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Literature summary for 4.98.1.1 extracted from

  • Chen, W.; Dailey, H.A.; Paw, B.H.
    Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis (2010), Blood, 116, 628-630.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
ferrochelatase protein is induced in parallel with mitoferrin-1 and Abcb10 during Friend mouse erythroleukemia cell erythroid differentiation Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protoporphyrin + Fe2+ Homo sapiens ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis protoheme + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrin + Fe2+ ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis Homo sapiens protoheme + 2 H+
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
FeCH
-
 Homo sapiens
ferrochelatase
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis Homo sapiens