarose
-
column chromatography on 2',5'-ADP-Sepharose, phospholipid composition relatively enriched in L-alpha-1,2-diacyl-sn-glycero-3-phosphoserine and L-alpha-1,2-diacyl-sn-glycero-3-phosphoinositol
-
column chromatography on DEAE-cellulose and 2',5'-ADP-Sepharose 4B
-
column chromatography on DEAE-cellulose and affinity chromatography on cytochrome-c-Sepharose 4B
-
column chromatography on Sephadex G-100 and DEAE-cellulose
-
DEAE-cellulose followed by sequential chromatography on Sephadex G-150, DEAE-cellulose and hydroxylapatite
-
DEAE-Sephadex gel filtration and 2',5'-ADP Sepharose 4B column chromatography
-
DEAE-Sepharose column chromatography
-
expressed in Escherichia coli
-
FAD-depleted enzyme
-
liver microsomes, column chromatography on Sephadex G-150 and hydroxylapatatite
-
Ni-NTA column chromatography
-
recombinant
-
single mutation K56Q
-
single-step procedure involving affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate or two-column procedure involving chromatography on n-octylamino-Sepharose 4B followed by chromatography on 2',5'-ADP
-
trypsin digestion followed by Sephadex filtration and column chromatography on DEAE-cellulose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene 147CC514, expression of wild-type, truncated mutant, and point mutations in Escherichia coli strain C41(DE3)
expressed in Bacillus subtilis DB104 under the transcriptional control of an IPTG-inducible fusion promoter of PgroE and Ptac. The expressed rCPR is released into the culture medium after sporulation by autolysis of the host cell. It is associated with and displayed on the spore surfaces
-
expressed in Escherichia coli C41 cells
-
expression in Escherichia coli
-
functional expression of mammalian NADPH-cytochrome P450 oxidoreductase on the cell surface of Escherichia coli
-
recombinant expression in Escherichia coli
-
wild-type and mutant K56Q, expression in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of hydroxylation of benzo-alpha-pyrene
-
riboflavin-deficient microsomes, reconstitution of activity with FAD, FMN and riboflavin
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
the enzyme is displayed on the cell surface of Escherichia coli, creating a whole-cell biocatalyst for oxidoreduction of various substrates
medicine
-
nitrofurantoin-induced redox cycling and subsequent generation of reactive oxygen intermediates are not sufficient to mediate cytotoxicity. Cytochrome P450 reductase is not a determinant of sensitivity to redox-active chemotherapeutic agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurzban, G.P.; Howarth, J.; Palmer, G.; Strobel, H.W.
NADPH-cytochrome P-450 reductase. Physical properties and redox behavior in the absence of the FAD moiety
J. Biol. Chem.
265
12272-12279
1990
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Vibet, A.; Dintinger, T.; Maboundou, J.C.; Gaillard, J.L.; Divoux, D.; Silberzahn, P.
Estrogen synthetase in the horse. Comparison of equine placental and rat liver NADPH-cytrochrome c (P-450) reductase activities
FEBS Lett.
261
31-34
1990
Equus caballus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Benveniste, I.; Lesot, A.; Hasenfratz, M.; Durst, F.
Immunochemical characterization of NADPH-cytochrome P-450 reductase from Jerusalem artichoke and other higher plants
Biochem. J.
259
847-853
1989
Saccharomyces cerevisiae, Helianthus tuberosus, Embryophyta, Locusta migratoria migratorioides, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Ardies, C.M.; Lasker, J.M.; Bloswick, B.P.; Lieber, C.S.
Purification of NADPH:cytochrome c (cytochrome P-450) reductase from hamster liver microsomes by detergent extraction and affinity chromatography
Anal. Biochem.
162
39-46
1987
Mesocricetus auratus, Rattus norvegicus
Manually annotated by BRENDA team
Takahashi, N.; Saito, T.; Goda, Y.; Tomita, K.
Characterization of microsomal NADPH-dependent aldehyde reductase from rat brain
J. Biochem.
99
513-519
1986
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Shephard, E.A.; Pike, S.F.; Rabin, B.R.; Phillips, I.R.
A rapid one-step purification of NADPH-cytochrome c (P-450) reductase from rat liver microsomes
Anal. Biochem.
129
430-433
1983
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Crankshaw, D.L.; Hetnarski, K.; Wilkinson, C.F.
Purification and characterization of NADPH--cytochrome c reductase from the midgut of the southern armyworm (Spodoptera eridania)
Biochem. J.
181
593-605
1979
Rattus norvegicus, Rattus norvegicus Sprague-Dawley, Spodoptera eridania
Manually annotated by BRENDA team
Zimmermann, J.J.; Kasper, C.B.
