Information on EC 1.18.1.6 - adrenodoxin-NADP+ reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.18.1.6
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RECOMMENDED NAME
GeneOntology No.
adrenodoxin-NADP+ reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced adrenodoxin + NADP+ + H+ = 2 oxidized adrenodoxin + NADPH
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
adrenodoxin:NADP+ oxidoreductase
A flavoprotein (FAD). The enzyme, which transfers electrons from NADPH to adrenodoxin molecules, is the first component of the mitochondrial cytochrome P-450 electron transfer systems, and is involved in the biosynthesis of all steroid hormones.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
diaphorase activity
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
oxidized adrenodoxin + NADH + H+
reduced adrenodoxin + NAD+
show the reaction diagram
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the enzyme has low affinity for NADH
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-
?
oxidized adrenodoxin + NADPH + H+
reduced adrenodoxin + NADP+
show the reaction diagram
reduced adrenodoxin + NADP
oxidized adrenodoxin + NADPH + H+
show the reaction diagram
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-
-
-
?
reduced ferredoxin + NAD(P)+
oxidized ferredoxin + NAD(P)H
show the reaction diagram
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-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
oxidized adrenodoxin + NADPH + H+
reduced adrenodoxin + NADP+
show the reaction diagram
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-
-
-
?
reduced ferredoxin + NAD(P)+
oxidized ferredoxin + NAD(P)H
show the reaction diagram
P9WIQ3
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
preference for NADP+
NADP+
[2Fe-2S]-center
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-
additional information
the enzyme contains a second, kinetically distinct and inhibitory pyridine nucleotide-binding site
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-ADP
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2',5'-ADP inhibits the NADPH-ferricyanide reductase activity of the enzyme competitively
5,5'-dithiobis(2-nitrobenzoate)
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NAD+, NADP+ prevent inhibition
diethyl dicarbonate
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NAD+, NADP+ prevent inhibition
additional information
the enzyme contains a second, kinetically distinct and inhibitory pyridine nucleotide-binding site
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adrenodoxin
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organized complexes consisting of adrenodoxin reductase and adrenodoxin are more active in the presence of free adrenodoxin than in its absence
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
2,6-dichlorophenolindophenol
pH 7.2, 30C
0.16
ferricyanide
pH 7.2, 30C
0.051 - 5.56
NADH
0.0012 - 0.0041
NADPH
0.000016 - 0.000017
oxidized adrenodoxin
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additional information
additional information
transient and steady-state kinetics of diaphorase and flavin reductase activities, determination of reduction potential
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
2,6-dichlorophenolindophenol
Mycobacterium tuberculosis
P9WIQ3
pH 7.2, 30C
33.7
ferricyanide
Mycobacterium tuberculosis
P9WIQ3
pH 7.2, 30C
25.6
NADH
Mycobacterium tuberculosis
P9WIQ3
flavin reduction, pH 7.2, 30C
50.6
NADPH
Mycobacterium tuberculosis
P9WIQ3
flavin reduction, pH 7.2, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
2',5'-ADP
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at 25C in 50 mM potassium phosphate, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
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tightly bound enzyme form from homogenate, at pH 7.4 and 25C
0.11
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crude extract, in potassium phosphate, pH 7.4, at 37C
1.01
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NADPH-oxidase activity at 25C
8.8
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NADPH-cytochrome c reductase acticvity
13.2
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purified enzyme, in potassium phosphate, pH 7.4, at 37C
20
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NADPH-ferricyanide reductase activity at 25C
22
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tightly bound enzyme form after 733fold purification, at pH 7.4 and 25C
22.8
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NADPH-ferricyanide reductase activity
23.05
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NADPH-ferricyanide reductase activity, purification method 1
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
additional information
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not detected in liver and testis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the enzyme associates with the inner mitochondrial membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22800
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proteolysed enzyme
39000
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gel filtration
45000
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analytical ultracentrifugation
49000
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ultracentrifugation, gel filtration, SDS-PAGE
50000
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gel filtration
51000
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sedimentation equilibrium
51400
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gel filtration
52000
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SDS-PAGE
53000
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SDS-PAGE
54000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 12% (w/v) PEG-8000 in 50 mM sodium cacodylate (pH 6.5), 100 mM calcium acetate
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 50 mm potassium phosphate buffer (pH 7.4) in the dark, at least 3 months, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adrenodoxin-Sepharose affinity column chromatography
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ammonium sulfate precipitation, adrenodoxin-Sepharose 6B column chromatography and Sephadex G-100 gel filtration
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DEAE-Fractogel column chromatography and adrenodoxin-Sepharose column chromatography
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ion exchange chromatography and 2'-5'-ADP-Sepharose column chromatography
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octylamino-Sepharose 4B column chromatography, Sephadex G- 100 gel filtration and DEAE-Biogel A column chromatography
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recombinant enzyme from Escherichia coli to homogeneity
Sephadex G-100 gel filtration and DEAE-cellulose column chromatography
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the tightly bound enzyme form is purified by sodium cholate solubilization, ammonium sulfate precipitation, DEAE-Sepharose column chromatography, 2,5-ADP-Sepharose column chromatography, and DEAE-Sepharose column chromatography. The loosely bound enzyme form is purified by ammonium sulfate precipitation, DEAE-cellulose column chromatography, 2,5-ADP-Sepharose column chromatography, and Sephadex G-25 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpressed with P450 27A1 and adrenodoxin in Escherichia coli DH5alpha cells
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expressed as a fusion protein system consisting of P45011beta, enzyme, and adrenodoxin in COS-1 cells
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli JM109 cells
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gene fprA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a SF-1 binding region is located within intron 2 of the human FDXR gene. FDXR transcription is activated through the SF-1 binding site within intron 2. Endogenous SF-1 knockdown in human adrenocortical H295R and KGN cells decreased FDXR expression. In H295R cells, strong binding of two histone markers of active enhancers, histones H3K27ac and H3K4me2, is detected near the SF-1 binding site within intron 2. The binding of these histone markers is decreased concurrent with SF-1 knockdown in H295R cells
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as compared to ovary adrenodoxin reductase concentration increases at least 50fold in corpora lutea
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