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Literature summary for 1.14.13.39 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
Search for more literature for 1.14.13.39

Protein Variants

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
heterodimer 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 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

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
additional information
-
-
 Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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

Subunits Comment Organism
dimer 2 * 130000, SDS-PAGE Mus musculus
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
More dimeric structure is required for enzyme activity, interaction between subunits via oxygenase domains Mus musculus

Cofactor

Cofactor Comment Organism Structure
5,6,7,8-tetrahydro-L-biopterin required Mus musculus
Calmodulin required Mus musculus
FAD required Mus musculus
FMN required Mus musculus
NADPH
-
 Mus musculus