BRENDA - Enzyme Database

Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816

Haigler, B.E.; Gibson, D.T.; J. Bacteriol. 172, 457-464 (1990)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
1.14.12.12
ferricyanide
activation, direct reduction by reductaseNAP in the presence of NADH in vitro
Pseudomonas sp.
General Stability
EC Number
General Stability
Organism
1.14.12.12
purification of reductase leads to significant loss of flavin cofactor
Pseudomonas sp.
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.14.12.12
1,10-phenanthroline
10 mM, 63% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
4-chloromercuribenzoate
0.0005 mM, 94% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
iodoacetate
10 mM, 50% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
N-ethylmaleimide
2 mM, 30% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
NaN3
40 mM, 46% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.18.1.3
1,10-phenanthroline
10 mM, 30% inhibition
Pseudomonas sp.
1.18.1.3
iodoacetate
10 mM, 50% inhibition
Pseudomonas sp.
1.18.1.3
NEM
10 mM, 67% inhibition
Pseudomonas sp.
1.18.1.3
PCMB
0.0005 mM, 94% inhibition
Pseudomonas sp.
1.18.1.3
Sodium azide
40 mM, 46% inhibition
Pseudomonas sp.
1.18.1.7
iodoacetate
50% inhibition at 10 mM
Pseudomonas putida
1.18.1.7
N-ethylmaleimide
67% inhibition at 10 mM
Pseudomonas putida
1.18.1.7
o-phenanthroline
63% inhibition at 10 mM
Pseudomonas putida
1.18.1.7
p-chloromercuribenzoate
94% inhibition at 0.0005 mM
Pseudomonas putida
1.18.1.7
Sodium azide
46% inhibition at 40 mM
Pseudomonas putida
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.14.12.12
cytoplasm
-
Pseudomonas sp.
5737
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.12.12
Fe2+
component A, i.e. NADH-ferredoxinNAP reductase, of the multienzyme system is an iron-containing flavoprotein containing 1.8 g-atoms Fe2+ and 2 g-atoms sulfur
Pseudomonas sp.
1.18.1.3
Iron
iron-sulfur flavoprotein, protein contains 1.8 gatom of iron and 2.0 gatom of acid-labile sulfur
Pseudomonas sp.
1.18.1.7
Iron
the purified protein contains 1.8 g atoms of iron
Pseudomonas putida
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.12.12
additional information
-
three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP
Pseudomonas sp.
1.14.12.12
34900
-
ferredoxinNAP reductase, native PAGE
Pseudomonas sp.
1.14.12.12
36000
-
1 * 36000, ferredoxinNAP reductase, SDS-PAGE
Pseudomonas sp.
1.14.12.12
37000
-
ferredoxinNAP reductase, gel filtration
Pseudomonas sp.
1.14.12.12
37100
-
ferredoxinNAP reductase, deduced from amino acid sequence
Pseudomonas sp.
1.18.1.3
34900
-
non-denaturing PAGE
Pseudomonas sp.
1.18.1.3
36000
-
1 * 36000, SDS-PAGE
Pseudomonas sp.
1.18.1.3
37000
-
gel filtration
Pseudomonas sp.
1.18.1.7
36000
-
1 * 36000, SDS-PAGE
Pseudomonas putida
1.18.1.7
37000
-
gel filtration
Pseudomonas putida
1.18.1.7
37104
-
1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.14.12.12
naphthalene + NADH + O2
Pseudomonas sp.
three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
Pseudomonas sp.
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.14.12.12
Pseudomonas sp.
-
-
-
1.18.1.3
Pseudomonas sp.
-
; NADH-ferredoxinNAP reductase component of naphthalene dioxygenase
-
1.18.1.3
Pseudomonas sp. NCIB 9816
-
-
-
1.18.1.7
Pseudomonas putida
Q52126
-
-
1.18.1.7
Pseudomonas putida NCIB 9816
Q52126
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.14.12.12
ferredoxinNAP reductase, Blue Sepharose, DEAE-cellulose
Pseudomonas sp.
