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Literature summary extracted from

  • Siddhanta, U.; Wu, C.; Abu-Soud, H.M.; Zhang, J.; Ghosh, D.K.; Stuehr, D.J.
    Heme iron reduction and catalysis by a nitric oxide synthase heterodimer containing one reductase and two oxygenase domains (1996), J. Biol. Chem., 271, 7309-7312.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.39 additional information construction of a heterodimer with one subunit being His-tagged Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Iron heme-iron Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.39 55000
-
 oxygenase subunit domain, gel filtration Mus musculus
1.14.13.39 130000
-
 2 * 130000, SDS-PAGE Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Mus musculus
-
 cytokine-inducible in macrophage
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 heterodimer 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 dimerization is required, activation of NO-synthesis by enabling electron transfer between the reductase and the oxygenase domains, isolated monomers are inactive 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 additional information
-
-
 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+ the overall reaction proceeds via 2 partial reactions: reaction 1 converts L-arginine into L-Ngamma-hydroxyarginine, reaction 2 converts L-Ngamma-hydroxyarginine into citrulline and nitric oxide Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 4 O2 + 3 H+ dimeric structure is required for enzyme activity Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.39 dimer 2 * 130000, 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 5,6,7,8-tetrahydro-L-biopterin required Mus musculus
1.14.13.39 Calmodulin required Mus musculus
1.14.13.39 FAD required Mus musculus
1.14.13.39 FMN required Mus musculus
1.14.13.39 NADPH
-
 Mus musculus