Cloned (Comment) | Organism |
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overexpression in Escherichia coli BL21 | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ferroheme o + H2O + 2 acceptor | Bacillus subtilis | 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 | ferroheme a + 2 reduced acceptor | - |
? | |
ferroheme o + H2O + 2 acceptor | Bacillus subtilis 168 | 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 | ferroheme a + 2 reduced acceptor | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P12946 | - |
- |
Bacillus subtilis 168 | P12946 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ctaA | - |
Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
metabolism | 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 |