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Literature summary extracted from

  • Medlock, A.; Swartz, L.; Dailey, T.A.; Dailey, H.A.; Lanzilotta, W.N.
    Substrate interactions with human ferrochelatase (2007), Proc. Natl. Acad. Sci. USA, 104, 1789-1793.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.98.1.1 by the hanging drop method, crystals of mutant E343K with the substrate protoporphyrin IX and mutant R115L without bound substrate. Enzyme with porphyrin bound possesses a significantly more closed active site conformation. In the substrate-bound form, the jaws of the active site mouth are closed so that the porphyrin substrate is completely engulfed in the pocket Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.98.1.1 E343K crystals belong to the triclinic space group P1, possess [2Fe-2S] clusters Homo sapiens
4.98.1.1 R115L crystal structure is orthorhombic (P212121), possess [2Fe-2S] clusters, presence of an imidazole in the active site Homo sapiens

Metals/Ions

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

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 by metal affinity chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.98.1.1 protoporphyrin IX + Fe2+ substrate is bound deep within an enclosed pocket Homo sapiens protoheme IX + 2 H+
-
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