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Literature summary 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 PubMedView publication on EuropePMC

General Stability

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.98.1.1 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
4.98.1.1 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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.98.1.1 40000
-
 x * 40000, SDS-PAGE Mus musculus
4.98.1.1 40000
-
 x * 40000, SDS-PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.98.1.1 Homo sapiens
-
-
-
4.98.1.1 Mus musculus
-
-
-

Oxidation Stability

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

Source Tissue

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
4.98.1.1 FeCH
-
 Mus musculus
4.98.1.1 FeCH
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.98.1.1 [2Fe-2S]-center ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis Mus musculus
4.98.1.1 [2Fe-2S]-center ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis Homo sapiens