Immunological and biochemical characterization of nuclear envelope reduced nicotinamide adenine dinucleotide phosphate-cytochrome c oxidoreductase
Arch. Biochem. Biophys.
190
726-735
1978
Rattus norvegicus
Manually annotated by BRENDA team
Yasukochi, Y.; Masters, B.S.S.
Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography
J. Biol. Chem.
251
5337-5344
1976
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Masters, B.S.S.; Prough, R.A.; Kamin, H.
Properties of the stable aerobic and anaerobic half-reduced states of NADPH-cytochrome c reductase
Biochemistry
14
607-613
1975
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Teschke, R.; Hasumura, Y.; Lieber, C.S.
Hepatic microsomal ethanol-oxidizing system: solubilization, isolation, and characterization
Arch. Biochem. Biophys.
163
404-415
1974
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Betz, G.; Roper, M.; Tsai, P.
Steroid 17,20-lyase from testis microsomes: participation of NADPH cytochrome c reductase
Arch. Biochem. Biophys.
163
318-323
1974
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Golf, S.W.; Graef, V.; Staudinger, H.
Solubilization and purification of the NADPH-cytochrome reductase from rat liver microsomes
Hoppe-Seyler's Z. Physiol. Chem.
355
1063-1069
1974
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Omura, T.; Takesue, S.
A new method for simultaneous purification of cytochrome b5 and NADPH-cytochrome c reductase from rat liver microsomes
J. Biochem.
67
249-257
1970
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Cooper, M.B.; Craft, J.A.; Estall, M.R.; Rabin, B.R.
Asymmetric distribution of cytochrome P-450 and NADPH-cytochrome P-450 (cytochrome c) reductase in vesicles from smooth endoplasmic reticulum of rat liver
Biochem. J.
190
737-746
1980
Rattus norvegicus
Manually annotated by BRENDA team
Yasukochi, Y.; Masters, B.S.S.
Tetramer-dimer dissociation in homoglobin and the Bohr effect
J. Biol. Chem.
251
5537-5544
1976
Rattus norvegicus
Manually annotated by BRENDA team
Erecinska, M.
Cytochrome c Interaction with membranes, formylated cytochrome c1
Arch. Biochem. Biophys.
169
199-208
1975
Rattus norvegicus
Manually annotated by BRENDA team
Dialameh, G.H.
Isolation and partial purification of cytochrome-P-450 from induced rat liver
Biochem. Biophys. Res. Commun.
81
19-23
1978
Rattus norvegicus
Manually annotated by BRENDA team
Hara, T.; Taniguchi, M.
Relationship between changes in properties and contents of riboflavin derivatives of NADPH-cytochrome P-450 reductase in the liver microsomes of riboflavin-deficient rats
J. Biochem.
97
473-482
1985
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Gut, J.; Kawato, S.; Cherry, R.J.; Winterhalter, K.H.; Richter, C.
Lipid peroxidation decreases the rotational mobility of cytochrome P-450 in rat liver microsomes
Biochim. Biophys. Acta
817
217-228
1985
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Lindeskog, P.; Haaparanta, T.; Norgard, M.; Glaumann, H.; Hansson, T.; Gustafsson J.
Isolation of rat intestinal microsomes: Partial characterisation of mucosal cytochrome P-450
Arch. Biochem. Biophys.
244
492-501
1986
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Balvers, W.G.; Boersma, M.G.; Vervoort, J.; Ouwehand, A.; Rietjens, I.M.C.M.
A specific interaction between NADPH-cytochrome reductase and phosphatidylserine and phosphatidylinositol
Eur. J. Biochem.
218
1021-1029
1993
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
McGuire, J.J.; Anderson, D.J.; McDonald, B.J.; Narayanasami, R.; Bennett, B.M.
Inhibition of NADPH-Cytochrome P450 Reductase and Glyceryl Trinitrate Biotransformation by Diphenyleneiodonium Sulfate
Biochem. Pharmacol.
56
881-893
1998
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Shen, A.L.; Porter, T.D.; Wilson, T.E.; Kasper, C.B.
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis
J. Biol. Chem.
264
7584-7589
1989
Rattus norvegicus
Manually annotated by BRENDA team
Shen, A.L.; Kasper, C.B.
Differential contributions of NADPH-Cytochrome P450 oxidoreductase FAD binding site residues to flavin binding and catalysis
J. Biol. Chem.
275
41087-41091
2000
Rattus norvegicus (P00388)
Manually annotated by BRENDA team
Kutty, R.K.; Maines, M.D.
Characterization of an NADH-dependent haem-degrading system in ox heart mitochondria
Biochem. J.
246
467-474
1987
Rattus norvegicus
Manually annotated by BRENDA team
Vatsis, K.P.; Coon, M.J.
