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Literature summary extracted from

  • Ma, K.; Linder, D.; Stetter, K.O.; Thauer, R.K.
    Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri (1991), Arch. Microbiol., 155, 593-600.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.5.98.2 phosphate maximal stimulation (100fold) at 2.5 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective Methanopyrus kandleri
1.5.98.2 phosphate maximal stimulation (5-6fold) at 1 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective Methanothermobacter marburgensis
1.5.98.2 phosphate maximal stimulation at 2.5 M. Sodium-, potassium-, and ammonium salts are equally effective Methanopyrus kandleri
1.5.98.2 sulfate maximal stimulation (100fold) at 2.2 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective Methanopyrus kandleri
1.5.98.2 sulfate maximal stimulation (5-6fold) at 1 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective Methanothermobacter marburgensis
1.5.98.2 sulfate maximal stimulation at 2.2 M. Sodium-, potassium-, and ammonium salts are equally effective Methanopyrus kandleri

General Stability

EC Number General Stability Organism
1.5.98.2 efficiency of salts in protecting the reductase from inactivation decreased in the following order: K2HPO4, KCl, (NH4)2SO4, NH4Cl, Na2HPO4, NaCl Methanopyrus kandleri
1.5.98.2 is of less importance Methanopyrus kandleri
1.5.98.2 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
1.5.98.2 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

EC Number Inhibitors Comment Organism Structure
1.5.98.2 phosphate
-
 Methanosarcina barkeri
1.5.98.2 sulfate
-
 Methanosarcina barkeri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.98.2 0.0037
-
 reduced coenzyme F420 65°C, pH 6.8 Methanopyrus kandleri
1.5.98.2 0.004
-
 reduced coenzyme F420 pH 6.8, 65°C Methanopyrus kandleri
1.5.98.2 0.006
-
 N5,N10-methylenetetrahydromethanopterin 65°C, pH 6.8 Methanopyrus kandleri
1.5.98.2 0.006
-
 5,10-methylenetetrahydromethanopterin pH 6.8, 65°C Methanopyrus kandleri

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.98.2 cytoplasm
-
 Methanopyrus kandleri 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.98.2 38000
-
 x * 38000, SDS-PAGE Methanopyrus kandleri
1.5.98.2 38000
-
 8 * 38000, SDS-PAGE Methanopyrus kandleri
1.5.98.2 300000
-
 gel filtration Methanopyrus kandleri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.98.2 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 Methanosarcina barkeri the enzyme is involved in methanogenesis from CO2 5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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

EC Number Organism UniProt Comment Textmining
1.5.98.2 Methanopyrus kandleri Q8TXY4
-
-
1.5.98.2 Methanopyrus kandleri DSM 6324 Q8TXY4
-
-
1.5.98.2 Methanosarcina barkeri
-
-
-
1.5.98.2 Methanothermobacter marburgensis Q50744
-
-
1.5.98.2 Methanothermobacter marburgensis DSM 2133 Q50744
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.5.98.2 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)

EC Number Purification (Comment) Organism
1.5.98.2
-
 Methanosarcina barkeri
1.5.98.2
-
 Methanopyrus kandleri
1.5.98.2
-
 Methanothermobacter marburgensis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.98.2 290
-
 65°C, pH 6.8 Methanopyrus kandleri
1.5.98.2 290
-
 pH 6.8, 65°C Methanopyrus kandleri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.98.2 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
 Methanosarcina barkeri 5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
 ?
1.5.98.2 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 the enzyme is involved in methanogenesis from CO2 Methanosarcina barkeri 5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
 Methanothermobacter marburgensis 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 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
-
 ?
1.5.98.2 N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
 Methanothermobacter marburgensis DSM 2133 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
 ?
1.5.98.2 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

EC Number Subunits Comment Organism
1.5.98.2 ? x * 38000, SDS-PAGE Methanopyrus kandleri
1.5.98.2 octamer 8 * 38000, SDS-PAGE Methanopyrus kandleri

Synonyms

EC Number Synonyms Comment Organism
1.5.98.2 MK0524 locus name Methanopyrus kandleri
1.5.98.2 MTBMA_c03270 locus name Methanothermobacter marburgensis
1.5.98.2 N5,N10-methylenetetrahydromethanopterin reductase
-
 Methanosarcina barkeri
1.5.98.2 N5,N10-methylenetetrahydromethanopterin reductase
-
 Methanopyrus kandleri
1.5.98.2 N5,N10-methylenetetrahydromethanopterin reductase
-
 Methanothermobacter marburgensis
1.5.98.2 N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
-
 Methanosarcina barkeri
1.5.98.2 N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
-
 Methanopyrus kandleri
1.5.98.2 N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
-
 Methanothermobacter marburgensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.98.2 65
-
-
 Methanopyrus kandleri
1.5.98.2 65
-
 assay at Methanopyrus kandleri

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.98.2 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.98.2 275
-
 reduced coenzyme F420 65°C, pH 6.8 Methanopyrus kandleri
1.5.98.2 275
-
 N5,N10-methylenetetrahydromethanopterin 65°C, pH 6.8 Methanopyrus kandleri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.98.2 6.5 7
-
 Methanopyrus kandleri
1.5.98.2 6.5 7 determined at 65°C Methanopyrus kandleri

General Information

EC Number General Information Comment Organism
1.5.98.2 physiological function the enzyme is involved in methanogenesis from CO2 Methanosarcina barkeri
1.5.98.2 physiological function the enzyme is involved in methanogenesis from CO2 Methanopyrus kandleri
1.5.98.2 physiological function the enzyme is involved in methanogenesis from CO2 Methanothermobacter marburgensis