1.18.1.3
NADH-ferredoxinNAP reductase component of naphthalene dioxygenase
Pseudomonas sp.
1.18.1.7
Sepharose CL-6B column chromatography and DEAE-cellulose column chromatography
Pseudomonas putida
Reaction
EC Number
Reaction
Commentary
Organism
1.14.12.12
naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
proposed electron transport chain: NADH, ferredoxixinNAP reductase, ferredoxinNAP, terminal oxygenase ISPNAP
Pseudomonas sp.
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.14.12.12
397
-
cytochrome c reduction by ferredoxinNAP reductase
Pseudomonas sp.
1.18.1.3
397
-
-
Pseudomonas sp.
1.18.1.7
397
-
purified enzyme, pH and temperature not specified in the publication
Pseudomonas putida
Storage Stability
EC Number
Storage Stability
Organism
1.14.12.12
-20°C, ferredoxinNAP reductase, 1 month, minimal loss of activity, prolonged storage leads to precipitation when preparation is heated above 5°C
Pseudomonas sp.
1.14.12.12
0-5°C, ferredoxinNAP reductase, 5 days, 30% loss of activity
Pseudomonas sp.
1.18.1.3
-20°C, 1 month, minimal loss of activity
Pseudomonas sp.
1.18.1.3
0-5°C, 30% loss of activity after 5 days
Pseudomonas sp.
1.18.1.7
-20°C, purified enzyme, 1 month, minimal loss of activity
Pseudomonas putida
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.12.12
naphthalene + NADH + O2
3 component enzyme system consisting of ferredoxinNAP reductase, ferredoxinNAP and oxygenase ISPNAP, ferredoxinNAP reductase reduces: 2,6-dichlorophenolindophenol, ferricyanide, nitro blue tetrazolium and cytochrome c, in the presence of FAD ferredoxinNAP reductase transfers electrons to ferredoxin
437842
Pseudomonas sp.
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
437842
Pseudomonas sp.
?
1.14.12.12
naphthalene + NADH + O2
three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase
437842
Pseudomonas sp.
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
437842
Pseudomonas sp.
-
1.18.1.3
2 ferricyanide + NADH
-
437842
Pseudomonas sp.
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.3
2 ferricyanide + NADH
-
437842
Pseudomonas sp. NCIB 9816
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.3
2 ferricytochrome c + NADH
-
437842
Pseudomonas sp.
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.3
2 ferricytochrome c + NADH
-
437842
Pseudomonas sp. NCIB 9816
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.3
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
437842
Pseudomonas sp.
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.3
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
437842
Pseudomonas sp. NCIB 9816
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.3
NADH + oxidized nitro blue tetrazolium + H+
-
437842
Pseudomonas sp.
NAD+ + reduced nitro blue tetrazolium
-
-
-
?
1.18.1.3
NADH + oxidized nitro blue tetrazolium + H+
-
437842
Pseudomonas sp. NCIB 9816
NAD+ + reduced nitro blue tetrazolium
-
-
-
?
1.18.1.3
NADPH + oxidized cytochrome c
39% of the activity with NADH
437842
Pseudomonas sp.
NADP+ + reduced cytochrome c
-
-
-
?
1.18.1.3
NADPH + oxidized cytochrome c
39% of the activity with NADH
437842
Pseudomonas sp. NCIB 9816
NADP+ + reduced cytochrome c
-
-
-
?
1.18.1.7
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.7
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida NCIB 9816
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.7
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.7
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida NCIB 9816
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.7
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.7
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida NCIB 9816
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.7
oxidized cytochrome c + NADPH
NADPH is also effective as an electron donor but yields only 39% of the activity obtained with NADH in the cytochrome c reductase assay
437842
Pseudomonas putida
reduced cytochrome c + NADP+ + H+
-
-
-
?
1.18.1.7
oxidized cytochrome c + NADPH
NADPH is also effective as an electron donor but yields only 39% of the activity obtained with NADH in the cytochrome c reductase assay
437842
Pseudomonas putida NCIB 9816
reduced cytochrome c + NADP+ + H+
-
-
-
?
