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.
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 |
- |
? |
|
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 |