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Literature summary for 4.98.1.1 extracted from

  • Pazdernik, M.; Mares, J.; Pilny, J.; Sobotka, R.
    The antenna-like domain of the cyanobacterial ferrochelatase can bind chlorophyll and carotenoids in an energy-dissipative configuration (2019), J. Biol. Chem., 294, 11131-11143 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
N-methyl mesoporphyrin IX specific inhibitor Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protoporphyrin IX + Fe2+ Synechocystis sp. PCC 6803
-
Fe-protoporphyrin IX + 2 H+
-
?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrin IX + Fe2+
-
Synechocystis sp. PCC 6803 Fe-protoporphyrin IX + 2 H+
-
?

Subunits

Subunits Comment Organism
monomer or homodimer the enzyme exists mostly as a pigment-free monomer in cells but can dimerize Synechocystis sp. PCC 6803

Synonyms

Synonyms Comment Organism
FeCH
-
Synechocystis sp. PCC 6803
ferrochelatase
-
Synechocystis sp. PCC 6803
protoheme ferro-lyase
-
Synechocystis sp. PCC 6803

General Information

General Information Comment Organism
malfunction the enzyme binds chlorophyll and carotenoids when its enzymatic activity is low. Decreased enzyme activity results in excess production of chlorophyll in the cell Synechocystis sp. PCC 6803