BRENDA - Enzyme Database show
show all sequences of 1.2.7.1

The anabolic pyruvate oxidoreductase from Methanococcus maripaludis

Lin, W.C.; Yang, Y.L.; Whitman, W.B.; Arch. Microbiol. 179, 444-456 (2003)

Data extracted from this reference:

General Stability
General Stability
Organism
following dialysis, the enzyme is very unstable in the absence of glycerol or ethylene glycol, thiamine diphosphate and MgCl2 also help to maintain activity
Methanococcus maripaludis
Inhibitors
Inhibitors
Commentary
Organism
Structure
Dithionite
with 5 mM dithionite, the half-life is 7 h at 2 °C, with about 90% of the original activity being lost after 24 h
Methanococcus maripaludis
glyoxylate
20 mM, about 40% of the original activity is lost. 2 mM glyoxylate inhibits 6%
Methanococcus maripaludis
additional information
no substrate inhibition with CoA up to 0.1 mM. Slightly or not inhibited at all by glyoxylate, nitrite, CO or potential physiological effectors. Not inhibited by CO. Potential affectors such as ATP, ADP, AMP, cAMP, GTP, GDP, GMP, NAD+, NADH, and glyceraldehyde 3-phosphate, at concentrations of 2 mM, do not affect the activity
Methanococcus maripaludis
oxygen
-
Methanococcus maripaludis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0058
-
CoA
pH 8.6, 37°C
Methanococcus maripaludis
0.115
-
pyruvate
pH 8.6, 37°C
Methanococcus maripaludis
0.205
-
2-oxobutyrate
pH 8.6, 37°C
Methanococcus maripaludis
0.264
-
oxaloacetate
pH 8.6, 37°C
Methanococcus maripaludis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron-sulfur cluster
porE encodes the 21500 Da subunit that contains a high cysteinyl residue content and a motif indicative of a [Fe–S] cluster. Subunit porF also also has a high cysteinyl residue content, and two [Fe–S] cluster motifs. Based upon these results, it is proposed that PorE and PorF are components of a specialized system required to transfer low-potential electrons for pyruvate biosynthesis
Methanococcus maripaludis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
190000
-
-
Methanococcus maripaludis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanococcus maripaludis
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
Q9P9E5: subunit alpha, Q9P9E4: subunit beta, Q9P9E6: subunit gamma, Q9P9E7: subunit delta, Q9P9E3: subunit PorE
-
Methanococcus maripaludis DSM Z 2067
Q9P9E5 and Q9P9E4 and Q9P9E6 and Q9P9E7 and Q9P9E3
Q9P9E5: subunit alpha, Q9P9E4: subunit beta, Q9P9E6: subunit gamma, Q9P9E7: subunit delta, Q9P9E3: subunit PorE
-
Oxidation Stability
Oxidation Stability
Organism
the enzyme is very sensitive to O2. Following incubation in air at 2°C for 40 min, about 60% of enzyme activity is lost. The half-life is 5.2 min when the purified enzyme is exposed to air in an ice bath. After inactivation of the purified enzyme by oxygen, activity is not restored byreplacing the oxygen with nitrogen and adding 0.01 mM dithionite no activity is lost after dialysis of extract in a basic buffer containing 20 mM potassium Tricine, pH 8.6, 5 mM MgCl2, 0.5 mM dithiothreitol, 0.1 mM thiamine diphosphate, and 10% glycerol
Methanococcus maripaludis
Purification (Commentary)
Commentary
Organism
-
Methanococcus maripaludis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.3
-
pH 8.6, 37°C, substrate: indol-3-pyruvate
Methanococcus maripaludis
3.6
-
pH 8.6, 37°C, substrate: 2-oxobutyrate
Methanococcus maripaludis
6.5
-
pH 8.6, 37°C, substrate: oxaloacetate
Methanococcus maripaludis
7.4
-
pH 8.6, 37°C, substrate: pyruvate
Methanococcus maripaludis
Storage Stability
Storage Stability
Organism
-20°C, 3 weeks, anaerobic conditions, no loss of activity of the partially purified enzyme
Methanococcus maripaludis
2°C, 2 weeks, anaerobic conditions, no loss of activity
Methanococcus maripaludis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxobutyrate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
propanoyl-CoA + CO2 + reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
propanoyl-CoA + CO2 + reduced methyl viologen
-
-
-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
?
