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
1.17.99.9 heme a synthaseAdvanced search results
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results (Engineering
Engineering on EC 1.17.99.9 - heme a synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C191A/C197A
C35A/C42A
DELTA211-217
Bacillus subtilis LMT20R is deleted for the ctaA gene and, therefore, completely blocked in heme A synthesis. Plasmid pH216MS is obtained from plasmid pH216M (encoding the mutant CtaA-H216M) and carries a 21 bp deletion in ctaA. The CtaADELTA211-217 variant encoded by pH216MS is active in heme A synthesis and supports assembly of normal levels of cytochrome caa3
E57A
heme content of the mutant enzyme is 62% compared to wild-type enzyme
E57A/H216A
heme content of the mutant enzyme is 28% compared to wild-type enzyme
E57A/H278A
heme content of the mutant enzyme is 42% compared to wild-type enzyme
E57Q
heme content of the mutant enzyme is 65% compared to wild-type enzyme
H123A
heme content of the mutant enzyme is 74% compared to wild-type enzyme
H123L
H123M
H123Q
heme content of the mutant enzyme is 64% compared to wild-type enzyme
H216A
heme content of the mutant enzyme is 22% compared to wild-type enzyme
H216A-H278A
heme content of the mutant enzyme is 5% compared to wild-type enzyme
H216M
H216M/DELTA211-217
Bacillus subtilis LMT20R is deleted for the ctaA gene and, therefore, completely blocked in heme A synthesis. Plasmid pH216MS is obtained from plasmid pH216M (encoding the mutant CtaA-H216M) and carries a 21 bp deletion in ctaA. The CtaADELTA211-217 variant encoded by pH216MS is active in heme A synthesis and supports assembly of normal levels of cytochrome caa3
H216Q
heme content of the mutant enzyme is 33% compared to wild-type enzyme
H216Q-H278Q
heme content of the mutant enzyme is 6% compared to wild-type enzyme
H278A
heme content of the mutant enzyme is 56% compared to wild-type enzyme
H278C
heme content of the mutant enzyme is 14% compared to wild-type enzyme
H278M
H278Q
heme content of the mutant enzyme is 15% compared to wild-type enzyme
H60A
heme content of the mutant enzyme is 74% compared to wild-type enzyme
H60A/H123A
heme content of the mutant enzyme is 88% compared to wild-type enzyme
H60M
H60Q
heme content of the mutant enzyme is 65% compared to wild-type enzyme
H60Q-H123Q
heme content of the mutant enzyme is 83% compared to wild-type enzyme
Q103A
heme content of the mutant enzyme is 82% compared to wild-type enzyme
Q257A
heme content of the mutant enzyme is 78% compared to wild-type enzyme
R217A
heme content of the mutant enzyme is 84% compared to wild-type enzyme
R217Q
heme content of the mutant enzyme is 89% compared to wild-type enzyme
R61A
heme content of the mutant enzyme is 77% compared to wild-type enzyme
R61Q
heme content of the mutant enzyme is 79% compared to wild-type enzyme
W39A
heme content of the mutant enzyme is 84% compared to wild-type enzyme
DELTA211-217
-
Bacillus subtilis LMT20R is deleted for the ctaA gene and, therefore, completely blocked in heme A synthesis. Plasmid pH216MS is obtained from plasmid pH216M (encoding the mutant CtaA-H216M) and carries a 21 bp deletion in ctaA. The CtaADELTA211-217 variant encoded by pH216MS is active in heme A synthesis and supports assembly of normal levels of cytochrome caa3
-
E57A
-
heme content of the mutant enzyme is 62% compared to wild-type enzyme
-
H123A
-
heme content of the mutant enzyme is 74% compared to wild-type enzyme
-
H216M
H216M/DELTA211-217
-
Bacillus subtilis LMT20R is deleted for the ctaA gene and, therefore, completely blocked in heme A synthesis. Plasmid pH216MS is obtained from plasmid pH216M (encoding the mutant CtaA-H216M) and carries a 21 bp deletion in ctaA. The CtaADELTA211-217 variant encoded by pH216MS is active in heme A synthesis and supports assembly of normal levels of cytochrome caa3
-
H278Q
-
heme content of the mutant enzyme is 15% compared to wild-type enzyme
-
H60A
-
heme content of the mutant enzyme is 74% compared to wild-type enzyme
-
H60M
H60Q
-
heme content of the mutant enzyme is 65% compared to wild-type enzyme
-
R217W
-
mutations of COX15 causing single amino acid conversions associated with fatal infantile hypertrophic cardiomyopathy and the neurological disorder Leigh syndrome results in impaired catalytic function, and the mutation affects oligomeric properties of the enzyme. The mutations affects protein folding and heme binding
S344P
-
mutations of COX15 causing single amino acid conversions associated with fatal infantile hypertrophic cardiomyopathy and the neurological disorder Leigh syndrome results in impaired stability. The mutations affect protein folding and heme binding
H129A
overexpression of the non-functional TcCox15 mutants causes a negative effect over heme A synthesis, affecting the function of the CcO complex and proliferation of epimastigotes
H206A
overexpression of the non-functional TcCox15 mutants causes a negative effect over heme A synthesis, affecting the function of the CcO complex and proliferation of epimastigotes
H307A
overexpression of the non-functional TcCox15 mutants causes a negative effect over heme A synthesis, affecting the function of the CcO complex and proliferation of epimastigotes
H129A
-
overexpression of the non-functional TcCox15 mutants causes a negative effect over heme A synthesis, affecting the function of the CcO complex and proliferation of epimastigotes
-
H206A
-
overexpression of the non-functional TcCox15 mutants causes a negative effect over heme A synthesis, affecting the function of the CcO complex and proliferation of epimastigotes
-
H307A
-
overexpression of the non-functional TcCox15 mutants causes a negative effect over heme A synthesis, affecting the function of the CcO complex and proliferation of epimastigotes
-
additional information
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mutations in COX15 repress heme O synthesis and have a dominant effect when combined with other mutations
C191A/C197A
the heme content is reduced to a half of the wild-type level
C35A/C42A
heme content of the mutant enzyme is 77% compared to wild-type enzyme
H216M
heme content of the mutant enzyme is 37% compared to wild-type enzyme
H216M
the H216M variant binds the enzyme substrate heme O, probably with methionine as an axial ligand, but is defective in heme A synthesis and accumulates a mono-hydroxylated reaction intermediate, heme I
H216M
the variant has a decreased heme A synthase activity. It contains heme B, heme O, and heme I, as well as trace amounts of heme A
H278M
heme content of the mutant enzyme is 40% compared to wild-type enzyme
H60M
the mutant enzyme contains heme B and heme A at levels comparable to that of wild-type enzyme
H216M
-
the H216M variant binds the enzyme substrate heme O, probably with methionine as an axial ligand, but is defective in heme A synthesis and accumulates a mono-hydroxylated reaction intermediate, heme I
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H216M
-
the variant has a decreased heme A synthase activity. It contains heme B, heme O, and heme I, as well as trace amounts of heme A
-
H60M
-
the mutant enzyme contains heme B and heme A at levels comparable to that of wild-type enzyme
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