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Literature summary extracted from
- Ferrochelatase catalyzes the formation of Zn-protoporphyrin of dry-cured ham via the conversion reaction from heme in meat (2011), J. Agric. Food Chem., 59, 12238-12245.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.98.1.1 | ascorbate | optimum activity at 6 mM ascorbate | Thermus thermophilus |  |
| 4.98.1.1 | ascorbate | optimum activity at 6 mM ascorbate | Sus scrofa | |
| 4.98.1.1 | ascorbate | optimum activity at 6 mM ascorbate | Saccharomyces cerevisiae | |
| 4.98.1.1 | L-cysteine | optimum activity at 6 mM L-cysteine | Thermus thermophilus | |
| 4.98.1.1 | L-cysteine | optimum activity at 6 mM L-cysteine | Sus scrofa | |
| 4.98.1.1 | L-cysteine | optimum activity at 6 mM L-cysteine | Saccharomyces cerevisiae | |
| 4.98.1.1 | NaCl | optimum activity at 100 mM NaCl | Thermus thermophilus | |
| 4.98.1.1 | NaCl | optimum activity at 100 mM NaCl | Sus scrofa | |
| 4.98.1.1 | NaCl | optimum activity at 100 mM NaCl | Saccharomyces cerevisiae | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.98.1.1 | expressed in Escherichia coli BL21(DE3) cells | Thermus thermophilus |
| 4.98.1.1 | expressed in Escherichia coli BL21(DE3) cells | Sus scrofa |
| 4.98.1.1 | expressed in Escherichia coli BL21(DE3) cells | Saccharomyces cerevisiae |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.98.1.1 | 0.012 | - |
myoglobin | at pH 6.5 and 30°C | Saccharomyces cerevisiae | |
| 4.98.1.1 | 0.06 | - |
Zn2+ | at pH 6.5 and 30°C | Saccharomyces cerevisiae | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.98.1.1 | mitochondrial inner membrane | - |
Sus scrofa | 5743 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.98.1.1 | 33000 | - |
x * 33000, SDS-PAGE | Thermus thermophilus |
| 4.98.1.1 | 39000 | - |
x * 39000, SDS-PAGE | Saccharomyces cerevisiae |
| 4.98.1.1 | 42000 | - |
x * 42000, SDS-PAGE | Sus scrofa |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.98.1.1 | protoporphyrin IX + Fe2+ | Thermus thermophilus | - |
protoheme IX + 2 H+ | - |
? | |
| 4.98.1.1 | protoporphyrin IX + Fe2+ | Sus scrofa | - |
protoheme IX + 2 H+ | - |
? | |
| 4.98.1.1 | protoporphyrin IX + Fe2+ | Saccharomyces cerevisiae | - |
protoheme IX + 2 H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.98.1.1 | Saccharomyces cerevisiae | - |
- |
- |
| 4.98.1.1 | Sus scrofa | - |
- |
- |
| 4.98.1.1 | Thermus thermophilus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.98.1.1 | Ni2+-NTA bead chromatography | Thermus thermophilus |
| 4.98.1.1 | Ni2+-NTA bead chromatography | Sus scrofa |
| 4.98.1.1 | Ni2+-NTA bead chromatography | Saccharomyces cerevisiae |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 4.98.1.1 | muscle | - |
Sus scrofa | - |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 4.98.1.1 | 18°C, in 20 mM Tris-HCl (pH 8.0) containing 0.3 M NaCl, about 2 weeks, 42% residual activity | Saccharomyces cerevisiae |
| 4.98.1.1 | 4°C, in 20 mM Tris-HCl (pH 8.0) containing 0.3 M NaCl, 1 month, no loss of activity | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.98.1.1 | hemoglobin + Zn2+ | - |
Thermus thermophilus | Zn-protoporphyrin + H+ | - |
? | |
| 4.98.1.1 | hemoglobin + Zn2+ | - |
Sus scrofa | Zn-protoporphyrin + H+ | - |
? | |
| 4.98.1.1 | hemoglobin + Zn2+ | - |
Saccharomyces cerevisiae | Zn-protoporphyrin + H+ | - |
? | |
| 4.98.1.1 | mesoporphyrin IX + Fe2+ | - |
Thermus thermophilus | ? | - |
? | |
| 4.98.1.1 | mesoporphyrin IX + Fe2+ | - |
Sus scrofa | ? | - |
? | |
| 4.98.1.1 | mesoporphyrin IX + Fe2+ | - |
Saccharomyces cerevisiae | ? | - |
? | |
| 4.98.1.1 | myoglobin + Zn2+ | - |
Thermus thermophilus | Zn-protoporphyrin + H+ | - |
? | |
| 4.98.1.1 | myoglobin + Zn2+ | - |
Sus scrofa | Zn-protoporphyrin + H+ | - |
? | |
| 4.98.1.1 | myoglobin + Zn2+ | - |
Saccharomyces cerevisiae | Zn-protoporphyrin + H+ | - |
? | |
| 4.98.1.1 | protoporphyrin IX + Fe2+ | - |
Thermus thermophilus | protoheme IX + 2 H+ | - |
? | |
| 4.98.1.1 | protoporphyrin IX + Fe2+ | - |
Sus scrofa | protoheme IX + 2 H+ | - |
? | |
| 4.98.1.1 | protoporphyrin IX + Fe2+ | - |
Saccharomyces cerevisiae | protoheme IX + 2 H+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.98.1.1 | ? | x * 42000, SDS-PAGE | Sus scrofa |
| 4.98.1.1 | ? | x * 39000, SDS-PAGE | Saccharomyces cerevisiae |
| 4.98.1.1 | ? | x * 33000, SDS-PAGE | Thermus thermophilus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.98.1.1 | FeCH | - |
Thermus thermophilus |
| 4.98.1.1 | FeCH | - |
Sus scrofa |
| 4.98.1.1 | FeCH | - |
Saccharomyces cerevisiae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.98.1.1 | 5.5 | - |
reverse reaction | Thermus thermophilus |
| 4.98.1.1 | 5.5 | - |
reverse reaction | Sus scrofa |
| 4.98.1.1 | 5.5 | - |
reverse reaction | Saccharomyces cerevisiae |
| 4.98.1.1 | 7.5 | 8 | forward reaction | Thermus thermophilus |
| 4.98.1.1 | 7.5 | 8 | forward reaction | Sus scrofa |
| 4.98.1.1 | 7.5 | 8 | forward reaction | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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