-
-
-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
?
-
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
?
-
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
?
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
the low molecular weight enzyme contains five polypeptides: 47000 Da (alpha), 33000 Da (beta), 25000 (gamma) and 13000 Da (gamma). The subunit stoichiometry for the alpha:beta:gamma:delta subunits is 1:1.08:0.90:1.32. In addition it contains a fifth polypeptide (21500 Da)
Methanococcus maripaludis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanococcus maripaludis
60
-
at pH 7.3, the temperature optimum is 60°C
Methanococcus maripaludis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
37
60
the activity detected at 60°C is five times the activity detected at 37°C
Methanococcus maripaludis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13
-
2-oxobutyrate
pH 8.6, 37°C
Methanococcus maripaludis
18
-
oxaloacetate
pH 8.6, 37°C
Methanococcus maripaludis
27
-
pyruvate
pH 8.6, 37°C
Methanococcus maripaludis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
at 37 °C, maximal activity is obtained at pH 7.3
Methanococcus maripaludis
8.6
-
assay at
Methanococcus maripaludis
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
it is possible that flavins play an important regulatory or structural role in the enzyme
Methanococcus maripaludis
FMN
it is possible that flavins play an important regulatory or structural role in the enzyme
Methanococcus maripaludis
additional information
the enzyme is not coenzyme F420-dependent
Methanococcus maripaludis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
it is possible that flavins play an important regulatory or structural role in the enzyme
Methanococcus maripaludis
FMN
it is possible that flavins play an important regulatory or structural role in the enzyme
Methanococcus maripaludis
additional information
the enzyme is not coenzyme F420-dependent
Methanococcus maripaludis
General Stability (protein specific)
General Stability
Organism
following dialysis, the enzyme is very unstable in the absence of glycerol or ethylene glycol, thiamine diphosphate and MgCl2 also help to maintain activity
Methanococcus maripaludis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Dithionite
with 5 mM dithionite, the half-life is 7 h at 2 °C, with about 90% of the original activity being lost after 24 h
Methanococcus maripaludis
glyoxylate
20 mM, about 40% of the original activity is lost. 2 mM glyoxylate inhibits 6%
Methanococcus maripaludis
additional information
no substrate inhibition with CoA up to 0.1 mM. Slightly or not inhibited at all by glyoxylate, nitrite, CO or potential physiological effectors. Not inhibited by CO. Potential affectors such as ATP, ADP, AMP, cAMP, GTP, GDP, GMP, NAD+, NADH, and glyceraldehyde 3-phosphate, at concentrations of 2 mM, do not affect the activity
Methanococcus maripaludis
oxygen
-
Methanococcus maripaludis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0058
-
CoA
pH 8.6, 37°C
Methanococcus maripaludis
0.115
-
pyruvate
pH 8.6, 37°C
Methanococcus maripaludis
0.205
-
2-oxobutyrate
pH 8.6, 37°C
Methanococcus maripaludis
0.264
-
oxaloacetate
pH 8.6, 37°C
Methanococcus maripaludis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron-sulfur cluster
porE encodes the 21500 Da subunit that contains a high cysteinyl residue content and a motif indicative of a [Fe–S] cluster. Subunit porF also also has a high cysteinyl residue content, and two [Fe–S] cluster motifs. Based upon these results, it is proposed that PorE and PorF are components of a specialized system required to transfer low-potential electrons for pyruvate biosynthesis
Methanococcus maripaludis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
190000
-
-
Methanococcus maripaludis
Oxidation Stability (protein specific)
Oxidation Stability
Organism
the enzyme is very sensitive to O2. Following incubation in air at 2°C for 40 min, about 60% of enzyme activity is lost. The half-life is 5.2 min when the purified enzyme is exposed to air in an ice bath. After inactivation of the purified enzyme by oxygen, activity is not restored byreplacing the oxygen with nitrogen and adding 0.01 mM dithionite no activity is lost after dialysis of extract in a basic buffer containing 20 mM potassium Tricine, pH 8.6, 5 mM MgCl2, 0.5 mM dithiothreitol, 0.1 mM thiamine diphosphate, and 10% glycerol
