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Literature summary for 4.98.1.1 extracted from

  • Taketani, S.; Ishigaki, M.; Mizutani, A.; Uebayashi, M.; Numata, M.; Ohgari, Y.; Kitajima, S.
    Heme synthase (ferrochelatase) catalyzes the removal of iron from heme and demetalation of metalloporphyrins (2007), Biochemistry, 46, 15054-15061.
    View publication on PubMed
Search for more literature for 4.98.1.1

Activating Compound

Activating Compound Comment Organism Structure
additional information b5 reductase required for the full enzyme activity Mus musculus
additional information recombinant ferrochelatase exhibits iron removal activity when added together with purified recombinant b5 reductase Homo sapiens

Application

Application Comment Organism
additional information reverse reaction of ferrochelatase, which may contribute to a new route of the recycling of protoporphyrin and heme in cells Mus musculus
additional information reverse reaction of ferrochelatase, which may contribute to a new route of the recycling of protoporphyrin and heme in cells Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli expressing His-tagged ferrochelatase Homo sapiens

Protein Variants

Protein Variants Comment Organism
C395delta deletion of the C-terminus of the enzyme, where the iron-sulfur is located, results in the loss of both ferrochelatase activity and iron-removal activity Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Mus musculus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+
-
 Homo sapiens
Co2+
-
 Homo sapiens
Fe2+
-
 Mus musculus
Fe2+
-
 Homo sapiens
Sn2+
-
 Homo sapiens
Zn2+
-
 Mus musculus
Zn2+
-
 Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 gel filtration Mus musculus

Organism

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

Purification (Commentary)

Purification (Comment) Organism
five-step purification, by gel filtration, purified about 410fold with a 3% yield Mus musculus
with Ni2+ beads Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
BALB/3T3 cell conversion of mesoporphyrin is dependent on the expression of ferrochelatase, since control Balb/3T3 cells have much lower expression of ferrochelatase than the ferrochelatase transfectants Mus musculus
-
liver
-
 Mus musculus
-
additional information M-TAT cell, when induced to undergo erythroid differentiation M-TAT cells convert more zinc mesoporphyrin than control cells, accompanied by an increase in hemoglobin-synthesizing cells Homo sapiens
-
additional information MEL cell, clear conversion of zinc mesoporphyrin, marked increase in the conversion in erythroid differentiation-induced MEL cells, in which ferrochelatase is induced Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Cd2+-protoporphyrin + H+ poor substrate Homo sapiens protoporphyrin + Cd2+
-
 ?
Co2+-protoporphyrin + H+
-
 Homo sapiens protoporphyrin + Co2+
-
 ?
Fe2+-mesoporphyrin IX + H+
-
 Mus musculus mesoporphyrin IX + Fe2+
-
 ?
Fe2+-protoporphyrin + H+
-
 Homo sapiens protoporphyrin + Fe2+
-
 ?
Sn2+-protoporphyrin + H+
-
 Homo sapiens protoporphyrin + Sn2+
-
 ?
Zn2+-mesoporphyrin + H+
-
 Mus musculus mesoporphyrin + Zn2+
-
 ?
Zn2+-mesoporphyrin + H+
-
 Homo sapiens mesoporphyrin + Zn2+
-
 ?
Zn2+-protoporphyrin + H+
-
 Mus musculus protoporphyrin + Zn2+
-
 ?
Zn2+-protoporphyrin + H+
-
 Homo sapiens protoporphyrin + Zn2+
-
 ?

Synonyms

Synonyms Comment Organism
heme synthase
-
 Mus musculus
heme synthase
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6
-
 Mus musculus