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Literature summary for 7.1.1.3 extracted from

  • Thomas, J.W.; Puustinen, A.; Alben, J.O.; Gennis, R.B.; Wikstroem, M.
    Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity (1993), Biochemistry, 32, 10923-10928.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D135E the mutant shows 45% activity compared to the wild type enzyme Escherichia coli
D135N the mutant shows 45% activity compared to the wild type enzyme, with proton pumping decoupled from the electron-transfer activity Escherichia coli
D188N the mutant shows 53% activity compared to the wild type enzyme Escherichia coli
D256N the mutant shows 25% activity compared to the wild type enzyme Escherichia coli
D407N the mutant shows 31% activity compared to the wild type enzyme Escherichia coli
E286A inactive Escherichia coli
E286Q the mutant shows 69% activity compared to the wild type enzyme Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli GL101
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquinol-1 + O2 + H+/in
-
Escherichia coli ubiquinone-1 + H2O + H+/out
-
?
ubiquinol-1 + O2 + H+/in
-
Escherichia coli GL101 ubiquinone-1 + H2O + H+/out
-
?

Synonyms

Synonyms Comment Organism
cytochrome bo ubiquinol oxidase
-
Escherichia coli