Information on EC 1.18.1.7 - ferredoxin-NAD(P)+ reductase (naphthalene dioxygenase ferredoxin-specific)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.18.1.7
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RECOMMENDED NAME
GeneOntology No.
ferredoxin-NAD(P)+ reductase (naphthalene dioxygenase ferredoxin-specific)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 reduced [2Fe-2S] ferredoxin + NAD(P)+ + H+ = 2 oxidized [2Fe-2S] ferredoxin + NAD(P)H
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NAD(P)+ oxidoreductase
The enzyme from the aerobic bacterium Ralstonia sp. U2 donates electrons to both EC 1.14.12.12, naphthalene 1,2-dioxygenase and EC 1.14.13.172, salicylate 5-hydroxylase [1]. The enzyme from Pseudomonas NCIB 9816 is specific for the ferredoxin associated with naphthalene dioxygenase; it contains FAD and a [2Fe-2S] cluster.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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 + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
oxidized cytochrome c + NADPH
reduced cytochrome c + NADP+ + H+
show the reaction diagram
oxidized Nitro Blue tetrazolium + NADH
reduced Nitro Blue tetrazolium + NAD+ + H+
show the reaction diagram
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
show the reaction diagram
reduced [2Fe-2S] ferredoxin + NADP+ + H+
oxidized [2Fe-2S] ferredoxin + NADPH
show the reaction diagram
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
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
show the reaction diagram
reduced [2Fe-2S] ferredoxin + NADP+ + H+
oxidized [2Fe-2S] ferredoxin + NADPH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetate
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50% inhibition at 10 mM
N-ethylmaleimide
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67% inhibition at 10 mM
o-phenanthroline
-
63% inhibition at 10 mM
p-chloromercuribenzoate
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94% inhibition at 0.0005 mM
Sodium azide
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46% inhibition at 40 mM
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
iodoacetate
Pseudomonas putida
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pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.52
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purified enzyme, in the absence of FAD and with NADPH as cosubstrate, pH and temperature not specified in the publication
13.2
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purified enzyme, in the absence of FAD and with NADH as cosubstrate, pH and temperature not specified in the publication
36.7
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purified enzyme, in the presence of FAD and NADPH, pH and temperature not specified in the publication
71
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purified enzyme, in the presence of FAD and NADH, pH and temperature not specified in the publication
397
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purified enzyme, pH and temperature not specified in the publication
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
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calculated from amino acid sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13600
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x * 13600, SDS-PAGE
36000
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1 * 36000, SDS-PAGE
37000
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gel filtration
37104
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1 * 37104, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 20
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the purified enzyme is unstable at room temperature. It loses 50% of its cytochrome c reductase activity within the first 8 h. At 0 to 5°C, the purified enzyme retains 70% of its cytochrome c reductase activity after 5 days
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, 1 month, minimal loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Blue Sepharose column chromatography, DEAE-cellulose column chromatography, and Sephadex G-75 gel filtration
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Sepharose CL-6B column chromatography and DEAE-cellulose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B L21(DE3)/pLysS cells