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Literature summary for 1.17.99.9 extracted from

  • Mogi, T.
    Probing structure of heme A synthase from Bacillus subtilis by site-directed mutagenesis (2009), J. Biochem., 145, 625-633 .
    View publication on PubMed
Search for more literature for 1.17.99.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
C191A/C197A the heme content is reduced to a half of the wild-type level Bacillus subtilis
C35A/C42A heme content of the mutant enzyme is 77% compared to wild-type enzyme Bacillus subtilis
E57A heme content of the mutant enzyme is 62% compared to wild-type enzyme Bacillus subtilis
E57A/H216A heme content of the mutant enzyme is 28% compared to wild-type enzyme Bacillus subtilis
E57A/H278A heme content of the mutant enzyme is 42% compared to wild-type enzyme Bacillus subtilis
E57Q heme content of the mutant enzyme is 65% compared to wild-type enzyme Bacillus subtilis
H123A heme content of the mutant enzyme is 74% compared to wild-type enzyme Bacillus subtilis
H123Q heme content of the mutant enzyme is 64% compared to wild-type enzyme Bacillus subtilis
H216A heme content of the mutant enzyme is 22% compared to wild-type enzyme Bacillus subtilis
H216A-H278A heme content of the mutant enzyme is 5% compared to wild-type enzyme Bacillus subtilis
H216M heme content of the mutant enzyme is 37% compared to wild-type enzyme Bacillus subtilis
H216Q heme content of the mutant enzyme is 33% compared to wild-type enzyme Bacillus subtilis
H216Q-H278Q heme content of the mutant enzyme is 6% compared to wild-type enzyme Bacillus subtilis
H278A heme content of the mutant enzyme is 56% compared to wild-type enzyme Bacillus subtilis
H278C heme content of the mutant enzyme is 14% compared to wild-type enzyme Bacillus subtilis
H278M heme content of the mutant enzyme is 40% compared to wild-type enzyme Bacillus subtilis
H278Q heme content of the mutant enzyme is 15% compared to wild-type enzyme Bacillus subtilis
H60A heme content of the mutant enzyme is 74% compared to wild-type enzyme Bacillus subtilis
H60A/H123A heme content of the mutant enzyme is 88% compared to wild-type enzyme Bacillus subtilis
H60Q heme content of the mutant enzyme is 65% compared to wild-type enzyme Bacillus subtilis
H60Q-H123Q heme content of the mutant enzyme is 83% compared to wild-type enzyme Bacillus subtilis
Q103A heme content of the mutant enzyme is 82% compared to wild-type enzyme Bacillus subtilis
Q257A heme content of the mutant enzyme is 78% compared to wild-type enzyme Bacillus subtilis
R217A heme content of the mutant enzyme is 84% compared to wild-type enzyme Bacillus subtilis
R217Q heme content of the mutant enzyme is 89% compared to wild-type enzyme Bacillus subtilis
R61A heme content of the mutant enzyme is 77% compared to wild-type enzyme Bacillus subtilis
R61Q heme content of the mutant enzyme is 79% compared to wild-type enzyme Bacillus subtilis
W39A heme content of the mutant enzyme is 84% compared to wild-type enzyme Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the enzyme has eight transmembrane helices Bacillus subtilis 16020
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Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Synonyms

Synonyms Comment Organism
ctaA
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
heme b two molecules of heme B are bound to the enzyme. Wild-type enzyme contains 54.6 nmol/mg protein. Heme composition of wild-type enzyme hemeB:hemeO:hemeOX:hemeOY is 1.95:0.02:0.03:0. Substitutions of His60 and His126 do not affect heme binding, while His216 and His278 in the carboxy-halves are essential in heme binding Bacillus subtilis