Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Yap, L.L.; Lin, M.T.; Ouyang, H.; Samoilova, R.I.; Dikanov, S.A.; Gennis, R.B.
    The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli (2010), Biochim. Biophys. Acta, 1797, 1924-1932.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.10.3.11 D188A site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme, The mutant oxidase is not able to support aerobic growth when expressed in a strain of Escherichia coli without a genomically encoded respiratory oxidase Escherichia coli
1.10.3.11 D188N site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme Escherichia coli
1.10.3.11 D75E site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows similar activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 D75H site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 D75N site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 D75R site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 H98N site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 H98S site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 H98S site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-100 compared to the wild-type enzyme Escherichia coli
1.10.3.11 H98T site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 Q101N site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 R257Q site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme. The mutant oxidase is not able to support aerobic growth when expressed in a strain of Escherichia coli without a genomically encoded respiratory oxidase Escherichia coli
1.10.3.11 R71D site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 R71D/D75R site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 R71K site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 R71Q site-directed mutagenesis at the QH-site of cytochrome bo3, the mutant shows highly reduced enzyme activity compared to the wild-type enzyme Escherichia coli
1.10.3.11 WI36A site-directed mutagenesis, the mutant shows altered sensitivity to inhibitor aurachin C1-10 compared to the wild-type enzyme Escherichia coli
7.1.1.3 D75E 135% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 D75H 4% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 D75N inactive Escherichia coli
7.1.1.3 D75R inactive Escherichia coli
7.1.1.3 H98N 1% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 H98S 2% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 H98T 1% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 Q101N 5% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 R71D inactive Escherichia coli
7.1.1.3 R71D/D75R inactive Escherichia coli
7.1.1.3 R71K inactive Escherichia coli
7.1.1.3 R71Q inactive Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.11 2-heptyl-4-hydroxyquinoline N-oxide i.e. HQNO, binds stoichiometrically to the enzyme and prevents formation of the ubisemiquinone at the QH-site, but does not displace the ubiquinone-8 bound at the QH-site, enzyme binding kineticss, overview Escherichia coli
1.10.3.11 aurachin C1-10 prevents formation of the ubisemiquinone at the QH-site, but appears to compete for quinol binding at the QL-site, enzyme binding kineticss, overview Escherichia coli
1.10.3.11 additional information presence of high affinity inhibitors, 2-heptyl-4-hydroxyquinoline N-oxide and aurachin C1–10, does not displace ubiquinone-8 from the QH site Escherichia coli
7.1.1.3 2-heptyl-4-hydroxyquinoline N-oxide
-
 Escherichia coli
7.1.1.3 aurachin C1-10 competitive inhibitor Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.3 0.052
-
 ubiquinol-1 mutant enzyme D188N, at 37°C, pH 7.0 Escherichia coli
7.1.1.3 0.053
-
 ubiquinol-1 wild type enzyme, at 37°C, pH 7.0 Escherichia coli
7.1.1.3 0.056
-
 ubiquinol-1 mutant enzyme D188A, at 37°C, pH 7.0 Escherichia coli
7.1.1.3 0.06
-
 ubiquinol-1 mutant enzyme R257Q, at 37°C, pH 7.0 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.10.3.11 membrane cytochrome bo3 is the major respiratory oxidase located in the cytoplasmic membrane of Escherichia coli when grown under high oxygen tension Escherichia coli 16020
-
7.1.1.3 cytoplasmic membrane
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.11 Fe2+ heme iron Escherichia coli
7.1.1.3 Cu copper-containing enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.10.3.11 2 ubiquinol + O2 Escherichia coli
-
 2 ubiquinone + 2 H2O
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.3 Ni-NTA column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.11 2 ubiquinol + O2
-
 Escherichia coli 2 ubiquinone + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-8 + O2 the quinone bound at the QH site can form a stable semiquinone. The tightly bound ubiquinone-8 at the QH site is not displaced by ubiquinol-1 even during enzyme turnover Escherichia coli 2 ubiquinone-8 + 2 H2O
-
 ?
1.10.3.11 additional information two assay methods: a coupled assay with rat liver DT-diaphorase and NADH as the reductant, and a direct assay using a oxygen electrode, overview Escherichia coli ?
-
 ?
7.1.1.3 ubiquinol-1 + O2 + H+/in
-
 Escherichia coli ubiquinone-1 + H2O + H+/out
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.11 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.11 7
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.3 heme heme b and heme o3 Escherichia coli
7.1.1.3 ubiquinone-8 the enzyme contains one equivalent of ubiquinone-8 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.10.3.11 0.000015
-
 aurachin C1-10 pH 7.0, 37°C, wild-type enzyme Escherichia coli
1.10.3.11 0.000074
-
 2-heptyl-4-hydroxyquinoline N-oxide pH 7.0, 37°C, wild-type enzyme Escherichia coli
7.1.1.3 0.000012
-
 aurachin C1-10 mutant enzyme R257Q, at 37°C, pH 7.0 Escherichia coli
7.1.1.3 0.000015
-
 aurachin C1-10 wild type enzyme, at 37°C, pH 7.0 Escherichia coli
7.1.1.3 0.000025
-
 aurachin C1-10 mutant enzyme D188A, at 37°C, pH 7.0 Escherichia coli
7.1.1.3 0.00074
-
 2-heptyl-4-hydroxyquinoline N-oxide wild type enzyme, at 37°C, pH 7.0 Escherichia coli

General Information

EC Number General Information Comment Organism
1.10.3.11 additional information analysis of a one-site Q-site model and a two-site Q-site model, overview Escherichia coli
1.10.3.11 physiological function cytochrome bo3 oxidase catalyzes the 2-electron oxidation of ubiquinol-8 and the 4-electron reduction of dioxygen to water Escherichia coli