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Literature summary for 4.98.1.1 extracted from

  • Hunter, G.A.; Al-Karadaghi, S.; Ferreira, G.C.
    Ferrochelatase: the convergence of the porphyrin biosynthesis and iron transport pathways (2011), J. Porphyr. Phthalocyanines, 15, 350-356.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.98.1.1

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P32396
-
-
Homo sapiens P22830
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ferric iron is not a substrate Bacillus subtilis ?
-
 ?
additional information ferric iron is not a substrate Homo sapiens ?
-
 ?
additional information the enzyme is highly specific for ferrous ion in vivo, however in vitro ferrochelatase catalyzes insertion of a remarkable variety of divalent metal ions into protoporphyrin and other closely related porphyrins Bacillus subtilis ?
-
 ?
additional information the enzyme is highly specific for ferrous ion in vivo, however in vitro ferrochelatase catalyzes insertion of a remarkable variety of divalent metal ions into protoporphyrin and other closely related porphyrins Homo sapiens ?
-
 ?
protoporphyrin IX + Fe2+
-
 Bacillus subtilis protoheme IX + 2 H+
-
 ?
protoporphyrin IX + Fe2+
-
 Homo sapiens protoheme IX + 2 H+
-
 ?

Synonyms

Synonyms Comment Organism
PPIX ferrochelatase
-
 Bacillus subtilis
PPIX ferrochelatase
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism ferrochelatase accelerates heme formation via binding the substrates in optimized positions within the active site Bacillus subtilis
metabolism ferrochelatase accelerates heme formation via binding the substrates in optimized positions within the active site Homo sapiens