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show all sequences of 1.5.98.2

Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri

Ma, K.; Linder, D.; Stetter, K.O.; Thauer, R.K.; Arch. Microbiol. 155, 593-600 (1991)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
phosphate
maximal stimulation (100fold) at 2.5 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective; maximal stimulation at 2.5 M. Sodium-, potassium-, and ammonium salts 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
sulfate
maximal stimulation (100fold) at 2.2 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective; maximal stimulation at 2.2 M. Sodium-, potassium-, and ammonium salts 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
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
Commentary
Organism
Structure
phosphate
-
Methanosarcina barkeri
sulfate
-
Methanosarcina barkeri
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
-
5,10-methylenetetrahydromethanopterin
pH 6.8, 65°C
Methanopyrus kandleri
0.006
-
N5,N10-methylenetetrahydromethanopterin
65°C, pH 6.8
Methanopyrus kandleri
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Methanopyrus kandleri
5737
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38000
-
8 * 38000, SDS-PAGE; x * 38000, SDS-PAGE
Methanopyrus kandleri
300000
-
gel filtration
Methanopyrus kandleri
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina barkeri
-
-
-
Methanothermobacter marburgensis
Q50744
-
-
Methanothermobacter marburgensis DSM 2133
Q50744
-
-
Methanopyrus kandleri
Q8TXY4
-
-
Methanopyrus kandleri DSM 6324
Q8TXY4
-
-
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)
Commentary
Organism
-
Methanopyrus kandleri
-
Methanosarcina barkeri
-
Methanothermobacter marburgensis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
290
-
65°C, pH 6.8; pH 6.8, 65°C
Methanopyrus kandleri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
726826
Methanosarcina barkeri
5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
the enzyme is involved in methanogenesis from CO2
726826
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
726826
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
726826
Methanopyrus kandleri DSM 6324
5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
726826
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
726826
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
726826
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
726826
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
726826
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
726826
Methanopyrus kandleri DSM 6324
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
726826
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
726826
Methanothermobacter marburgensis DSM 2133
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 38000, SDS-PAGE
Methanopyrus kandleri
octamer
8 * 38000, SDS-PAGE
Methanopyrus kandleri
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
; assay at
Methanopyrus kandleri
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
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
Commentary
Organism
Structure
275
-
N5,N10-methylenetetrahydromethanopterin
65°C, pH 6.8
Methanopyrus kandleri
275
-
reduced coenzyme F420
65°C, pH 6.8
Methanopyrus kandleri
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
; determined at 65°C
Methanopyrus kandleri
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
phosphate
maximal stimulation (100fold) at 2.5 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective; maximal stimulation at 2.5 M. Sodium-, potassium-, and ammonium salts 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
sulfate
maximal stimulation (100fold) at 2.2 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective; maximal stimulation at 2.2 M. Sodium-, potassium-, and ammonium salts 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
General Stability (protein specific)
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 (protein specific)
Inhibitors
Commentary
Organism
Structure
phosphate
-
Methanosarcina barkeri
sulfate
-
Methanosarcina barkeri
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
-
5,10-methylenetetrahydromethanopterin
pH 6.8, 65°C
Methanopyrus kandleri
0.006
-
N5,N10-methylenetetrahydromethanopterin
65°C, pH 6.8
Methanopyrus kandleri
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Methanopyrus kandleri
5737
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38000
-
8 * 38000, SDS-PAGE; x * 38000, SDS-PAGE
Methanopyrus kandleri
300000
-
gel filtration
Methanopyrus kandleri
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Oxidation Stability (protein specific)
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) (protein specific)
Commentary
Organism
-
Methanopyrus kandleri
-
Methanosarcina barkeri
-
Methanothermobacter marburgensis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
290
-
65°C, pH 6.8; pH 6.8, 65°C
Methanopyrus kandleri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
726826
Methanosarcina barkeri
5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
the enzyme is involved in methanogenesis from CO2
726826
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
726826
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
726826
Methanopyrus kandleri DSM 6324
5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
726826
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
726826
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
726826
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
726826
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
726826
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
726826
Methanopyrus kandleri DSM 6324
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
-
726826
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
726826
Methanothermobacter marburgensis DSM 2133
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 38000, SDS-PAGE
Methanopyrus kandleri
octamer
8 * 38000, SDS-PAGE
Methanopyrus kandleri
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
; assay at
Methanopyrus kandleri
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
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] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
275
-
N5,N10-methylenetetrahydromethanopterin
65°C, pH 6.8
Methanopyrus kandleri
275
-
reduced coenzyme F420
65°C, pH 6.8
Methanopyrus kandleri
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
; determined at 65°C
Methanopyrus kandleri
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in methanogenesis from CO2
Methanopyrus kandleri
physiological function
the enzyme is involved in methanogenesis from CO2
Methanosarcina barkeri
physiological function
the enzyme is involved in methanogenesis from CO2
Methanothermobacter marburgensis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in methanogenesis from CO2
Methanopyrus kandleri
physiological function
the enzyme is involved in methanogenesis from CO2
Methanosarcina barkeri
physiological function
the enzyme is involved in methanogenesis from CO2
Methanothermobacter marburgensis
Other publictions for EC 1.5.98.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
687420
Hendrickson
Roles of coenzyme F420-reducin ...
Methanococcus maripaludis
J. Bacteriol.
190
4818-4821
2008
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2
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1
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1
-
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-
-
-
-
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1
-
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-
-
-
-
1
-
-
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-
-
-
-
-
-
1
-
-
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
288531
Shima
Structure of coenzyme F(420) d ...
Methanopyrus kandleri, Methanothermobacter thermautotrophicus
J. Mol. Biol.
300
935-950
2000
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2
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2
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2
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2
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2
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721443
Vorholt
Pathways of autotrophic CO2 fi ...
Ferroglobus placidus, Ferroglobus placidus DSM 10642
Arch. Microbiol.
167
19-23
1997
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2
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1
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1
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1
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1
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1
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1
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1
1
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288528
Vaupel
Coenzyme F420-dependent N5,N10 ...
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
Eur. J. Biochem.
231
773-778
1995
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36
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288530
Nolling
Cloning, sequencing, and growt ...
Methanopyrus kandleri
J. Bacteriol.
177
7238-7244
1995
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1
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1
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721441
Vornolt
-
Enzymes and coenzymes of the c ...
Archaeoglobus fulgidus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus, Archaeoglobus profundus DSM 5631
Arch. Microbiol.
163
112-118
1995
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5
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3
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3
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3
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3
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3
3
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288527
Kunow
Si-face stereospecificity at C ...
Archaeoglobus fulgidus
Eur. J. Biochem.
214
641-646
1993
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288524
te Brommelstroet
Purification and properties of ...
Methanosarcina barkeri
Biochim. Biophys. Acta
1079
293-302
1991
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288526
Rospert
Methyl-coenzyme M reductase an ...
Methanopyrus kandleri
Arch. Microbiol.
156
49-55
1991
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2
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4
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726826
Ma
Purification and properties of ...
Methanopyrus kandleri, Methanopyrus kandleri DSM 6324, Methanosarcina barkeri, Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133
Arch. Microbiol.
155
593-600
1991
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4
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1
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3
3
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288523
Ma
Purification and properties of ...
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
Eur. J. Biochem.
191
187-193
1990
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4
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31
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288525
te Brommelstroet
Purification and properties of ...
Methanothermobacter thermautotrophicus
J. Biol. Chem.
265
1852-1857
1990
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288529
Ma
Single step purification of me ...
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
FEBS Lett.
268
59-62
1990
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31
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