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Literature summary for 1.17.99.9 extracted from

  • Hederstedt, L.
    Heme A biosynthesis (2012), Biochim. Biophys. Acta, 1817, 920-927 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C191A/C197A low activity Bacillus subtilis
C35A low activity Bacillus subtilis
C35A/C42A no detectable activity Bacillus subtilis
H123L no detectable activity Bacillus subtilis
H123M no detectable activity Bacillus subtilis
H216L no detectable activity Bacillus subtilis
H216M low activity Bacillus subtilis
H278L low activity Bacillus subtilis
H278M low activity Bacillus subtilis
H60L no detectable activity Bacillus subtilis
H60M low activity Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Saccharomyces cerevisiae 5737
-
cytoplasm
-
Bacillus subtilis 5737
-

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
-
?
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

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-
Bacillus subtilis P12946
-
-
Bacillus subtilis 168 P12946
-
-
Halobacterium salinarum
-
-
-
Saccharomyces cerevisiae
-
-
-
Schizosaccharomyces pombe
-
-
-

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
-
?
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
-
?

Subunits

Subunits Comment Organism
homodimer
-
Halobacterium salinarum
homodimer
-
Aeropyrum pernix
homodimer
-
Bacillus subtilis

Synonyms

Synonyms Comment Organism
COX15
-
Saccharomyces cerevisiae
COX15
-
Schizosaccharomyces pombe
ctaA
-
Halobacterium salinarum
ctaA
-
Schizosaccharomyces pombe
ctaA
-
Aeropyrum pernix
ctaA
-
Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
heme
-
Aeropyrum pernix
heme a between 0.2 and 1.95 mol heme B per mol CtaA polypeptide and up to 0.2 mol heme A per mol enzyme (CtaA) Bacillus subtilis
heme b between 0.2 and 1.95 mol heme B per mol CtaA polypeptide and up to 0.2 mol heme A per mol enzyme (CtaA) Bacillus subtilis