1.18.1.7
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
1.18.1.7
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida NCIB 9816
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.14.12.12
monomer
1 * 36000, ferredoxinNAP reductase, SDS-PAGE
Pseudomonas sp.
1.18.1.3
monomer
1 * 36000, SDS-PAGE
Pseudomonas sp.
1.18.1.7
monomer
1 * 36000, SDS-PAGE; 1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.14.12.12
25
-
room temperature, ferredoxinNAP reductase, t1/2: 8 h
Pseudomonas sp.
1.18.1.3
0.5
-
5 d, 30% loss of activity
Pseudomonas sp.
1.18.1.3
21
-
room temperature, 8 h, 50% loss of activity
Pseudomonas sp.
1.18.1.7
-
20
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
Pseudomonas putida
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.14.12.12
additional information
-
ferredoxin reductaseNAP, pI: 6.3
Pseudomonas sp.
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.14.12.12
FAD
1 mol FAD/mol enzyme in flavin-reconstituted protein; addition enhances ferredoxinNAP reductase activity with all in vitro electron-acceptors, e.g. cytochrome c, 2,6-dichlorophenolindophenol, Nitroblue tetrazolium and ferricyanide; component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD
Pseudomonas sp.
1.14.12.12
FMN
requirement, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD, addition stimulates dioxygenase activity by 53% of FAD-stimulation
Pseudomonas sp.
1.14.12.12
NADH
-
Pseudomonas sp.
1.14.12.12
NADPH
can replace NADH with 39%; ferredoxinNAP reductase
Pseudomonas sp.
1.18.1.3
FAD
1 mol of FAD is bound per mol of enzyme
Pseudomonas sp.
1.18.1.3
NADH
-
Pseudomonas sp.
1.18.1.3
NADPH
39% of the activity with NADH in the reaction with cytochrome c
Pseudomonas sp.
1.18.1.7
FAD
the enzyme binds 1 mol of FAD per mol of enzyme protein
Pseudomonas putida
1.18.1.7
NADH
-
Pseudomonas putida
pI Value
EC Number
Organism
Commentary
pI Value Maximum
pI Value
1.18.1.7
Pseudomonas putida
calculated from amino acid sequence
-
6.3
IC50 Value
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
1.18.1.7
10
-
pH and temperature not specified in the publication
Pseudomonas putida
iodoacetate
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
1.14.12.12
ferricyanide
activation, direct reduction by reductaseNAP in the presence of NADH in vitro
Pseudomonas sp.
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.14.12.12
FAD
1 mol FAD/mol enzyme in flavin-reconstituted protein; addition enhances ferredoxinNAP reductase activity with all in vitro electron-acceptors, e.g. cytochrome c, 2,6-dichlorophenolindophenol, Nitroblue tetrazolium and ferricyanide; component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD
Pseudomonas sp.
1.14.12.12
FMN
requirement, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD, addition stimulates dioxygenase activity by 53% of FAD-stimulation
Pseudomonas sp.
1.14.12.12
NADH
-
Pseudomonas sp.
1.14.12.12
NADPH
can replace NADH with 39%; ferredoxinNAP reductase
Pseudomonas sp.
1.18.1.3
FAD
1 mol of FAD is bound per mol of enzyme
Pseudomonas sp.
1.18.1.3
NADH
-
Pseudomonas sp.
1.18.1.3
NADPH
39% of the activity with NADH in the reaction with cytochrome c
Pseudomonas sp.
1.18.1.7
FAD
the enzyme binds 1 mol of FAD per mol of enzyme protein
Pseudomonas putida
1.18.1.7
NADH
-
Pseudomonas putida
General Stability (protein specific)
EC Number
General Stability
Organism
1.14.12.12
purification of reductase leads to significant loss of flavin cofactor
Pseudomonas sp.
