Any feedback?
Literature summary extracted from
- Characterization of a quinole-oxidase activity in crude extracts of Thermoplasma acidophilum and isolation of an 18-kDa cytochrome (1991), Eur. J. Biochem., 200, 215-222 .
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 7.1.1.5 | addition of total lipids from Thermoplasma acidophilum increases stability | Thermoplasma acidophilum |
| 7.1.1.5 | asolectin from soya beans decreases stability | Thermoplasma acidophilum |
| 7.1.1.5 | stability is lowered by the presence of detergent | Thermoplasma acidophilum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.5 | 2-hydroxy-3-undecyl-1,4-naphthoquinone | 0.01 mM, 20% inhibition | Thermoplasma acidophilum |  |
| 7.1.1.5 | 2n-heptyl-4-hydroxyquinoline N-oxide | most potent inhibitor | Thermoplasma acidophilum | |
| 7.1.1.5 | asolectin | - |
Thermoplasma acidophilum | |
| 7.1.1.5 | Lipid | addition of total lipids from Thermoplasma acidophilum decreases activity | Thermoplasma acidophilum | |
| 7.1.1.5 | additional information | antimycin A, myxothiazol, methyl 3-methoxy-2-(2-styrylphenyl) propenate and stigmatellin (at concentration up to 0.030 mM) and Zn2+ at a concentration up to 1 mM, do not inhibit | Thermoplasma acidophilum |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.5 | 0.018 | - |
ubiquinol-10 | pH 5.4, 50°C | Thermoplasma acidophilum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.1.1.5 | membrane | - |
Thermoplasma acidophilum | 16020 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.5 | 150000 | - |
gel filtration | Thermoplasma acidophilum |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.5 | thermoplasmaquinol + O2 + H+[side 1] | Thermoplasma acidophilum | likely candidate to the physiological electron donor | thermoplasmaquinone + H2O + H+[side 2] | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.5 | Thermoplasma acidophilum | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.1.1.5 | - |
Thermoplasma acidophilum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.5 | 2,3-dimethylnaphthohydroquinone + O2 + H+[side 1] | - |
Thermoplasma acidophilum | ? | - |
? | |
| 7.1.1.5 | menadione + O2 + H+[side 1] | - |
Thermoplasma acidophilum | ? | - |
? | |
| 7.1.1.5 | menaquinol-4 + O2 + H+[side 1] | menaquinols are oxidized at 6-12fold higher rates than ubiquinols | Thermoplasma acidophilum | menaquinone-4 + H2O + H+[side 2] | - |
? | |
| 7.1.1.5 | thermoplasmaquinol + O2 + H+[side 1] | likely candidate to the physiological electron donor | Thermoplasma acidophilum | thermoplasmaquinone + H2O + H+[side 2] | - |
? | |
| 7.1.1.5 | ubiquinol-1 + O2 + H+[side 1] | - |
Thermoplasma acidophilum | ubiquinone-1 + H2O + H+[side 2] | - |
? | |
| 7.1.1.5 | ubiquinol-10 + O2 + H+[side 1] | menaquinols are oxidized at 6-12fold higher rates than ubiquinols. However, because of the greater tendency for autoxidation of menaquinols, ubiquinol is a more convenient substrate for the enzyme assay | Thermoplasma acidophilum | ubiquinone-10 + H2O + H+[side 2] | - |
? | |
| 7.1.1.5 | ubiquinol-6 + O2 + H+[side 1] | - |
Thermoplasma acidophilum | ubiquinone-6 + H2O + H+[side 2] | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.5 | oligomer | 12-16 * 14000, SDS-PAGE | Thermoplasma acidophilum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.1.5 | Q10H2 oxidase | - |
Thermoplasma acidophilum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.5 | 50 | - |
- |
Thermoplasma acidophilum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.5 | 5.4 | - |
- |
Thermoplasma acidophilum |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.5 | cytochrome | cytochrome-o-type quinol oxidase | Thermoplasma acidophilum |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.5 | 0.00015 | - |
2n-heptyl-4-hydroxyquinoline N-oxide | pH 5.4, 50°C | Thermoplasma acidophilum | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
