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Literature summary extracted from
- The conserved active-site loop residues of ferrochelatase induce porphyrin conformational changes necessary for catalysis (2006), Biochemistry, 45, 2904-2912.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.98.1.1 | expression in Escherichia coli | Mus musculus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.98.1.1 | 0.0014 | - |
protoporphyrin IX | wild-type, under strictly anaerobic conditions | Mus musculus |  |
| 4.98.1.1 | 0.00251 | - |
protoporphyrin IX | mutant P255G, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.00265 | - |
protoporphyrin IX | mutant P255R, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.00684 | - |
protoporphyrin IX | mutant S249A/K250Q/V251C, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.01034 | - |
protoporphyrin IX | mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.01125 | - |
protoporphyrin IX | mutant K250M/V251L/W256Y, under strictly anaerobic conditions | Mus musculus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.98.1.1 | protoporphyrin + Fe2+ | Mus musculus | - |
protoheme + H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.98.1.1 | Mus musculus | P22315 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.98.1.1 | recombinant protein | Mus musculus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.98.1.1 | protoporphyrin + Fe2+ | - |
Mus musculus | protoheme + H+ | - |
? | |
| 4.98.1.1 | protoporphyrin IX + Fe2+ | under strictly anaerobic conditions | Mus musculus | protoheme + 2 H+ | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.98.1.1 | ferrochelatase | - |
Mus musculus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.98.1.1 | 0.051 | - |
protoporphyrin IX | mutant K250M/V251L/W256Y, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.068 | - |
protoporphyrin IX | wild-type, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.098 | - |
protoporphyrin IX | mutant P255G, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.13 | - |
protoporphyrin IX | mutant P255R, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.234 | - |
protoporphyrin IX | mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions | Mus musculus | |
| 4.98.1.1 | 0.3 | - |
protoporphyrin IX | mutant S249A/K250Q/V251C, under strictly anaerobic conditions | Mus musculus | |
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Release 2023.1 (January 2023)
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