BRENDA - Enzyme Database
show all sequences of 1.18.1.7

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:

Inhibitors
Inhibitors
Commentary
Organism
Structure
iodoacetate
50% inhibition at 10 mM
Pseudomonas putida
N-ethylmaleimide
67% inhibition at 10 mM
Pseudomonas putida
o-phenanthroline
63% inhibition at 10 mM
Pseudomonas putida
p-chloromercuribenzoate
94% inhibition at 0.0005 mM
Pseudomonas putida
Sodium azide
46% inhibition at 40 mM
Pseudomonas putida
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
the purified protein contains 1.8 g atoms of iron
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
1 * 36000, SDS-PAGE
Pseudomonas putida
37000
-
gel filtration
Pseudomonas putida
37104
-
1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
Q52126
-
-
Pseudomonas putida NCIB 9816
Q52126
-
-
Purification (Commentary)
Commentary
Organism
Sepharose CL-6B column chromatography and DEAE-cellulose column chromatography
Pseudomonas putida
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
397
-
purified enzyme, pH and temperature not specified in the publication
Pseudomonas putida
Storage Stability
Storage Stability
Organism
-20°C, purified enzyme, 1 month, minimal loss of activity
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida NCIB 9816
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida NCIB 9816
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida NCIB 9816
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida NCIB 9816
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 36000, SDS-PAGE; 1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-
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
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
the enzyme binds 1 mol of FAD per mol of enzyme protein
Pseudomonas putida
NADH
-
Pseudomonas putida
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Pseudomonas putida
calculated from amino acid sequence
-
6.3
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
10
-
pH and temperature not specified in the publication
Pseudomonas putida
iodoacetate
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
the enzyme binds 1 mol of FAD per mol of enzyme protein
Pseudomonas putida
NADH
-
Pseudomonas putida
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
10
-
pH and temperature not specified in the publication
Pseudomonas putida
iodoacetate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
iodoacetate
50% inhibition at 10 mM
Pseudomonas putida
N-ethylmaleimide
67% inhibition at 10 mM
Pseudomonas putida
o-phenanthroline
63% inhibition at 10 mM
Pseudomonas putida
p-chloromercuribenzoate
94% inhibition at 0.0005 mM
Pseudomonas putida
Sodium azide
46% inhibition at 40 mM
Pseudomonas putida
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
the purified protein contains 1.8 g atoms of iron
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
1 * 36000, SDS-PAGE
Pseudomonas putida
37000
-
gel filtration
Pseudomonas putida
37104
-
1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Purification (Commentary) (protein specific)
Commentary
Organism
Sepharose CL-6B column chromatography and DEAE-cellulose column chromatography
Pseudomonas putida
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
397
-
purified enzyme, pH and temperature not specified in the publication
Pseudomonas putida
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, purified enzyme, 1 month, minimal loss of activity
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADH
best substrate
437842
Pseudomonas putida NCIB 9816
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
2 ferricytochrome c + NADH
-
437842
Pseudomonas putida NCIB 9816
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
-
437842
Pseudomonas putida NCIB 9816
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
oxidized Nitro Blue tetrazolium + NADH
-
437842
Pseudomonas putida NCIB 9816
reduced Nitro Blue tetrazolium + NAD+ + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 36000, SDS-PAGE; 1 * 37104, calculated from amino acid sequence
Pseudomonas putida
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-
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
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Pseudomonas putida
calculated from amino acid sequence
-
6.3
Other publictions for EC 1.18.1.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745688
Peng
Metabolic engineering of Arab ...
Pseudomonas putida, Pseudomonas putida G7
Metab. Eng.
26
100-110
2014
-
-
1
-
-
-
-
-
-
-
-
2
-
11
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
722507
Zhou
Salicylate 5-hydroxylase from ...
Ralstonia sp., Ralstonia sp. U2
J. Bacteriol.
184
1547-1555
2002
-
-
1
-
-
-
-
-
-
-
-
4
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
437842
Haigler
Purification and properties of ...
Pseudomonas putida, Pseudomonas putida NCIB 9816
J. Bacteriol.
172
457-464
1990
-
-
-
-
-
-
5
-
-
1
3
-
-
3
-
-
1
-
-
-
1
1
10
1
-
-
1
-
-
-
-
2
-
1
1
-
-
-
2
-
-
-
1
5
-
-
-
1
3
-
-
-
-
1
-
-
1
1
10
1
-
-
1
-
-
-
-
1
-
-
-
-
-
-
722477
Haigler
Purification and properties of ...
Pseudomonas putida, Pseudomonas putida NCIB 9816
J. Bacteriol.
172
465-468
1990
-
-
-
-
-
-
-
-
-
1
1
-
-
3
-
-
1
-
-
-
4
-
4
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
4
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-