Oxidative aldehyde deformylation catalyzed by NADPH-cytochrome P450 reductase and the flavoprotein domain of neuronal nitric oxide synthase
Biochem. Biophys. Res. Commun.
337
1107-1111
2005
Rattus norvegicus
Manually annotated by BRENDA team
Bonina, T.A.; Gilep, A.A.; Estabrook, R.W.; Usanov, S.A.
Engineering of proteolytically stable NADPH-cytochrome P450 reductase
Biochemistry
70
357-365
2005
Rattus norvegicus
Manually annotated by BRENDA team
Higashimoto, Y.; Sato, H.; Sakamoto, H.; Takahashi, K.; Palmer, G.; Noguchi, M.
The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN
J. Biol. Chem.
281
31659-31667
2006
Rattus norvegicus
Manually annotated by BRENDA team
Yim, S.K.; Jung, H.C.; Pan, J.G.; Kang, H.S.; Ahn, T.; Yun, C.H.
Functional expression of mammalian NADPH-cytochrome P450 oxidoreductase on the cell surface of Escherichia coli
Protein Expr. Purif.
49
292-298
2006
Rattus norvegicus
Manually annotated by BRENDA team
Higashimoto, Y.; Sugishima, M.; Sato, H.; Sakamoto, H.; Fukuyama, K.; Palmer, G.; Noguchi, M.
Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase
Biochem. Biophys. Res. Commun.
367
852-858
2008
Rattus norvegicus (P00388)
Manually annotated by BRENDA team
Huber, W.J.; Backes, W.L.
Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase
Biochemistry
46
12212-12219
2007
Rattus norvegicus
Manually annotated by BRENDA team
Cherala, G.; Shapiro, B.H.; Dmello, A.P.
Effect of perinatal low protein diets on the ontogeny of select hepatic cytochrome p450 enzymes and cytochrome p450 reductase in the rat
Drug Metab. Dispos.
35
1057-1063
2007
Rattus norvegicus
Manually annotated by BRENDA team
Yao, H.T.; Chang, Y.W.; Lan, S.J.; Yeh, T.K.
The inhibitory effect of tannic acid on cytochrome P450 enzymes and NADPH-CYP reductase in rat and human liver microsomes
Food Chem. Toxicol.
46
645-653
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Wang, Y.; Gray, J.P.; Mishin, V.; Heck, D.E.; Laskin, D.L.; Laskin, J.D.
Role of cytochrome P450 reductase in nitrofurantoin-induced redox cycling and cytotoxicity
Free Radic. Biol. Med.
44
1169-1179
2008
Rattus norvegicus
Manually annotated by BRENDA team
Yim, S.K.; Jung, H.C.; Yun, C.H.; Pan, J.G.
Functional expression in Bacillus subtilis of mammalian NADPH-cytochrome P450 oxidoreductase and its spore-display
Protein Expr. Purif.
63
5-11
2008
Rattus norvegicus
Manually annotated by BRENDA team
Mast, N.; Liao, W.L.; Pikuleva, I.A.; Turko, I.V.
Combined use of mass spectrometry and heterologous expression for identification of membrane-interacting peptides in cytochrome P450 46A1 and NADPH-cytochrome P450 oxidoreductase
Arch. Biochem. Biophys.
483
81-89
2009
Rattus norvegicus (P00388)
Manually annotated by BRENDA team
Hall, C.N.; Keynes, R.G.; Garthwaite, J.
Cytochrome P450 oxidoreductase participates in nitric oxide consumption by rat brain
Biochem. J.
419
411-418
2009
Rattus norvegicus
Manually annotated by BRENDA team
Huber III, W.J.; Scruggs, B.A.; Backes, W.L.
C-Terminal membrane spanning region of human heme oxygenase-1 mediates a time-dependent complex formation with cytochrome P450 reductase
Biochemistry
48
190-197
2009
Rattus norvegicus
Manually annotated by BRENDA team
Kim, D.H.; Yim, S.K.; Kim, K.H.; Ahn, T.; Yun, C.H.
Continuous spectrofluorometric and spectrophotometric assays for NADPH-cytochrome P450 reductase activity using 5-cyano-2,3-ditolyl tetrazolium chloride
Biotechnol. Lett.
31
271-275
2009
Rattus norvegicus
Manually annotated by BRENDA team
Hamdane, D.; Xia, C.; Im, S.C.; Zhang, H.; Kim, J.J.; Waskell, L.
Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450
J. Biol. Chem.
284
11374-11384
2009
Rattus norvegicus (P00388)
Manually annotated by BRENDA team
Guengerich, F.P.; Martin, M.V.; Sohl, C.D.; Cheng, Q.
Measurement of cytochrome P450 and NADPH-cytochrome P450 reductase
Nat. Protoc.
