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Literature summary extracted from

  • Lin, W.C.; Yang, Y.L.; Whitman, W.B.
    The anabolic pyruvate oxidoreductase from Methanococcus maripaludis (2003), Arch. Microbiol., 179, 444-456.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.2.7.1 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

EC Number Inhibitors Comment Organism Structure
1.2.7.1 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
1.2.7.1 glyoxylate 20 mM, about 40% of the original activity is lost. 2 mM glyoxylate inhibits 6% Methanococcus maripaludis
1.2.7.1 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
1.2.7.1 oxygen
-
Methanococcus maripaludis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.7.1 0.0058
-
CoA pH 8.6, 37°C Methanococcus maripaludis
1.2.7.1 0.115
-
pyruvate pH 8.6, 37°C Methanococcus maripaludis
1.2.7.1 0.205
-
2-oxobutyrate pH 8.6, 37°C Methanococcus maripaludis
1.2.7.1 0.264
-
oxaloacetate pH 8.6, 37°C Methanococcus maripaludis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.7.1 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.7.1 190000
-
-
Methanococcus maripaludis

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.1 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
-
1.2.7.1 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

EC Number Oxidation Stability Organism
1.2.7.1 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)

EC Number Purification (Comment) Organism
1.2.7.1
-
Methanococcus maripaludis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.7.1 0.3
-
pH 8.6, 37°C, substrate: indol-3-pyruvate Methanococcus maripaludis
1.2.7.1 3.6
-
pH 8.6, 37°C, substrate: 2-oxobutyrate Methanococcus maripaludis
1.2.7.1 6.5
-
pH 8.6, 37°C, substrate: oxaloacetate Methanococcus maripaludis
1.2.7.1 7.4
-
pH 8.6, 37°C, substrate: pyruvate Methanococcus maripaludis

Storage Stability

EC Number Storage Stability Organism
1.2.7.1 -20°C, 3 weeks, anaerobic conditions, no loss of activity of the partially purified enzyme Methanococcus maripaludis
1.2.7.1 2°C, 2 weeks, anaerobic conditions, no loss of activity Methanococcus maripaludis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.1 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 Methanococcus maripaludis propanoyl-CoA + CO2 + reduced methyl viologen
-
?
1.2.7.1 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 Methanococcus maripaludis DSM Z 2067 propanoyl-CoA + CO2 + reduced methyl viologen
-
?
1.2.7.1 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 Methanococcus maripaludis ?
-
?
1.2.7.1 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 Methanococcus maripaludis DSM Z 2067 ?
-
?
1.2.7.1 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 Methanococcus maripaludis ?
-
?
1.2.7.1 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 Methanococcus maripaludis DSM Z 2067 ?
-
?
1.2.7.1 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 Methanococcus maripaludis acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
?
1.2.7.1 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 Methanococcus maripaludis DSM Z 2067 acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
?
1.2.7.1 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 Methanococcus maripaludis acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
?
1.2.7.1 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 Methanococcus maripaludis DSM Z 2067 acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
?

Subunits

EC Number Subunits Comment Organism
1.2.7.1 ? 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

Synonyms

EC Number Synonyms Comment Organism
1.2.7.1 POR
-
Methanococcus maripaludis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.7.1 37
-
assay at Methanococcus maripaludis
1.2.7.1 60
-
at pH 7.3, the temperature optimum is 60°C Methanococcus maripaludis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.7.1 37 60 the activity detected at 60°C is five times the activity detected at 37°C Methanococcus maripaludis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.7.1 13
-
2-oxobutyrate pH 8.6, 37°C Methanococcus maripaludis
1.2.7.1 18
-
oxaloacetate pH 8.6, 37°C Methanococcus maripaludis
1.2.7.1 27
-
pyruvate pH 8.6, 37°C Methanococcus maripaludis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.7.1 7.3
-
at 37 °C, maximal activity is obtained at pH 7.3 Methanococcus maripaludis
1.2.7.1 8.6
-
assay at Methanococcus maripaludis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.7.1 FAD it is possible that flavins play an important regulatory or structural role in the enzyme Methanococcus maripaludis
1.2.7.1 FMN it is possible that flavins play an important regulatory or structural role in the enzyme Methanococcus maripaludis
1.2.7.1 additional information the enzyme is not coenzyme F420-dependent Methanococcus maripaludis

General Information

EC Number General Information Comment Organism
1.2.7.1 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.7.1 3.6
-
2-oxobutyrate pH 8.6, 37°C Methanococcus maripaludis
1.2.7.1 68.2
-
oxaloacetate pH 8.6, 37°C Methanococcus maripaludis
1.2.7.1 234.8
-
pyruvate pH 8.6, 37°C Methanococcus maripaludis