Methanococcus maripaludis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Methanococcus maripaludis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.3
-
pH 8.6, 37°C, substrate: indol-3-pyruvate
Methanococcus maripaludis
3.6
-
pH 8.6, 37°C, substrate: 2-oxobutyrate
Methanococcus maripaludis
6.5
-
pH 8.6, 37°C, substrate: oxaloacetate
Methanococcus maripaludis
7.4
-
pH 8.6, 37°C, substrate: pyruvate
Methanococcus maripaludis
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 3 weeks, anaerobic conditions, no loss of activity of the partially purified enzyme
Methanococcus maripaludis
2°C, 2 weeks, anaerobic conditions, no loss of activity
Methanococcus maripaludis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxobutyrate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
propanoyl-CoA + CO2 + reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
propanoyl-CoA + CO2 + reduced methyl viologen
-
-
-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
?
-
-
-
?
indol-3 pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
?
-
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
?
-
-
-
?
oxaloacetate + CoA + oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
?
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
the enzyme has a broad substrate specificity. In the presence of CoA, it oxidizes pyruvate, oxaloacetate, 2-oxobutyrate, and indol-3-pyruvate with specific activities of 7.4, 6.5, 3.6, and 0.3 U/mg, respectively. The enzyme reduces clostridial rubredoxin, clostridial and spinach ferredoxin, cytochrome c, FMN, and FAD. No activity is detected with NAD+, NADP+, and vitamin K1. The catalytic efficiencies or kcat/Km values for FAD and FMN are calculated to be 24000–32000/min * M, which are about two orders of magnitude lower than observed for the likely physiological electron carriers of other pyruvate oxidoreductases. Therefore, it is unlikely that flavins are the physiological electron carrier of the methanococcal pyruvate oxidoreductase
654391
Methanococcus maripaludis DSM Z 2067
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
the low molecular weight enzyme contains five polypeptides: 47000 Da (alpha), 33000 Da (beta), 25000 (gamma) and 13000 Da (gamma). The subunit stoichiometry for the alpha:beta:gamma:delta subunits is 1:1.08:0.90:1.32. In addition it contains a fifth polypeptide (21500 Da)
Methanococcus maripaludis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanococcus maripaludis
60
-
at pH 7.3, the temperature optimum is 60°C
Methanococcus maripaludis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
37
60
the activity detected at 60°C is five times the activity detected at 37°C
Methanococcus maripaludis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13
-
2-oxobutyrate
pH 8.6, 37°C
Methanococcus maripaludis
18
-
oxaloacetate
pH 8.6, 37°C
Methanococcus maripaludis
27
-
pyruvate
pH 8.6, 37°C
Methanococcus maripaludis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
at 37 °C, maximal activity is obtained at pH 7.3
Methanococcus maripaludis
8.6
-
assay at
Methanococcus maripaludis
General Information
General Information
Commentary
Organism
physiological function
in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon
Methanococcus maripaludis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
in autotrophic methanogens, pyruvate oxidoreductase plays a key role in the assimilation of CO2 and the biosynthesis of organic carbon
Methanococcus maripaludis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.6
-
2-oxobutyrate
pH 8.6, 37°C
Methanococcus maripaludis
68.2
-
oxaloacetate
pH 8.6, 37°C
Methanococcus maripaludis
234.8
-
pyruvate
pH 8.6, 37°C
Methanococcus maripaludis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.6
-
2-oxobutyrate
pH 8.6, 37°C
Methanococcus maripaludis
68.2
-
oxaloacetate
pH 8.6, 37°C
Methanococcus maripaludis
234.8
-
pyruvate
pH 8.6, 37°C
Methanococcus maripaludis
Other publictions for EC 1.2.7.1
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)
740173
Takenaka
Acetyl-CoA production by encap ...
