EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
7.1.1.3 | D135N | the mutations specifically eliminates the CuB center from the oxidase complex | Escherichia coli |
7.1.1.3 | D188N | the mutant possesses 100% copper and 81% cytochrome o compared to the wild type enzyme | Escherichia coli |
7.1.1.3 | D256N | the mutant possesses 103% copper and 74% cytochrome o compared to the wild type enzyme | Escherichia coli |
7.1.1.3 | D407N | the mutation affects the CO-binding by the heme-copper binuclear center | Escherichia coli |
7.1.1.3 | E286D | the mutant does not show significant perturbations on the redox metal centers even though it is still inactive | Escherichia coli |
7.1.1.3 | E286Q | the mutations specifically eliminates the CuB center from the oxidase complex | Escherichia coli |
7.1.1.3 | E540Q | the mutation affects the CO-binding by the heme-copper binuclear center | Escherichia coli |
7.1.1.3 | K362Q | the mutation affects the CO-binding by the heme-copper binuclear center | Escherichia coli |
7.1.1.3 | K55Q | the mutant possesses 100% copper and 73% cytochrome o compared to the wild type enzyme | Escherichia coli |
7.1.1.3 | R257Q | the mutations specifically eliminates the CuB center from the oxidase complex | Escherichia coli |
7.1.1.3 | R481Q | the mutant possesses 91% copper and 73% cytochrome o compared to the wild type enzyme | Escherichia coli |
7.1.1.3 | R482Q | the mutant possesses 82% copper and 100% cytochrome o compared to the wild type enzyme | Escherichia coli |
7.1.1.3 | R80Q | the mutation causes loss of a diagnostic peak for low-spin heme b in the 77 K redox difference spectrum | Escherichia coli |
7.1.1.3 | Y173F | the mutant possesses 91% copper and 108% cytochrome o compared to the wild type enzyme | Escherichia coli |
7.1.1.3 | Y288F | the mutations specifically eliminates the CuB center from the oxidase complex | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
7.1.1.3 | cytoplasmic membrane | - |
Escherichia coli | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
7.1.1.3 | copper | the enzyme contains CuB | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.1.1.3 | Escherichia coli | - |
- |
- |
7.1.1.3 | Escherichia coli ST4676 | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.1.1.3 | ubiquinol-1 + O2 + H+/in | - |
Escherichia coli | ubiquinone-1 + H2O + H+/out | - |
? | |
7.1.1.3 | ubiquinol-1 + O2 + H+/in | - |
Escherichia coli ST4676 | ubiquinone-1 + H2O + H+/out | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
7.1.1.3 | bo-type ubiquinol oxidase | - |
Escherichia coli |
7.1.1.3 | cytochrome bo | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
7.1.1.3 | heme | low-spin heme b and high-spin heme o | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
7.1.1.3 | physiological function | cytochrome bo is a four-subunit quinol oxidase in the aerobic respiratory chain of Escherichia coli and functions as a redox-coupled proton pump | Escherichia coli |