EC Number | Crystallization (Comment) | Organism |
---|---|---|
7.1.1.3 | hanging drop vapor diffusion method, using 9-10% (w/v) PEG 1500, 100 mM NaCl, 100 mM MgCl2 and 5% (v/v) ethanol | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
7.1.1.3 | D75N | the mutation inhibits activity by 99% | Escherichia coli |
7.1.1.3 | H98N | the mutation inhibits activity by 97% | Escherichia coli |
7.1.1.3 | Q101N | the mutation inhibits activity by 75% and causes a 10fold increase in the apparent KM for ubiquinol-1 | Escherichia coli |
7.1.1.3 | R71L | the mutation inhibits activity by 99% | Escherichia coli |
7.1.1.3 | R71Q | the mutation inhibits activity by 99% | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
7.1.1.3 | 0.018 | - |
ubiquinol-1 | wild type enzyme, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C | Escherichia coli | |
7.1.1.3 | 0.023 | - |
ubiquinol-1 | mutant enzyme Q101N, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C | Escherichia coli | |
7.1.1.3 | 0.024 | - |
ubiquinol-1 | mutant enzyme Q101N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C | Escherichia coli | |
7.1.1.3 | 0.045 | - |
ubiquinol-1 | wild type enzyme, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C | Escherichia coli | |
7.1.1.3 | 0.175 | - |
ubiquinol-1 | mutant enzyme H98N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
7.1.1.3 | membrane | - |
Escherichia coli | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
7.1.1.3 | copper | the enzyme is a four-subunit heme-copper oxidase containing CuB | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.1.1.3 | Escherichia coli | P0ABJ1 | - |
- |
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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
7.1.1.3 | tetramer | x-ray crystallography | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
7.1.1.3 | cytochrome bo3 | - |
Escherichia coli |
7.1.1.3 | ubiquinol oxidase | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
7.1.1.3 | heme | heme b and heme o3 | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
7.1.1.3 | physiological function | cytochrome bo3 ubiquinol oxidase from Escherichia coli is a four-subunit heme-copper oxidase that catalyzes the four-electron reduction of O2 to water and functions as a proton pump | Escherichia coli |