BRENDA - Enzyme Database

Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery

Crooks, D.; Ghosh, M.; Haller, R.; Tong, W.; Rouault, T.; Blood 115, 860-869 (2010)

Data extracted from this reference:

General Stability
EC Number
General Stability
Organism
4.99.1.1
ferrochelatase shows a calculated half-life of approximately 35 h in vivo
Mus musculus
4.99.1.1
ferrochelatase shows a calculated half-life of approximately 35 h in vivo
Homo sapiens
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.99.1.1
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
4.99.1.1
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
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.99.1.1
40000
-
x * 40000, SDS-PAGE
Homo sapiens
4.99.1.1
40000
-
x * 40000, SDS-PAGE
Mus musculus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.99.1.1
Homo sapiens
-
-
-
4.99.1.1
Mus musculus
-
-
-
Oxidation Stability
EC Number
Oxidation Stability
Organism
4.99.1.1
FECH is destabilized by oxygen and mitochondrial oxidative stress
Mus musculus
4.99.1.1
FECH is destabilized by oxygen and mitochondrial oxidative stress
Homo sapiens
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
4.99.1.1
erythroblast
splenic erythroblast
Mus musculus
-
4.99.1.1
erythroleukemia cell
-
Mus musculus
-
4.99.1.1
muscle
-
Homo sapiens
-
4.99.1.1
myoblast
-
Homo sapiens
-
4.99.1.1
spleen
-
Mus musculus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.99.1.1
deuteroporphyrin IX + Zn2+
-
714596
Mus musculus
Zn-deuteroporphyrin IX + H+
-
-
-
?
4.99.1.1
deuteroporphyrin IX + Zn2+
-
714596
Homo sapiens
Zn-deuteroporphyrin IX + H+
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
4.99.1.1
?
x * 40000, SDS-PAGE
Homo sapiens
4.99.1.1
?
x * 40000, SDS-PAGE
Mus musculus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
4.99.1.1
[2Fe-2S]-center
ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis
Homo sapiens
4.99.1.1
[2Fe-2S]-center
ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis
Mus musculus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
4.99.1.1
[2Fe-2S]-center
ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis
Homo sapiens
4.99.1.1
[2Fe-2S]-center
ferrochelatase possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis
Mus musculus
General Stability (protein specific)
EC Number
General Stability
Organism
4.99.1.1
ferrochelatase shows a calculated half-life of approximately 35 h in vivo
Mus musculus
4.99.1.1
ferrochelatase shows a calculated half-life of approximately 35 h in vivo
Homo sapiens
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.99.1.1
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
4.99.1.1
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
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.99.1.1
40000
-
x * 40000, SDS-PAGE
Homo sapiens
4.99.1.1
40000
-
x * 40000, SDS-PAGE
Mus musculus
Oxidation Stability (protein specific)
EC Number
Oxidation Stability
Organism
4.99.1.1
FECH is destabilized by oxygen and mitochondrial oxidative stress
Mus musculus
4.99.1.1
FECH is destabilized by oxygen and mitochondrial oxidative stress
Homo sapiens
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
4.99.1.1
erythroblast
splenic erythroblast
Mus musculus
-
4.99.1.1
erythroleukemia cell
-
Mus musculus
-
4.99.1.1
muscle
-
Homo sapiens
-
4.99.1.1
myoblast
-
Homo sapiens
-
4.99.1.1
spleen
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.99.1.1
deuteroporphyrin IX + Zn2+
-
714596
Mus musculus
Zn-deuteroporphyrin IX + H+
-
-
-
?
4.99.1.1
deuteroporphyrin IX + Zn2+
-
714596
Homo sapiens
Zn-deuteroporphyrin IX + H+
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.99.1.1
?
x * 40000, SDS-PAGE
Homo sapiens
4.99.1.1
?
x * 40000, SDS-PAGE
Mus musculus