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Literature summary extracted from

  • Abu-Soud, H.M.; Loftus, M.; Stuehr, D.J.
    Subunit dissociation and unfolding of macrophage NO synthase: relationship between enzyme structure, prosthetic group binding, and catalytic function (1995), Biochemistry, 34, 11167-11175.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.39 dithiothreitol
-
 Mus musculus
1.14.13.39 interferon gamma activates Mus musculus
1.14.13.39 lipopolysaccharide from Escherichia coli, activates Mus musculus

General Stability

EC Number General Stability Organism
1.14.13.39 bovine serum albumin stabilizes during refolding Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Iron protoporphyrin IX heme Mus musculus
1.14.13.39 Iron 0.83 mol per mol of subunit 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
1.14.13.39 from interferon-gamma- and lipopolysaccharide-activated macrophage 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 relation between structure, function and binding of prosthetic groups during dissociation, unfolding and renaturation Mus musculus
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.14.13.39 refolding after treatment/equilibration with 5 M urea in presence of L-arginine and tetrahydrobiopterin Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.39 macrophage RAW 264.7 cells 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
-
 ?

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

Synonyms

EC Number Synonyms Comment Organism
1.14.13.39 i-NOS isoform II, inducible 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 0.04 mol per mol of subunit Mus musculus
1.14.13.39 FAD
-
 Mus musculus
1.14.13.39 FMN
-
 Mus musculus
1.14.13.39 NADPH
-
 Mus musculus