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Literature summary for 1.13.11.19 extracted from

  • Nozaki, M.
    Nonheme iron dioxygenase (1974), Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York, , 135-165.
No PubMed abstract available
Search for more literature for 1.13.11.19

Activating Compound

Activating Compound Comment Organism Structure
hydroxylamine cofactor-like compound Equus caballus
hydroxylamine sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine) Equus caballus
Se cofactor-like compound Equus caballus
Se sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine) Equus caballus
Sulfide cofactor-like compound Equus caballus
Sulfide sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine) Equus caballus
sulfur cofactor-like compound Equus caballus
sulfur sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine) Equus caballus

Inhibitors

Inhibitors Comment Organism Structure
S sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine) Equus caballus
Se sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine) Equus caballus
Sulfide sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine) Equus caballus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe a non-heme-iron protein, contains 1 g-atom of iron per mol of enzyme (based on a MW of 83000), nearly all of the iron is in the ferric state Equus caballus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 2 * 50000 SDS-PAGE Equus caballus
100000
-
 method not mentioned Equus caballus

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Equus caballus

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Equus caballus
-

Storage Stability

Storage Stability Organism
0°C, 70% saturated ammonium sulfate, stable for months Equus caballus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cysteamine + O2
-
 Equus caballus hypotaurine
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 50000 SDS-PAGE Equus caballus