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Literature summary for 1.8.98.5 extracted from
- Process of energy conservation in the extremely haloalkaliphilic methyl-reducing methanogen Methanonatronarchaeum thermophilum (2022), FEBS J., 289, 549-563 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition of HdrDE and VhoGAC by diphenyleneiodonium chloride | Methanonatronarchaeum thermophilum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | the catalytic subunit of heterodisulfide reductase (HdrD) is located at the cytoplasmic side of the cytoplasmic membrane. The oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC) | Methanonatronarchaeum thermophilum | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| KCl | activates HdrDE activity, best at 3 M KCl, about 50% activity at 2 and 4 M KCl | Methanonatronarchaeum thermophilum |  |
| additional information | at pH 7.5, the specific activity of HdrDE with 2 M potassium chloride is about 40% higher than with 2 M sodium chloride | Methanonatronarchaeum thermophilum | |
| NaCl | activates VhoGAC activity, highest activity at 1 M | Methanonatronarchaeum thermophilum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | Methanonatronarchaeum thermophilum | - |
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | Methanonatronarchaeum thermophilum AMET1 | - |
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanonatronarchaeum thermophilum | A0A1Y3GAE7 | CoB-CoM heterodisulfide reductase subunit E; isolated from a hypersaline soda lake | - |
| Methanonatronarchaeum thermophilum AMET1 | A0A1Y3GAE7 | CoB-CoM heterodisulfide reductase subunit E; isolated from a hypersaline soda lake | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | Methanonatronarchaeum thermophilum strain AMET1 is able to grow on all tested substrates (methanol, trimethylamine (TMA), dimethylamine (DMA), monomethylamine (MMA)) in combination with formate or molecular hydrogen | Methanonatronarchaeum thermophilum | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 3.4 | - |
CoM-S-S-CoB reduction with methyl viologen as artificial electron donor by HdrDE, membrane fraction, pH 8.5, temperature not specified in the publication, at 2 M KCl | Methanonatronarchaeum thermophilum |
| 10.7 | - |
CoM-S-S-CoB reduction with methyl viologen as artificial electron donor by HdrDE, membrane fraction, pH 7.5, temperature not specified in the publication, at 2 M KCl | Methanonatronarchaeum thermophilum |
| 20.1 | - |
VhoGAC activity on H2 with methyl viologen as artificial electron acceptor, membrane fraction, pH 9.5, temperature not specified in the publication, at 2 M NaCl | Methanonatronarchaeum thermophilum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
Methanonatronarchaeum thermophilum | 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1 | Methanonatronarchaeum thermophilum | 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
Methanonatronarchaeum thermophilum AMET1 | 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1 | Methanonatronarchaeum thermophilum AMET1 | 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| H2: CoM-S-S-CoB oxidoreductase | - |
Methanonatronarchaeum thermophilum |
| HdrDE | - |
Methanonatronarchaeum thermophilum |
| HdrDE-VhoGAC | - |
Methanonatronarchaeum thermophilum |
| heterodisulfide reductase | - |
Methanonatronarchaeum thermophilum |
| More | see also EC 1.8.98.6 | Methanonatronarchaeum thermophilum |
| VhoGAC | - |
Methanonatronarchaeum thermophilum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
HdrDE activity | Methanonatronarchaeum thermophilum |
| 9.5 | - |
VhoGAC activity | Methanonatronarchaeum thermophilum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 10.5 | enzyme activity range, profile overview | Methanonatronarchaeum thermophilum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Ferredoxin | - |
Methanonatronarchaeum thermophilum | |
| additional information | a methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1 | Methanonatronarchaeum thermophilum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the oxidation of formate is catalyzed by a membrane-bound formate dehydrogenase (FdhGHI), whereas the oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC). Based on this, the electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system, overview. Three energy-conserving, membrane-bound electron transport systems are known in methanogens: (a) H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.5), (b) coenzyme F420H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.4), and (c) reduced ferredoxin:CoM-S-S-CoB oxidoreductase (EC 1.8.7.3) | Methanonatronarchaeum thermophilum |
| physiological function | the energy conservation of Methanonatronarchaeum thermophilum is dependent on a respiratory chain consisting of a hydrogenase (VhoGAC, EC 1.8.98.5), a formate dehydrogenase (FdhGHI, EC 1.8.98.6), and a heterodisulfide reductase (HdrDE) that are well adapted to the harsh physicochemical conditions in the natural habitat. Methanogen Methanonatronarchaeum thermophilum is an extremely haloalkaliphilic and moderately thermophilic archaeon. A methanophenazine-like cofactor might function as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase. A methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1. The electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system | Methanonatronarchaeum thermophilum |
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Release 2023.1 (January 2023)
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