Citrobacter sp.
Biores. Technol.
227
279-285
2017
-
-
-
-
-
1
-
4
-
1
2
-
-
2
1
-
1
-
-
-
-
-
2
1
1
1
-
4
1
1
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
4
-
1
2
-
-
1
-
1
-
-
-
-
2
1
1
1
-
4
1
1
-
-
-
-
-
-
4
4
748573
Patil
Fermentation of glycerol by A ...
Anaerobium acetethylicum
Microb. Biotechnol.
10
203-217
2017
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
740931
Song
Influence of 120 kDa pyruvate: ...
Trichomonas vaginalis
Korean J. Parasitol.
54
71-74
2016
-
-
-
-
-
-
-
-
-
-
1
1
-
6
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
735819
Zhou
Physiological roles of pyruvat ...
Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum JW/SL-YS485
Biotechnol. Biofuels
8
138
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
736379
Eram
Molecular and biochemical char ...
Pseudothermotoga hypogea, Thermotoga maritima, Thermotoga maritima DSM 3109
J. Biochem.
158
459-466
2015
-
-
-
-
-
-
-
5
-
-
10
-
-
6
2
-
2
-
-
-
2
-
3
2
3
-
1
-
2
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
5
-
-
10
-
-
2
-
2
-
-
2
-
3
2
3
-
1
-
2
-
-
-
-
-
-
-
-
-
740333
Saranyah
Homology modeling and in silic ...
Hungateiclostridium thermocellum
Comb. Chem. High Throughput Screen.
18
975-989
2015
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741314
Kushkevych
Kinetic properties of pyruvate ...
Desulfomicrobium sp., Desulfomicrobium sp. Rod-9, Desulfovibrio piger, Desulfovibrio piger Vib-7
Pol. J. Microbiol.
64
107-114
2015
-
-
-
-
-
-
-
4
-
-
-
4
-
18
-
-
-
-
-
3
-
-
8
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
4
-
-
-
-
-
3
-
-
8
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
726840
Eram
The bifunctional pyruvate deca ...
Thermococcus guaymasensis, Thermococcus guaymasensis DSM 11113
Archaea
2014
349379
2014
-
-
-
-
-
-
-
2
-
-
5
2
-
4
1
-
1
-
-
-
1
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
5
2
-
1
-
1
-
-
1
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
736364
Nohara
Genetic examination and mass b ...
Thermococcus kodakarensis
J. Bacteriol.
196
3831-3839
2014
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
725544
Noth
Pyruvate:ferredoxin oxidoreduc ...
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
J. Biol. Chem.
288
4368-4377
2013
-
1
1
-
-
-
-
3
-
-
1
6
-
10
-
-
1
-
-
-
-
-
10
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
3
-
-
1
6
-
-
-
1
-
-
-
-
10
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726231
van Lis
Chlamydomonas reinhardtii chlo ...
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC124
Plant Physiol.
161
57-71
2013
1
-
1
-
-
-
1
4
1
1
2
4
-
9
1
-
1
-
-
-
7
-
12
1
1
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
-
-
-
1
-
4
1
1
2
4
-
1
-
1
-
-
7
-
12
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
735589
Wang
Regulation of enzyme activity ...
Caldanaerobacter subterraneus subsp. tengcongensis, Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242
Biochem. Biophys. Res. Commun.
