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Literature summary for 1.14.13.39 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
Search for more literature for 1.14.13.39

Metals/Ions

Metals/Ions Comment Organism Structure
Iron required Mus musculus
Iron 0.9-1.2 mol heme per mol of dimer Mus musculus
Iron protoporphyrin IX heme Mus musculus
Iron heme-iron Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
 2 * 130000, SDS-PAGE Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
 cytokine-inducible in macrophage
-

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 structure-function study of macrophage enzyme Mus musculus
a

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+ capacity to synthesize NO only through dimerization and binding of heme and tetrahydrobiopterin Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
 ?
additional information dimeric enzyme and subunits are equivalent in catalyzing electron transfer from NADPH to cytochrome c, dichlorophenolindiphenol, and ferricyanide Mus musculus ?
-
 ?
additional information D-arginine is no substrate Mus musculus ?
-
 ?
Ngamma-hydroxy-L-arginine + NADPH + O2
-
 Mus musculus citrulline + NADP+ + NO
-
 ?

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Mus musculus

Cofactor

Cofactor Comment Organism Structure
5,6,7,8-tetrahydro-L-biopterin required Mus musculus
5,6,7,8-tetrahydro-L-biopterin 0.19 mol bound per mol of dimer Mus musculus
Calmodulin required Mus musculus
FAD 0.49 mol per mol of dimer Mus musculus
FMN required Mus musculus
FMN 0.71 mol per mol of dimer Mus musculus
NADPH dependent on Mus musculus
NADPH at high concentration inhibits dimer reconstitution from subunits Mus musculus