BRENDA - Enzyme Database

Macrophage NO synthase: characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interaction

Ghosh, D.K.; Stuehr, D.J.; Biochemistry 34, 801-807 (1995)

Data extracted from this reference:

Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.13.39
Iron
protoporphyrin IX heme
Mus musculus
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.13.39
56000
-
2 * 56000, oxygenase subunit domain, SDS-PAGE
Mus musculus
1.14.13.39
74000
-
reductase subunit domain, gel filtration
Mus musculus
1.14.13.39
112000
-
oxygenase subunit domain, gel filtration
Mus musculus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.14.13.39
Mus musculus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.14.13.39
dimeric enzyme and subunits
Mus musculus
Reaction
EC Number
Reaction
Commentary
Organism
1.14.13.39
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
subunits align in head-to-head manner with oxygenase domains interacting to form a dimer and reductase domains existing as independent extensions
Mus musculus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.14.13.39
macrophage
RAW 264.7 cells
Mus musculus
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.14.13.39
1.1
-
purified enzyme
Mus musculus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.13.39
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
440225
Mus musculus
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
440225
Mus musculus
?
1.14.13.39
oxidized cytochrome c + NADPH + O2
-
440225
Mus musculus
reduced cytochrome c + NADP+ + H2O
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.14.13.39
dimer
2 * 56000, oxygenase subunit domain, SDS-PAGE
Mus musculus
1.14.13.39
monomer
1 * 74000, reductase domain, SDS-PAGE
Mus musculus
1.14.13.39
More
dimer formation, each subunit consists of: 1 oxygenase domain containing heme, tetrahydrobiopterin, substrate binding site and 1 reductase domain containing FAD, FMN, calmodulin, NADPH binding site; dimeric structure is required for enzyme activity, interaction between subunits via oxygenase domains
Mus musculus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.14.13.39
Calmodulin
required
Mus musculus
1.14.13.39
FAD
-
Mus musculus
1.14.13.39
FMN
-
Mus musculus
1.14.13.39
NADPH
-
Mus musculus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.14.13.39
Calmodulin
required
Mus musculus
1.14.13.39
FAD
-
Mus musculus
1.14.13.39
FMN
-
Mus musculus
1.14.13.39
NADPH
-
Mus musculus
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.14.13.39
Iron
protoporphyrin IX heme
Mus musculus
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.13.39
56000
-
2 * 56000, oxygenase subunit domain, SDS-PAGE
Mus musculus
1.14.13.39
74000
-
reductase subunit domain, gel filtration
Mus musculus
1.14.13.39
112000
-
oxygenase subunit domain, gel filtration
Mus musculus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.13.39
dimeric enzyme and subunits
Mus musculus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.14.13.39
macrophage
RAW 264.7 cells
Mus musculus
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.14.13.39
1.1
-
purified enzyme
Mus musculus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.13.39
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
440225
Mus musculus
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
440225
Mus musculus
?
1.14.13.39
oxidized cytochrome c + NADPH + O2
-
440225
Mus musculus
reduced cytochrome c + NADP+ + H2O
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.14.13.39
dimer
2 * 56000, oxygenase subunit domain, SDS-PAGE
Mus musculus
1.14.13.39
monomer
1 * 74000, reductase domain, SDS-PAGE
Mus musculus
1.14.13.39
More
dimer formation, each subunit consists of: 1 oxygenase domain containing heme, tetrahydrobiopterin, substrate binding site and 1 reductase domain containing FAD, FMN, calmodulin, NADPH binding site; dimeric structure is required for enzyme activity, interaction between subunits via oxygenase domains
Mus musculus