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Literature summary for 4.98.1.1 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
Search for more literature for 4.98.1.1

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
protoporphyrin IX + Fe2+
-
 Mus musculus protoheme IX + 2 H+
-
 ?

Synonyms

Synonyms Comment Organism
FeCH
-
 Mus musculus
protoporhyrin IX ferrochelatase
-
 Mus musculus

Ki Value [mM]

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