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Literature summary for 4.98.1.1 extracted from

  • Dailey, H.A.
    Purification and characterization of membrane-bound ferrochelatase from Rhodopseudomonas sphaeroides (1982), J. Biol. Chem., 257, 14714-14718.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Cereibacter sphaeroides
hemin
-
Cereibacter sphaeroides
Hg2+
-
Cereibacter sphaeroides
iodoacetamide
-
Cereibacter sphaeroides
N-ethylmaleimide
-
Cereibacter sphaeroides
Pb2+
-
Cereibacter sphaeroides

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Cereibacter sphaeroides 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ inhibition Cereibacter sphaeroides

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
115000
-
1 * 115000, SDS-PAGE, gel filtration in presence of sodium deoxycholate Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Cereibacter sphaeroides

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6
-
-
Cereibacter sphaeroides

Storage Stability

Storage Stability Organism
membrane-bound enzyme stable to freezing for months, storage at 4°C for at least several weeks, solubilized enzyme labile Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrin + Fe2+
-
Cereibacter sphaeroides protoheme + 2 H+
-
?

Subunits

Subunits Comment Organism
? 1 * 115000, SDS-PAGE, gel filtration in presence of sodium deoxycholate Cereibacter sphaeroides