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Literature summary extracted from

  • Shi, Z.; Ferreira, G.C.
    Modulation of inhibition of ferrochelatase by N-methylprotoporphyrin (2006), Biochem. J., 399, 21-28.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.98.1.1 analysis Pro255 has a crucial role in maintaining an appropriate protein conformation and modulating the selectivity and/or regiospecificity of ferrochelatase, ferrochelatase mutants with improved tolerance towards N-methylprotoporphyrin may be potentially used in cell assay systems to study physiological responses to haem deficiency Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.98.1.1 Escherichia coli deltavis cells harbouring plasmids encoding active ferrochelatase mutants, wild-type murine ferrochelatase and mutants overexpressed, under the control of the Escherichia coli alkaline phosphatase promoter phoA, in Escherichia coli BL21(DE3) cells Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
4.98.1.1 K250M/V251L/W256Y can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus
4.98.1.1 K250N can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus
4.98.1.1 P255G drastically reduced inhibition of the variants by N-methylprotoporphyrin, can form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin, but is not paralleled with a decrease in specificity constant and/or catalytic activity Mus musculus
4.98.1.1 P255R drastically reduced inhibition of the variants by N-methylprotoporphyrin, can form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin, but is not paralleled with a decrease in specificity constant and/or catalytic activity Mus musculus
4.98.1.1 Q248P/S249G/K250P/G252W can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus
4.98.1.1 V251L can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.98.1.1 N-Methylprotoporphyrin binds to wild-type ferrochelatase and P255R mutant via a two-step pathway with a kinetically significant intermediate, firstly formation of an initial complex, which subsequently is rearranged into a more stable complex, secondly slow conformational change of the inhibitor–protein complex Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.98.1.1 Zn2+
-
 Mus musculus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
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 protoporphyrin IX + Zn2+
-
 Mus musculus Zn2+-protoporphyrin IX + H+
-
 ?

Synonyms

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.98.1.1 0.0683
-
 protoporphyrin IX wild-type Mus musculus
4.98.1.1 0.0983
-
 protoporphyrin IX mutant P255G Mus musculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.98.1.1 0.0014
-
 N-Methylprotoporphyrin wild-type Mus musculus
4.98.1.1 0.00251
-
 N-Methylprotoporphyrin mutant P255G Mus musculus