EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.17.99.9 | ferroheme i + H2O + acceptor |
the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group |
Bacillus subtilis |
hydroxyferroheme i + reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme i + H2O + acceptor |
the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group |
Bacillus subtilis 168 |
hydroxyferroheme i + reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor |
overall reaction |
Aeropyrum pernix |
ferroheme a + 2 reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor |
overall reaction. The enzyme is involved in biosynthesis of heme A, an obligatory cofactor in eukaryotic cytochrome c oxidase. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a |
Bacillus subtilis |
ferroheme a + 2 reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor |
overall reaction. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a |
Bacillus subtilis |
ferroheme a + 2 reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor |
overall reaction |
Aeropyrum pernix ATCC 700893 |
ferroheme a + 2 reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor |
overall reaction. The enzyme is involved in biosynthesis of heme A, an obligatory cofactor in eukaryotic cytochrome c oxidase. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a |
Bacillus subtilis 168 |
ferroheme a + 2 reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + 2 acceptor |
overall reaction. The enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a |
Bacillus subtilis 168 |
ferroheme a + 2 reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + acceptor |
the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group |
Bacillus subtilis |
ferroheme i + reduced acceptor |
- |
? |
| 1.17.99.9 | ferroheme o + H2O + acceptor |
the enzyme catalyses the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source. The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group |
Bacillus subtilis 168 |
ferroheme i + reduced acceptor |
- |
? |
