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Literature summary extracted from

  • Garcia-Horsman, J.; Puustinen, A.; Gennis, R.; Wikstrom, M.
    Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135-->Asn (1995), Biochemistry, 34, 4428-4433.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.1.3 expressed in Escherichia coli RG 129 cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.3 D135K the mutant is deficient in proton pumping (23% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 D135N the mutant is deficient in proton pumping (45% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 F138G the mutant shows 63% proton-translocating activity compared to the wild type enzyme Escherichia coli
7.1.1.3 F138R the mutant shows 55% proton-translocating activity compared to the wild type enzyme Escherichia coli
7.1.1.3 G132A the mutant shows wild type proton-translocation activity (113% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 G132D/D135N the mutant shows 66% proton-translocating activity compared to the wild type enzyme Escherichia coli
7.1.1.3 G132R the mutant shows wild type proton-translocation activity Escherichia coli
7.1.1.3 K362D/Dl35K the mutant is devoid of redox activity Escherichia coli
7.1.1.3 N124D the mutant is deficient in proton pumping (56% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 N124D/D135N the mutant shows 21% proton-translocating activity compared to the wild type enzyme Escherichia coli
7.1.1.3 N124H the mutant is deficient in proton pumping (16% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 N142D the mutant is deficient in proton pumping (48% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 N142D/D135N the mutant shows 33% proton-translocating activity compared to the wild type enzyme Escherichia coli
7.1.1.3 N142Q the mutant shows wild type proton-translocation activity (109% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 N142V the mutant is deficient in proton pumping (22% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 P128A the mutant shows wild type proton-translocation activity (115% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 P128D/D135N inactive Escherichia coli
7.1.1.3 P139E/D135N the mutant shows 95% proton-translocating activity compared to the wild type enzyme Escherichia coli
7.1.1.3 Pl39A the mutant shows wild type proton-translocation activity (67% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 Pl39E the mutant shows wild type proton-translocation activity (46% activity compared to the wild type enzyme) Escherichia coli
7.1.1.3 R134P the mutant shows 112% proton-translocating activity compared to the wild type enzyme Escherichia coli

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.3 Cu2+ the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.3 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.3 ubiquinol + O2 + H+/in
-
Escherichia coli ubiquinone + H2O + H+/out
-
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Synonyms

EC Number Synonyms Comment Organism
7.1.1.3 cytochrome bo3 ubiquinol oxidase
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.3 heme the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family Escherichia coli

General Information

EC Number General Information Comment Organism
7.1.1.3 physiological function the ubiquinol oxidase, cytochrome b03, of Escherichia coli is a member of the respiratory heme-copper oxidase family and conserves energy from the reduction of dioxygen to water by translocation of protons across the bacterial membrane Escherichia coli