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Literature summary 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

Cloned(Commentary)

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

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.98.1.1 Fe2+
-
Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.98.1.1 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

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.98.1.1 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

EC Number Subunits Comment Organism
4.98.1.1 homodimer
-
Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
4.98.1.1 FeCH
-
Homo sapiens
4.98.1.1 ferrochelatase
-
Homo sapiens

General Information

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