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Literature summary extracted from

  • Asuru, A.P.; An, M.; Busenlehner, L.S.
    Dissection of porphyrin-induced conformational dynamics in the heme biosynthesis enzyme ferrochelatase (2012), Biochemistry, 51, 7116-7127.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.98.1.1 expressed in Escherichia coli HB101 cells Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.98.1.1 mitochondrial inner membrane
-
 Homo sapiens 5743
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.98.1.1 Fe2+ contains 1.8 mol iron per mol ferrochelatase Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.98.1.1 84000
-
 gel filtration 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 IX + Fe2+ Homo sapiens
-
 protoheme IX + 2 H+
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
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 mesoporphyrin IX + Fe2+
-
 Homo sapiens ?
-
 ?
4.98.1.1 protoporphyrin IX + Fe2+
-
 Homo sapiens protoheme IX + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
4.98.1.1 homodimer
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.98.1.1 [2Fe-2S]-center
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
4.98.1.1 metabolism the enzyme catalyzes the insertion ferrous iron into protoporphyrin IX as the last step in heme biosynthesis Homo sapiens