4
1245-1251
2009
Rattus norvegicus
Manually annotated by BRENDA team
Inaoka, Y.; Yazawa, T.; Mizutani, T.; Kokame, K.; Kangawa, K.; Uesaka, M.; Umezawa, A.; Miyamoto, K.
Regulation of P450 oxidoreductase by gonadotropins in rat ovary and its effect on estrogen production
Reprod. Biol. Endocrinol.
6
62
2008
Rattus norvegicus (P00388), Homo sapiens (P16435), Homo sapiens
Manually annotated by BRENDA team
Grinkova, Y.V.; Denisov, I.G.; Sligar, S.G.
Functional reconstitution of monomeric CYP3A4 with multiple cytochrome P450 reductase molecules in Nanodiscs
Biochem. Biophys. Res. Commun.
398
194-198
2010
Rattus norvegicus
Manually annotated by BRENDA team
Jang, H.H.; Jamakhandi, A.P.; Sullivan, S.Z.; Yun, C.H.; Hollenberg, P.F.; Miller, G.P.
Beta sheet 2-alpha helix C loop of cytochrome P450 reductase serves as a docking site for redox partners
Biochim. Biophys. Acta
1804
1285-1293
2010
Rattus norvegicus
Manually annotated by BRENDA team
Laursen, T.; Jensen, K.; Moller, B.L.
Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450
Biochim. Biophys. Acta
1814
132-138
2011
Rattus norvegicus
Manually annotated by BRENDA team
Flueck, C.E.; Mullis, P.E.; Pandey, A.V.
Modeling of human P450 oxidoreductase structure by in silico mutagenesis and MD simulation
Mol. Cell. Endocrinol.
313
17-22
2009
Rattus norvegicus (P00388), Homo sapiens (P16435), Homo sapiens
Manually annotated by BRENDA team
Gray, J.P.; Mishin, V.; Heck, D.E.; Laskin, D.L.; Laskin, J.D.
Inhibition of NADPH cytochrome P450 reductase by the model sulfur mustard vesicant 2-chloroethyl ethyl sulfide is associated with increased production of reactive oxygen species
Toxicol. Appl. Pharmacol.
247
76-82
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Iyanagi, T.; Xia, C.; Kim, J.J.
NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family
Arch. Biochem. Biophys.
528
72-89
2012
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kenaan, C.; Zhang, H.; Shea, E.V.; Hollenberg, P.F.
Uncovering the role of hydrophobic residues in cytochrome P450-cytochrome P450 reductase interactions
Biochemistry
50
3957-3967
2011
Rattus norvegicus
Manually annotated by BRENDA team
Xia, C.; Hamdane, D.; Shen, A.L.; Choi, V.; Kasper, C.B.; Pearl, N.M.; Zhang, H.; Im, S.C.; Waskell, L.; Kim, J.J.
Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding
J. Biol. Chem.
286
16246-16260
2011
Rattus norvegicus (P00388)
Manually annotated by BRENDA team
Shinkai, Y.; Nishihara, Y.; Amamiya, M.; Wakayama, T.; Li, S.; Kikuchi, T.; Nakai, Y.; Shimojo, N.; Kumagai, Y.
NADPH-cytochrome P450 reductase-mediated denitration reaction of 2,4,6-trinitrotoluene to yield nitrite in mammals
Free Radic. Biol. Med.
91
178-187
2016
Rattus norvegicus
Manually annotated by BRENDA team
Huang, R.; Zhang, M.; Rwere, F.; Waskell, L.; Ramamoorthy, A.
Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c
J. Biol. Chem.
290
4843-4855
2015
Rattus norvegicus
Manually annotated by BRENDA team
Dai, Y.; Zhen, J.; Zhang, X.; Zhong, Y.; Liu, S.; Sun, Z.; Guo, Y.; Wu, Q.
Analysis of the complex formation, interaction and electron transfer pathway between the open conformation of NADPH-cytochrome P450 reductase and aromatase
Steroids
101
116-124
2015
Rattus norvegicus (P00388)
Manually annotated by BRENDA team
Nemeikaite-Ceniene, A.; Sarlauskas, J.; Miseviciene, L.; Maroziene, A.; Jonusiene, V.; Lesanavicius, M.; Cenas, N.
Aerobic cytotoxicity of aromatic N-oxides the role of NAD(P)H quinone oxidoreductase (NQO1)
Int. J. Mol. Sci.
21
8754
2020
Rattus norvegicus (P00388)
Manually annotated by BRENDA team
Park, H.G.; Lim, Y.R.; Han, S.; Jeong, D.; Kim, D.
Enhanced purification of recombinant rat NADPH-P450 reductase by using a hexahistidine-tag
J. Microbiol. Biotechnol.
27
983-989
2017
Rattus norvegicus (P00388)
Manually annotated by BRENDA team