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Literature summary for 1.5.98.2 extracted from
- Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri (1991), Arch. Microbiol., 155, 593-600.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phosphate | maximal stimulation (100fold) at 2.5 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective | Methanopyrus kandleri |  |
| phosphate | maximal stimulation (5-6fold) at 1 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective | Methanothermobacter marburgensis | |
| phosphate | maximal stimulation at 2.5 M. Sodium-, potassium-, and ammonium salts are equally effective | Methanopyrus kandleri | |
| sulfate | maximal stimulation (100fold) at 2.2 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective | Methanopyrus kandleri | |
| sulfate | maximal stimulation (5-6fold) at 1 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective | Methanothermobacter marburgensis | |
| sulfate | maximal stimulation at 2.2 M. Sodium-, potassium-, and ammonium salts are equally effective | Methanopyrus kandleri | |
General Stability
| General Stability | Organism |
|---|---|
| efficiency of salts in protecting the reductase from inactivation decreased in the following order: K2HPO4, KCl, (NH4)2SO4, NH4Cl, Na2HPO4, NaCl | Methanopyrus kandleri |
| is of less importance | Methanopyrus kandleri |
| salt concentrations between 0.1 M and 1.5 M are required for maximal stability. Potassium salts are more effective than ammonium salts, and the latter more effective than sodium salts in stabilizing the enzyme activity. The anion | Methanopyrus kandleri |
| thermostability of the reductase is very low in the absence of salts. In their presence, however, the reductase is highly thermostable. Salt concentrations between 0.1 M and 1.5 M are required for maximal stability. Potassium salts prove more effective than ammonium salts | Methanopyrus kandleri |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| phosphate | - |
Methanosarcina barkeri | |
| sulfate | - |
Methanosarcina barkeri | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0037 | - |
reduced coenzyme F420 | 65°C, pH 6.8 | Methanopyrus kandleri | |
| 0.004 | - |
reduced coenzyme F420 | pH 6.8, 65°C | Methanopyrus kandleri | |
| 0.006 | - |
N5,N10-methylenetetrahydromethanopterin | 65°C, pH 6.8 | Methanopyrus kandleri | |
| 0.006 | - |
5,10-methylenetetrahydromethanopterin | pH 6.8, 65°C | Methanopyrus kandleri | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | - |
Methanopyrus kandleri | 5737 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 38000 | - |
x * 38000, SDS-PAGE | Methanopyrus kandleri |
| 38000 | - |
8 * 38000, SDS-PAGE | Methanopyrus kandleri |
| 300000 | - |
gel filtration | Methanopyrus kandleri |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 | Methanosarcina barkeri | the enzyme is involved in methanogenesis from CO2 | 5-methyltetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | Methanopyrus kandleri | the enzyme is involved in methanogenesis from CO2 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | Methanothermobacter marburgensis | the enzyme is involved in methanogenesis from CO2 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | Methanopyrus kandleri DSM 6324 | the enzyme is involved in methanogenesis from CO2 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | Methanothermobacter marburgensis DSM 2133 | the enzyme is involved in methanogenesis from CO2 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanopyrus kandleri | Q8TXY4 | - |
- |
| Methanopyrus kandleri DSM 6324 | Q8TXY4 | - |
- |
| Methanosarcina barkeri | - |
- |
- |
| Methanothermobacter marburgensis | Q50744 | - |
- |
| Methanothermobacter marburgensis DSM 2133 | Q50744 | - |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| under aerobic conditions at 4°C approximately 20% activity is lost within 24 h. Under anaerobic conditions only 10% activity is lost | Methanopyrus kandleri |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanosarcina barkeri |
- |
Methanopyrus kandleri |
- |
Methanothermobacter marburgensis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 290 | - |
65°C, pH 6.8 | Methanopyrus kandleri |
| 290 | - |
pH 6.8, 65°C | Methanopyrus kandleri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 | - |
Methanosarcina barkeri | 5-methyltetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the enzyme is involved in methanogenesis from CO2 | Methanosarcina barkeri | 5-methyltetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the reductase is specific for reduced coenzyme F420 as electron donor. NADH, NADPH or reduced dyes can not substitute for the 5-deazaflavin | Methanopyrus kandleri | 5-methyltetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the reductase is specific for reduced coenzyme F420 as electron donor. NADH, NADPH or reduced dyes can not substitute for the 5-deazaflavin | Methanopyrus kandleri DSM 6324 | 5-methyltetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | - |
Methanothermobacter marburgensis | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the enzyme is involved in methanogenesis from CO2 | Methanopyrus kandleri | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the enzyme is involved in methanogenesis from CO2 | Methanothermobacter marburgensis | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the enzyme is specific for reduced coenzyme F420. Ternary complex mechanism | Methanopyrus kandleri | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the enzyme is involved in methanogenesis from CO2 | Methanopyrus kandleri DSM 6324 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the enzyme is specific for reduced coenzyme F420. Ternary complex mechanism | Methanopyrus kandleri DSM 6324 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | - |
Methanothermobacter marburgensis DSM 2133 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
| N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 | the enzyme is involved in methanogenesis from CO2 | Methanothermobacter marburgensis DSM 2133 | 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 38000, SDS-PAGE | Methanopyrus kandleri |
| octamer | 8 * 38000, SDS-PAGE | Methanopyrus kandleri |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MK0524 | locus name | Methanopyrus kandleri |
| MTBMA_c03270 | locus name | Methanothermobacter marburgensis |
| N5,N10-methylenetetrahydromethanopterin reductase | - |
Methanosarcina barkeri |
| N5,N10-methylenetetrahydromethanopterin reductase | - |
Methanopyrus kandleri |
| N5,N10-methylenetetrahydromethanopterin reductase | - |
Methanothermobacter marburgensis |
| N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) | - |
Methanosarcina barkeri |
| N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) | - |
Methanopyrus kandleri |
| N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) | - |
Methanothermobacter marburgensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
- |
Methanopyrus kandleri |
| 65 | - |
assay at | Methanopyrus kandleri |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 90 | - |
the enzyme is completely inactivated within a few min when incubated in 100 mM Tris/HCl pH 6.8. The rate of inactivation decreases with increasing potassium phosphate concentrations. At 100 mM potassium phosphate complete thermostability for 60 min is reached | Methanopyrus kandleri |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 275 | - |
reduced coenzyme F420 | 65°C, pH 6.8 | Methanopyrus kandleri | |
| 275 | - |
N5,N10-methylenetetrahydromethanopterin | 65°C, pH 6.8 | Methanopyrus kandleri | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7 | - |
Methanopyrus kandleri |
| 6.5 | 7 | determined at 65°C | Methanopyrus kandleri |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme is involved in methanogenesis from CO2 | Methanosarcina barkeri |
| physiological function | the enzyme is involved in methanogenesis from CO2 | Methanopyrus kandleri |
| physiological function | the enzyme is involved in methanogenesis from CO2 | Methanothermobacter marburgensis |
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