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Literature summary for 4.98.1.1 extracted from

  • Sobotka, R.; Tichy, M.; Wilde, A.; Hunter, C.N.
    Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: the CAB domain plays a regulatory role, and region II is essential for catalysis (2011), Plant Physiol., 155, 1735-1747.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information deletion of the CAB domain prevents the DELTAH347 ferrochelatase mutant strain from growing at higher light intensities and affects the cellular accumulation of tetrapyrroles. The mutant is active as a monomer Synechocystis sp.

General Stability

General Stability Organism
region II is critical for both the stability and enzyme activity of Synechocystis ferrochelatase Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
anti-FLAG M2 affinity gel column chromatography or Ni2+-charged His-select resin column chromatography Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrin IX + Zn2+
-
 Synechocystis sp. Zn-protoporphyrin IX + H+
-
 ?

Subunits

Subunits Comment Organism
dimer full-length enzyme, the CAB domain is necessary for the dimerization of Synechocystis ferrochelatase in vivo Synechocystis sp.

Synonyms

Synonyms Comment Organism
FeCH
-
 Synechocystis sp.

General Information

General Information Comment Organism
physiological function the apparent surplus of ferrochelatase activity in the wild type is critical for cell viability under high light due to a regulatory role of ferrochelatase in the distribution of chlorophyll into apoproteins Synechocystis sp.