417
1018-1023
2012
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
749590
Warren
Amixicile, a novel inhibitor ...
Clostridioides difficile, Clostridioides difficile ATCC 43255
Antimicrob. Agents Chemother.
56
4103-4111
2012
-
-
-
-
-
-
10
-
-
-
-
2
-
9
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
2
10
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725220
Leitsch
Pyruvate:ferredoxin oxidoreduc ...
Giardia intestinalis
J. Antimicrob. Chemother.
66
1756-1765
2011
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
725463
Pieulle
Study of the thiol/disulfide r ...
Desulfovibrio vulgaris
J. Biol. Chem.
286
7812-7821
2011
1
-
-
-
-
-
-
-
-
-
-
1
-
5
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725902
Emelyanov
Fermentation enzymes of Giardi ...
Giardia intestinalis, Giardia intestinalis WB / CC 30957
Microbiology
157
1602-1611
2011
-
-
1
-
-
-
-
-
2
-
1
2
-
7
-
-
1
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
2
-
-
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725907
Meza-Cervantez
Pyruvate:ferredoxin oxidoreduc ...
Trichomonas vaginalis
Microbiology
157
3469-3482
2011
-
-
1
-
-
-
-
-
5
-
1
-
-
4
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
5
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
737156
Shaw
Metabolic engineering of a the ...
Thermoanaerobacterium saccharolyticum
Proc. Natl. Acad. Sci. USA
105
13769-13774
2008
-
1
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671738
Ikeda
Anabolic five subunit-type pyr ...
Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695
Biochem. Biophys. Res. Commun.
340
76-82
2006
-
-
1
-
-
-
-
-
-
-
6
-
-
5
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673610
Nishizawa
Gene expression and characteri ...
Aeropyrum pernix
FEBS Lett.
579
2319-2322
2005
-
-
1
-
-
-
1
1
-
-
5
-
-
2
-
-
1
-
-
-
-
-
7
1
2
1
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
1
-
-
5
-
-
-
-
1
-
-
-
-
7
1
2
1
1
-
1
1
-
-
-
-
-
-
-
-
654391
Lin
The anabolic pyruvate oxidored ...
Methanococcus maripaludis, Methanococcus maripaludis DSM Z 2067
Arch. Microbiol.
179
444-456
2003
-
-
-
-
-
1
4
4
-
1
1
-
-
2
1
-
1
-
-
-
4
2
10
1
2
1
-
3
2
-
-
3
-
-
-
-
-
-
3
-
-
1
-
4
-
4
-
1
1
-
-
1
-
1
-
-
4
2
10
1
2
1
-
3
2
-
-
-
-
1
1
-
3
3
721449
Labes
Sugar utilization in the hyper ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
Arch. Microbiol.
176
329-338
2001
-
-
-
-
-
-
-
-
-
-
-
1
-
9
-
-
-
-
-
1
1
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
2
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
736377
Imai
Characterization and cloning o ...
Thermococcus profundus
J. Biochem.
130
649-655
2001
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736515
Smith
Direct electrochemical charact ...
Thermococcus celer
J. Biol. Inorg. Chem.
6
227-231
2001
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
745202
Adams
Key role for sulfur in peptid ...
Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
721579
Menon
The delta-subunit of pyruvate ...
Pyrococcus furiosus
Biochemistry
37
12838-12846
1998
-
-
1
-
-
-
-
-
-
1
-
1
-
5
-
-
1
-
-
-
-
-
1
1
-
-
1
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
288436
Yoon
Purification and characterizat ...
Hydrogenobacter thermophilus, Hydrogenobacter thermophilus TK-6 / IAM 12695
Arch. Microbiol.
167
275-279
1997
-
-
-
-
-
-
-
2
-
-
5
2
-
20
1
-
1
-
-
-
1
-
10
1
1
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
5
2
-
1
-
1
-
-
1
-
10
1
1
-
2
-
1
-
-
-
-
-
-
-
-
-
721578
Zhou
Site-directed mutations of the ...
