1.17.99.9: heme a synthase
This is an abbreviated version!
For detailed information about heme a synthase, go to the full flat file.
Reaction
Synonyms
ape1694, cCtaA, COX15, COX15p, ctaA, CtaA protein, HAS, TcCox15
ECTree
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Substrates Products
Substrates Products on EC 1.17.99.9 - heme a synthase
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REACTION DIAGRAM
hydroxyferroheme i + reduced 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
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-
?
ferroheme i + H2O + acceptor
hydroxyferroheme i + reduced 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
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-
?
ferroheme a + 2 reduced acceptor
overall reaction
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-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced acceptor
Aeropyrum pernix ATCC 700893
overall reaction
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-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
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-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
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-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
-
-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
-
-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
-
-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
-
-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
-
-
?
ferroheme o + H2O + 2 acceptor
ferroheme a + 2 reduced 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
-
-
?
ferroheme i + reduced 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
-
-
?
ferroheme o + H2O + acceptor
ferroheme i + reduced 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
-
-
?