Literature summary for 4.98.1.1 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P22830	-	-

Purification (Commentary)

Purification (Comment)	Organism
by metal affinity chromatography	Homo sapiens

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)