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Literature summary extracted from

  • Hunter, G.; Ferreira, G.
    Identification and characterization of an inhibitory metal ion-binding site in ferrochelatase (2010), J. Biol. Chem., 285, 41836-41841.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.98.1.1 F283L the mutation eliminates inhibition by Ni2+ Mus musculus
4.98.1.1 H287C the mutant is substrate-inhibited by Zn2+ and Cu2+ and shows decreased inhibition by Ni2+ compare to the wild type enzyme Mus musculus
4.98.1.1 H287L the mutant is not substrate-inhibited by Ni2+ but is weakly inhibited by Co2+, Zn2+, and inhibited by Cu2+ Mus musculus
4.98.1.1 H287N the mutant is substrate-inhibited by Ni2+, Fe2+, Zn2+, and Co2+ Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.98.1.1 Co2+ substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components Mus musculus
4.98.1.1 Cu2+ substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components Mus musculus
4.98.1.1 Ni2+ substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components Mus musculus
4.98.1.1 Zn2+ substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.98.1.1 0.001
-
 protoporphyrin IX wild type enzyme, at pH 8.0, temperature not specified in the publication Mus musculus
4.98.1.1 0.005
-
 protoporphyrin IX mutant enzyme F283L, at pH 8.0, temperature not specified in the publication Mus musculus
4.98.1.1 0.116
-
 protoporphyrin IX mutant enzyme H287L, at pH 8.0, temperature not specified in the publication Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
4.98.1.1 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.98.1.1 additional information the inhibitory metal ion-binding site of ferrochelatase is composed of multiple residues but primarily defined by His-287 and Phe-283 and is crucial for optimal activity at low metal ion concentrations. This binding site may be important for ferrous iron acquisition and desolvation in vivo Mus musculus ?
-
 ?
4.98.1.1 protoporphyrin IX + Fe2+
-
 Mus musculus protoheme IX + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.98.1.1 FeCH
-
 Mus musculus
4.98.1.1 protoporhyrin IX ferrochelatase
-
 Mus musculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.98.1.1 0.007
-
 Ni2+ wild type enzyme, at pH 8.0, temperature not specified in the publication Mus musculus
4.98.1.1 2.4
-
 Ni2+ mutant enzyme F283L, at pH 8.0, temperature not specified in the publication Mus musculus