IC50 Value (protein specific)
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
1.18.1.7
10
-
pH and temperature not specified in the publication
Pseudomonas putida
iodoacetate
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.14.12.12
1,10-phenanthroline
10 mM, 63% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
4-chloromercuribenzoate
0.0005 mM, 94% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
iodoacetate
10 mM, 50% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
N-ethylmaleimide
2 mM, 30% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.14.12.12
NaN3
40 mM, 46% inhibition of ferredoxinNAP reductase
Pseudomonas sp.
1.18.1.3
1,10-phenanthroline
10 mM, 30% inhibition
Pseudomonas sp.
1.18.1.3
iodoacetate
10 mM, 50% inhibition
Pseudomonas sp.
1.18.1.3
NEM
10 mM, 67% inhibition
Pseudomonas sp.
1.18.1.3
PCMB
0.0005 mM, 94% inhibition
Pseudomonas sp.
1.18.1.3
Sodium azide
40 mM, 46% inhibition
Pseudomonas sp.
1.18.1.7
iodoacetate
50% inhibition at 10 mM
Pseudomonas putida
1.18.1.7
N-ethylmaleimide
67% inhibition at 10 mM
Pseudomonas putida
1.18.1.7
o-phenanthroline
63% inhibition at 10 mM
Pseudomonas putida
1.18.1.7
p-chloromercuribenzoate
94% inhibition at 0.0005 mM
Pseudomonas putida
1.18.1.7
Sodium azide
46% inhibition at 40 mM
Pseudomonas putida
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.14.12.12
cytoplasm
-
Pseudomonas sp.
5737
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.12.12
Fe2+
component A, i.e. NADH-ferredoxinNAP reductase, of the multienzyme system is an iron-containing flavoprotein containing 1.8 g-atoms Fe2+ and 2 g-atoms sulfur
Pseudomonas sp.
1.18.1.3
Iron
iron-sulfur flavoprotein, protein contains 1.8 gatom of iron and 2.0 gatom of acid-labile sulfur
Pseudomonas sp.
1.18.1.7
Iron
the purified protein contains 1.8 g atoms of iron
Pseudomonas putida
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.12.12
additional information
-
three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP
Pseudomonas sp.
1.14.12.12
34900
-
ferredoxinNAP reductase, native PAGE
Pseudomonas sp.
1.14.12.12
36000
-
1 * 36000, ferredoxinNAP reductase, SDS-PAGE
Pseudomonas sp.
1.14.12.12
37000
-
ferredoxinNAP reductase, gel filtration
Pseudomonas sp.
1.14.12.12
37100
-
ferredoxinNAP reductase, deduced from amino acid sequence
Pseudomonas sp.
1.18.1.3
34900
-
non-denaturing PAGE
Pseudomonas sp.
1.18.1.3
36000
-
1 * 36000, SDS-PAGE
Pseudomonas sp.
1.18.1.3
37000
-
gel filtration
Pseudomonas sp.
1.18.1.7
36000
-
1 * 36000, SDS-PAGE
Pseudomonas putida
1.18.1.7
37000
-
gel filtration
Pseudomonas putida
1.18.1.7
37104
-
1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.14.12.12
naphthalene + NADH + O2
Pseudomonas sp.
three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
Pseudomonas sp.
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.12.12
ferredoxinNAP reductase, Blue Sepharose, DEAE-cellulose
Pseudomonas sp.
1.18.1.3
NADH-ferredoxinNAP reductase component of naphthalene dioxygenase
Pseudomonas sp.
1.18.1.7
Sepharose CL-6B column chromatography and DEAE-cellulose column chromatography
Pseudomonas putida
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.14.12.12
397
-
cytochrome c reduction by ferredoxinNAP reductase
Pseudomonas sp.
1.18.1.3
397
-
-
Pseudomonas sp.
1.18.1.7
397
-
purified enzyme, pH and temperature not specified in the publication
Pseudomonas putida
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
1.14.12.12
-20°C, ferredoxinNAP reductase, 1 month, minimal loss of activity, prolonged storage leads to precipitation when preparation is heated above 5°C
Pseudomonas sp.
1.14.12.12
0-5°C, ferredoxinNAP reductase, 5 days, 30% loss of activity
Pseudomonas sp.
