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Literature summary for 4.98.1.1 extracted from

  • Shipovskov, S.; Karlberg, T.; Fodje, M.; Hansson, M.D.; Ferreira, G.C.; Hansson, M.; Reimann, C.T.; Al-Karadaghi, S.
    Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism (2005), J. Mol. Biol., 352, 1081-1090.
    View publication on PubMed
Search for more literature for 4.98.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and mutants Y13F and H183C with N-methyl mesoporphyrin Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
H183C inactive Bacillus subtilis
Y13F activity is equal to that of the wild-type enzyme Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
N-methyl mesoporphyrin transition-state inhibitor Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 Zn2+ pH 7.4 Bacillus subtilis
0.17
-
 Cu2+ pH 7.4 Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protoporphyrin + Fe2+ Bacillus subtilis
-
 protoheme + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P32396
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-methyl mesoporphyrin + Cu2+ pH 7.4 Bacillus subtilis ?
-
 ?
N-methyl mesoporphyrin + Zn2+ pH 7.4 Bacillus subtilis ?
-
 ?
protoporphyrin + Fe2+
-
 Bacillus subtilis protoheme + H+
-
 ?
protoporphyrin IX + Fe2+
-
 Bacillus subtilis protoheme + 2 H+
-
 ?

Synonyms

Synonyms Comment Organism
ferrochelatase
-
 Bacillus subtilis
protoporphyrin IX ferrochelatase
-
 Bacillus subtilis