Literature summary extracted from
Cornejo, J.; Beale, S.I.
Algal heme oxygenase from Cyanidium caldarium. Partial purification and fractionation into three required protein components (1988), J. Biol. Chem., 263, 11915-11921.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.14.14.18 |
Fe/S cluster |
heme oxygenase consists of 3 required protein components: a ferredoxin-like Fe-S cluster protein that can be replaced by ferredoxin, a protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a protein with ferredoxin-linked cytochrome c reductase activity |
Cyanidium caldarium |
|
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.14.14.18 |
Sn-protoporphyrin |
0.002 mM, 80% inhibition |
Cyanidium caldarium |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.14.14.18 |
soluble |
- |
Cyanidium caldarium |
- |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.14.14.18 |
Iron |
heme oxygenase consists of 3 required protein components: a ferredoxin-like Fe-S cluster protein that can be replaced by ferredoxin, a protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a protein with ferredoxin-linked cytochrome c reductase activity |
Cyanidium caldarium |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.14.14.18 |
additional information |
- |
heme oxygenase consists of 3 components: a 22000 Da ferredoxin-like Fe/S cluster protein that can be replaced by ferredoxin, a 38000 Da protein that is inactivated by diethyldicarbonate, inactivation is blocked by heme, a 37000 Da protein with ferredoxin-linked cytochrome c reductase activity |
Cyanidium caldarium |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.14.14.18 |
Cyanidium caldarium |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.14.14.18 |
partial |
Cyanidium caldarium |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.14.14.18 |
heme + electron donor + O2 |
algal heme oxygenase requires a second reductant in addition to reduced pyridine nucleotide |
Cyanidium caldarium |
biliverdin + Fe2+ + CO + oxidized eletron donor + H2O |
- |
? |
|