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Literature summary extracted from

  • Asuru, A.; Busenlehner, L.
    Analysis of human ferrochelatase iron binding via amide hydrogen/deuterium exchange mass spectrometry (2011), Int. J. Mass Spectrom., 302, 76-84.
No PubMed abstract available

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 mitochondrion inner mitochondrial membrane Homo sapiens 5739
-

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 P22830
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.98.1.1 Ni-NTA column chromatography. After aerobic purification, the cysteine residues can oxidize and release the [2Fe-2S] cluster, causing ferrochelatase to precipitate. CHAPS is best at solubilizing ferrochelatase, while retaining full activity as compared to the enzyme in sodium cholate Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.98.1.1 mesoporphyrin IX + Fe2+ activity measurements were perfomed with a second redox reaction with protoporphyrin IX / protoheme IX as product Homo sapiens Fe-mesoporphyrin IX + 2 H+
-
 ?
4.98.1.1 protoporphyrin IX + Fe2+
-
 Homo sapiens protoheme IX + 2 H+
-
 ?

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 ferrochelatase catalyzes the last step in the heme biosynthetic pathway Homo sapiens