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Literature summary for 4.98.1.1 extracted from

  • Grzybowska, E.; Gora, M.; Plochocka, D.; Rytka, J.
    Saccharomyces cerevisiae ferrochelatase forms a homodimer (2002), Arch. Biochem. Biophys., 398, 170-178.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D246V/Y248F dimerization-defective, partially blocked in activity Saccharomyces cerevisiae
E314A no enzymic activity Saccharomyces cerevisiae
G47Delta no enzymic activity Saccharomyces cerevisiae
H235L no enzymic activity Saccharomyces cerevisiae
L62Y no enzymic activity Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
2 * 40000, SDS-PAGE, complementation analysis Saccharomyces cerevisiae
80000
-
chemical crosslinking plus SDS-PAGE Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
protoheme + 2 H+ = protoporphyrin + Fe2+ structural model Saccharomyces cerevisiae

Subunits

Subunits Comment Organism
dimer 2 * 40000, SDS-PAGE, complementation analysis Saccharomyces cerevisiae