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Literature summary for 4.98.1.1 extracted from

  • Crooks, D.; Ghosh, M.; Haller, R.; Tong, W.; Rouault, T.
    Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery (2010), Blood, 115, 860-869.
    View publication on PubMed
Search for more literature for 4.98.1.1

General Stability

General Stability Organism
ferrochelatase shows a calculated half-life of approximately 35 h in vivo Homo sapiens
ferrochelatase shows a calculated half-life of approximately 35 h in vivo Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability. Decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apoferrochelatase Homo sapiens
Fe2+ the posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability. Decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apoferrochelatase Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 x * 40000, SDS-PAGE Mus musculus
40000
-
 x * 40000, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-

Oxidation Stability

Oxidation Stability Organism
FECH is destabilized by oxygen and mitochondrial oxidative stress Homo sapiens
FECH is destabilized by oxygen and mitochondrial oxidative stress Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
erythroblast splenic erythroblast Mus musculus
-
erythroleukemia cell
-
 Mus musculus
-
muscle
-
 Homo sapiens
-
myoblast
-
 Homo sapiens
-
spleen
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deuteroporphyrin IX + Zn2+
-
 Homo sapiens Zn-deuteroporphyrin IX + H+
-
 ?
deuteroporphyrin IX + Zn2+
-
 Mus musculus Zn-deuteroporphyrin IX + H+
-
 ?

Subunits

Subunits Comment Organism
? x * 40000, SDS-PAGE Homo sapiens
? x * 40000, SDS-PAGE Mus musculus

Synonyms

Synonyms Comment Organism
FeCH
-
 Homo sapiens
FeCH
-
 Mus musculus

Cofactor

Cofactor Comment Organism Structure
[2Fe-2S]-center ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis Homo sapiens
[2Fe-2S]-center ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis Mus musculus