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Literature summary for 1.17.99.9 extracted from

  • Brown, K.; Allan, B.; Do, P.; Hegg, E.
    Identification of novel hemes generated by heme A synthase Evidence for two successive monooxygenase reactions (2002), Biochemistry, 41, 10906-10913 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli BL21 Bacillus subtilis

Natural Substrates/ Products (Substrates)

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
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 ?
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
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 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P12946
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Bacillus subtilis 168 P12946
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-

Substrates and Products (Substrate)

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
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 ?
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
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 ?
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
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 ?
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
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 ?
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
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 ?
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
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 ?
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
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 ?

Synonyms

Synonyms Comment Organism
ctaA
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 Bacillus subtilis

General Information

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