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

BRENDA support

Literature summary 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

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment 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 UniProt Comment Textmining
1.14.13.39 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 dimeric enzyme and subunits Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
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
a

Source Tissue

EC Number Source Tissue Comment 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] Comment Organism
1.14.13.39 1.1
-
 purified enzyme Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.39 2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
 Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 oxidized cytochrome c + NADPH + O2
-
 Mus musculus reduced cytochrome c + NADP+ + H2O
-
 ?

Subunits

EC Number Subunits Comment 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 Mus musculus
1.14.13.39 More dimeric structure is required for enzyme activity, interaction between subunits via oxygenase domains Mus musculus

Cofactor

EC Number Cofactor Comment 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