Pyrococcus furiosus
Biochemistry
36
10892-10900
1997
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
723667
Ma
Pyruvate ferredoxin oxidoreduc ...
Pyrococcus furiosus
Proc. Natl. Acad. Sci. USA
94
9608-9613
1997
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
1
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
727496
Bock
The iron-sulfur centers of the ...
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
FEBS Lett.
414
209-212
1997
-
-
-
-
-
-
-
-
-
1
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288443
Kletzin
Molecular and phylogenetic cha ...
Pyrococcus furiosus, Thermotoga maritima, Thermotoga maritima DSM 3109
J. Bacteriol.
178
248-257
1996
-
-
-
-
-
-
-
-
4
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
288446
Townson
Characterization and purificat ...
Giardia intestinalis, Giardia intestinalis BRIS/83/HEPU/106
Mol. Biochem. Parasitol.
79
183-193
1996
-
-
-
-
-
-
-
-
-
-
2
2
-
5
-
-
1
-
-
-
1
1
11
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
1
-
-
1
1
11
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
288448
Bock
Catalytic properties, molecula ...
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
Eur. J. Biochem.
237
35-44
1996
1
-
-
-
-
1
1
4
-
1
5
2
-
14
-
-
1
-
-
-
-
2
10
1
1
1
-
-
1
-
-
1
1
-
-
1
-
-
1
-
-
1
-
1
1
4
-
1
5
2
-
-
-
1
-
-
-
2
10
1
1
1
-
-
1
-
-
-
-
1
1
-
-
-
744835
Bock
Catalytic properties, molecul ...
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
Eur. J. Biochem.
237
35-44
1996
-
-
-
-
-
-
1
4
-
-
1
2
-
14
1
-
1
-
-
-
-
-
8
1
2
1
-
-
1
-
-
2
1
-
-
-
-
-
2
-
-
-
-
1
1
4
-
-
1
2
-
1
-
1
-
-
-
-
8
1
2
1
-
-
1
-
-
-
-
1
1
-
-
-
288449
Kunow
Pyruvate:ferredoxin oxidoreduc ...
Archaeoglobus fulgidus
Arch. Microbiol.
163
21-28
1995
-
-
-
-
-
-
3
3
-
1
6
-
-
8
1
-
1
-
-
-
-
-
2
1
2
-
1
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
3
-
1
6
-
-
1
-
1
-
-
-
-
2
1
2
-
1
-
1
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
3
3
-
-
-
3
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
3
-
-
-
3
-
-
-
-
-
-
-
-
-
735659
Blamey
Characterization of an ancestr ...
Thermotoga maritima
Biochemistry
33
1000-1007
1994
1
-
-
-
-
-
2
2
-
-
5
-
-
4
1
-
1
-
-
-
-
-
2
1
1
-
1
-
-
-
-
1
1
-
-
1
-
-
1
-
-
-
-
2
1
2
-
-
5
-
-
1
-
1
-
-
-
-
2
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
735660
Smith
Pyruvate ferredoxin oxidoreduc ...
Pyrococcus furiosus, Thermotoga maritima, Thermotoga maritima DSM 3109
Biochemistry
33
1008-1016
1994
-
-
-
-
-
-
-
-
-
1
-
-
-
8
-
-
-
-
-
-
-
-
3
-
2
2
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
288442
Blamey
Purification and characterizat ...
Pyrococcus furiosus
Biochim. Biophys. Acta
1161
19-27
1993
-
-
-
-
-
1
2
3
-
1
4
1
-
3
-
-
1
-
-
-
1
-
3
1
-
-
2
-
-
-
-
1
1
-
-
-
-
-
1
-
-
1
-
2
1
3
-
1
4
1
-
-
-
1
-
-
1
-
3
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
735729
Forget
Purification and characterizat ...
Hungateiclostridium thermocellum
Biochimie
64
1009-1014
1983
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-