1.18.1.3
-20°C, 1 month, minimal loss of activity
Pseudomonas sp.
1.18.1.3
0-5°C, 30% loss of activity after 5 days
Pseudomonas sp.
1.18.1.7
-20°C, purified enzyme, 1 month, minimal loss of activity
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.12.12
naphthalene + NADH + O2
3 component enzyme system consisting of ferredoxinNAP reductase, ferredoxinNAP and oxygenase ISPNAP, ferredoxinNAP reductase reduces: 2,6-dichlorophenolindophenol, ferricyanide, nitro blue tetrazolium and cytochrome c, in the presence of FAD ferredoxinNAP reductase transfers electrons to ferredoxin
437842
Pseudomonas sp.
cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
437842
Pseudomonas sp.
?
1.14.12.12
naphthalene + NADH + O2
three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase
437842
Pseudomonas sp.
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
437842
Pseudomonas sp.
-
1.18.1.3
2 ferricyanide + NADH
-
437842
Pseudomonas sp.
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.3
2 ferricyanide + NADH
-
437842
Pseudomonas sp. NCIB 9816
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.3
2 ferricytochrome c + NADH
-
437842
Pseudomonas sp.
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.3
2 ferricytochrome c + NADH
-
437842
Pseudomonas sp. NCIB 9816
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.3
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
437842
Pseudomonas sp.
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.3
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
437842
Pseudomonas sp. NCIB 9816
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.3
NADH + oxidized nitro blue tetrazolium + H+
-
437842
Pseudomonas sp.
NAD+ + reduced nitro blue tetrazolium
-
-
-
?
1.18.1.3
NADH + oxidized nitro blue tetrazolium + H+
-
437842
Pseudomonas sp. NCIB 9816
NAD+ + reduced nitro blue tetrazolium
-
-
-
?
1.18.1.3
NADPH + oxidized cytochrome c
39% of the activity with NADH
437842
Pseudomonas sp.
NADP+ + reduced cytochrome c
-
-
-
?
1.18.1.3
NADPH + oxidized cytochrome c
39% of the activity with NADH
437842
Pseudomonas sp. NCIB 9816
NADP+ + reduced cytochrome c
-
-
-
?
1.18.1.7
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.7
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida NCIB 9816
2 ferrocyanide + NAD+ + H+
-
-
-
?
1.18.1.7
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.7
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida NCIB 9816
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
1.18.1.7
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.7
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida NCIB 9816
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.18.1.7
oxidized cytochrome c + NADPH
NADPH is also effective as an electron donor but yields only 39% of the activity obtained with NADH in the cytochrome c reductase assay
437842
Pseudomonas putida
reduced cytochrome c + NADP+ + H+
-
-
-
?
1.18.1.7
oxidized cytochrome c + NADPH
NADPH is also effective as an electron donor but yields only 39% of the activity obtained with NADH in the cytochrome c reductase assay
437842
Pseudomonas putida NCIB 9816
reduced cytochrome c + NADP+ + H+
-
-
-
?
1.18.1.7
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
1.18.1.7
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida NCIB 9816
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.14.12.12
monomer
1 * 36000, ferredoxinNAP reductase, SDS-PAGE
Pseudomonas sp.
1.18.1.3
monomer
1 * 36000, SDS-PAGE
Pseudomonas sp.
1.18.1.7
monomer
1 * 36000, SDS-PAGE; 1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.14.12.12
25
-
room temperature, ferredoxinNAP reductase, t1/2: 8 h
Pseudomonas sp.
1.18.1.3
0.5
-
5 d, 30% loss of activity
Pseudomonas sp.
1.18.1.3
21
-
room temperature, 8 h, 50% loss of activity
Pseudomonas sp.
1.18.1.7
-
20
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
Pseudomonas putida
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.14.12.12
additional information
-
ferredoxin reductaseNAP, pI: 6.3
Pseudomonas sp.
pI Value (protein specific)
EC Number
Organism
Commentary
pI Value Maximum
pI Value
1.18.1.7
Pseudomonas putida
calculated from amino acid sequence
-
6.3