Any feedback?
Literature summary for 1.1.98.4 extracted from
- F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters (1994), Eur. J. Biochem., 223, 503-511.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.05 | - |
reduced coenzyme F420 | pH 8.0, 65°C | Archaeoglobus fulgidus |  |
| 0.19 | - |
2,3-dimethyl-1,4-naphthoquinone | pH 8.0, 65°C | Archaeoglobus fulgidus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Archaeoglobus fulgidus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron-sulfur cluster | the purified complex contains 9 mol non-heme iron and 7 mol acid-labile sulfur per mol of complex | Archaeoglobus fulgidus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 32000 | - |
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
| 33000 | - |
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
| 37000 | - |
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
| 39000 | - |
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
| 41000 | - |
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
| 45000 | - |
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
| 56000 | - |
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
| 270000 | - |
gel filtration, native PAGE | Archaeoglobus fulgidus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| menaquinone + reduced coenzyme F420 | Archaeoglobus fulgidus | the physiological electron acceptor of the enzyme complex is most likely the menaquinone found in the membrane fraction of Archaeoglobus fulgidus. The reduction of menaquinone by F420H2 in Archaeoglobus fulgidus is catalyzed by a membrane-bound complex composed of at least seven different subunits. It contains 1-2 mol FAD and8 mol Fe-S/mol complex. The complex subunit composition indicates that the F420H2:quinone oxidoreductase complex from Archaeoglobus fulgidus is functionally analogous to the NADH:quinone oxidoreductase complex from mitochondria and bacteria | menaquinol + oxidized coenzyme F420 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | - |
- |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| enzyme activity is almost stable in aerobic solutions. No activity is lost when 2 mg purified protein in 1 ml 50 mM Tricine/KOH, pH 7.5, containing 0.2% dodecyl-/I-D-maltoside is stored at 4°C for 6 h under air as the gas phase | Archaeoglobus fulgidus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,4-naphthoquinone + reduced coenzyme F420 | - |
Archaeoglobus fulgidus | 1,4-naphthoquinol + oxidized coenzyme F420 | - |
? | |
| 2,3-dimethoxy-5-methyl-1,4-benzoquinone + reduced coenzyme F420 | - |
Archaeoglobus fulgidus | 2,3-dimethoxy-5-methyl-1,4-benzoquinol + oxidized coenzyme F420 | - |
? | |
| 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + reduced coenzyme F420 | - |
Archaeoglobus fulgidus | 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol + oxidized coenzyme F420 | - |
? | |
| 2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420 | - |
Archaeoglobus fulgidus | 2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420 | - |
? | |
| 2-hydroxy-1,4-naphthoquinone + reduced coenzyme F420 | - |
Archaeoglobus fulgidus | 2-hydroxy-1,4-naphthoquinol + oxidized coenzyme F420 | - |
? | |
| 2-methyl-1,4-naphthoquinone + reduced coenzyme F420 | i.e. menadione | Archaeoglobus fulgidus | 2-methyl-1,4-naphthoquinol + oxidized coenzyme F420 | - |
? | |
| menaquinone + reduced coenzyme F420 | the physiological electron acceptor of the enzyme complex is most likely the menaquinone found in the membrane fraction of Archaeoglobus fulgidus. The reduction of menaquinone by F420H2 in Archaeoglobus fulgidus is catalyzed by a membrane-bound complex composed of at least seven different subunits. It contains 1-2 mol FAD and8 mol Fe-S/mol complex. The complex subunit composition indicates that the F420H2:quinone oxidoreductase complex from Archaeoglobus fulgidus is functionally analogous to the NADH:quinone oxidoreductase complex from mitochondria and bacteria | Archaeoglobus fulgidus | menaquinol + oxidized coenzyme F420 | - |
? | |
| additional information | no activity with NADH and NADPH | Archaeoglobus fulgidus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| oligomer | x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides | Archaeoglobus fulgidus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| F420H2:quinone oxidoreductase complex | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
- |
Archaeoglobus fulgidus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 80 | 20°C: about 40% of maximal activity, 80°C: about 55% of maximal activity | Archaeoglobus fulgidus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
1 h, stable in presence of 1 M (NH4)2SO4, in the presence of 1 M K2HPO (pH 8) only 60% activity is recovered | Archaeoglobus fulgidus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Archaeoglobus fulgidus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the purified complex contains 1.6 mol FAD per mol of complex | Archaeoglobus fulgidus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme is involved in energy conservation during growth on lactate plus sulfate | Archaeoglobus fulgidus |
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
