Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.39 extracted from

  • Ghosh, D.K.; Stuehr, D.J.
    Macrophage NO synthase: characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interaction (1995), Biochemistry, 34, 801-807.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron protoporphyrin IX heme Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
2 * 56000, oxygenase subunit domain, SDS-PAGE Mus musculus
74000
-
reductase subunit domain, gel filtration Mus musculus
112000
-
oxygenase subunit domain, gel filtration Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
dimeric enzyme and subunits Mus musculus

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
macrophage RAW 264.7 cells Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1
-
purified enzyme Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
oxidized cytochrome c + NADPH + O2
-
Mus musculus reduced cytochrome c + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
dimer 2 * 56000, oxygenase subunit domain, SDS-PAGE Mus musculus
monomer 1 * 74000, reductase domain, SDS-PAGE Mus musculus
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 Mus musculus
More dimeric structure is required for enzyme activity, interaction between subunits via oxygenase domains Mus musculus

Cofactor

Cofactor Comment Organism Structure
Calmodulin required Mus musculus
FAD
-
Mus musculus
FMN
-
Mus musculus
NADPH
-
Mus musculus