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Literature summary extracted from

  • Baek, K.J.; Thiel, B.A.; Lucas, S.; Stuehr, D.J.
    Macrophage nitric oxide synthase subunits. Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme (1993), J. Biol. Chem., 268, 21120-21129.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Iron required Mus musculus
1.14.13.39 Iron 0.9-1.2 mol heme per mol of dimer Mus musculus
1.14.13.39 Iron protoporphyrin IX heme Mus musculus
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 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 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 structure-function study of macrophage enzyme 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+ capacity to synthesize NO only through dimerization and binding of heme and tetrahydrobiopterin Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 additional information dimeric enzyme and subunits are equivalent in catalyzing electron transfer from NADPH to cytochrome c, dichlorophenolindiphenol, and ferricyanide Mus musculus ?
-
 ?
1.14.13.39 additional information D-arginine is no substrate Mus musculus ?
-
 ?
1.14.13.39 Ngamma-hydroxy-L-arginine + NADPH + O2
-
 Mus musculus citrulline + NADP+ + NO
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.39 dimer 2 * 130000, SDS-PAGE Mus musculus
1.14.13.39 More D-arginine inhibits reconstitution of dimer from subunits Mus musculus
1.14.13.39 More subunit composition of dimeric enzyme Mus musculus
1.14.13.39 More dissociation of dimer into subunits at pH 6.8 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.39 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.39 7.8
-
 assay at 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 5,6,7,8-tetrahydro-L-biopterin 0.19 mol bound per mol of dimer Mus musculus
1.14.13.39 Calmodulin required Mus musculus
1.14.13.39 FAD 0.49 mol per mol of dimer Mus musculus
1.14.13.39 FMN required Mus musculus
1.14.13.39 FMN 0.71 mol per mol of dimer Mus musculus
1.14.13.39 NADPH dependent on Mus musculus
1.14.13.39 NADPH at high concentration inhibits dimer reconstitution from subunits Mus musculus