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Literature summary for 4.98.1.1 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
Search for more literature for 4.98.1.1

Application

Application Comment Organism
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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
K250M/V251L/W256Y can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus
K250N can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus
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
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
Q248P/S249G/K250P/G252W can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus
V251L can not form colonies onto medium containing more than 0.02 mM N-methylprotoporphyrin Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
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

Metals/Ions Comment Organism Structure
Zn2+
-
 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrin IX + Zn2+
-
 Mus musculus Zn2+-protoporphyrin IX + H+
-
 ?

Synonyms

Synonyms Comment Organism
protoporhyrin IX ferrochelatase
-
 Mus musculus

Turnover Number [1/s]

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

Ki Value [mM]

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