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Literature summary for 1.2.7.1 extracted from
- Purification and characterization of pyruvate:ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6 (1997), Arch. Microbiol., 167, 275-279.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.054 | - |
CoA | pH 7.6, 70°C | Hydrogenobacter thermophilus |  |
| 3.45 | - |
pyruvate | pH 7.6, 70°C | Hydrogenobacter thermophilus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 24500 | - |
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE | Hydrogenobacter thermophilus |
| 29000 | - |
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE | Hydrogenobacter thermophilus |
| 31500 | - |
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE | Hydrogenobacter thermophilus |
| 46000 | - |
1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE | Hydrogenobacter thermophilus |
| 135000 | - |
gel filtration | Hydrogenobacter thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate + CoA + 2 oxidized ferredoxin | Hydrogenobacter thermophilus | ferredoxin is an electron donor for the enzyme reaction in vivo | acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+ | - |
? | |
| pyruvate + CoA + 2 oxidized ferredoxin | Hydrogenobacter thermophilus TK-6 / IAM 12695 | ferredoxin is an electron donor for the enzyme reaction in vivo | acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hydrogenobacter thermophilus | - |
- |
- |
| Hydrogenobacter thermophilus TK-6 / IAM 12695 | - |
- |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| the enzyme is inactivated by oxygen, which makes it difficult to purify the enzyme under oxic conditions. The enzyme can be stabilized when 0.1% Triton X-100 is added to the purification buffers | Hydrogenobacter thermophilus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Hydrogenobacter thermophilus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 3.46 | - |
pH 7.6, 70°C | Hydrogenobacter thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxobutyrate + CoA + oxidized methyl viologen | the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate | Hydrogenobacter thermophilus | propanoyl-CoA + CO2 + reduced methyl viologen | - |
? | |
| 2-oxobutyrate + CoA + oxidized methyl viologen | the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate | Hydrogenobacter thermophilus TK-6 / IAM 12695 | propanoyl-CoA + CO2 + reduced methyl viologen | - |
? | |
| additional information | no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate | Hydrogenobacter thermophilus | ? | - |
? | |
| additional information | no activity with 2-oxoglutarate, oxomalonate, 2-oxoisocaproate, phosphoenolpyruvate, indole-3-pyruvate, or phenylpyruvate | Hydrogenobacter thermophilus TK-6 / IAM 12695 | ? | - |
? | |
| oxaloacetate + CoA + oxidized methyl viologen | the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate | Hydrogenobacter thermophilus | ? | - |
? | |
| oxaloacetate + CoA + oxidized methyl viologen | the enzyme reacts with 2-oxobutyrate and oxaloacetate at 38% activity relative to the activity against pyruvate | Hydrogenobacter thermophilus TK-6 / IAM 12695 | ? | - |
? | |
| pyruvate + CoA + 2 oxidized ferredoxin | ferredoxin is an electron donor for the enzyme reaction in vivo | Hydrogenobacter thermophilus | acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+ | - |
? | |
| pyruvate + CoA + 2 oxidized ferredoxin | ferredoxin is an electron donor for the enzyme reaction in vivo | Hydrogenobacter thermophilus TK-6 / IAM 12695 | acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+ | - |
? | |
| pyruvate + CoA + oxidized methyl viologen | specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin | Hydrogenobacter thermophilus | acetyl-CoA + CO2 + reduced methyl viologen | - |
? | |
| pyruvate + CoA + oxidized methyl viologen | specific activity with methyl viologen is 10fold higher compared to the specific activity with Hydrogenobacter thermophilus ferredoxin | Hydrogenobacter thermophilus TK-6 / IAM 12695 | acetyl-CoA + CO2 + reduced methyl viologen | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 1 * 46000 + 1 * 31500 + 1 * 29000 + 1 * 24500, SDS-PAGE | Hydrogenobacter thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pyruvate:ferredoxin oxidoreductase | - |
Hydrogenobacter thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | 85 | - |
Hydrogenobacter thermophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
8 h, anoxic conditions, 50% loss of activity | Hydrogenobacter thermophilus |
| 75 | - |
30 min, anoxic conditions, more than 80% residual activity after heating | Hydrogenobacter thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | 7.8 | - |
Hydrogenobacter thermophilus |
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