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Literature summary extracted from
- Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system (1991), J. Bacteriol., 173, 757-767.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 2.3.1.12 | sensitive to proteolysis | Syntrophotalea carbinolica |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.4 | 0.15 | - |
NADH | - |
Syntrophotalea carbinolica |  |
| 1.8.1.4 | 0.4 | - |
dihydrolipoamide | - |
Syntrophotalea carbinolica | |
| 1.8.1.4 | 0.62 | - |
NAD+ | - |
Syntrophotalea carbinolica | |
| 1.8.1.4 | 3.7 | - |
Lipoamide | - |
Syntrophotalea carbinolica | |
| 2.3.1.12 | 2.2 | - |
dihydrolipoamide | - |
Syntrophotalea carbinolica | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.4 | 54000 | - |
2 * 54000, SDS-PAGE | Syntrophotalea carbinolica |
| 1.8.1.4 | 110000 | - |
non-denaturing gradient PAGE | Syntrophotalea carbinolica |
| 2.3.1.12 | 60000 | - |
x * 60000, SDS-PAGE | Syntrophotalea carbinolica |
| 2.3.1.12 | 60000 | - |
24 * 60000, SDS-PAGE | Syntrophotalea carbinolica |
| 2.3.1.12 | 500000 | - |
gel filtration | Syntrophotalea carbinolica |
| 2.3.1.12 | 500000 | - |
above, gel filtration | Syntrophotalea carbinolica |
| 2.3.1.190 | 143000 | 177000 | gel filtration | Syntrophotalea carbinolica |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.3.1.12 | dihydrolipoamide + acetyl-CoA | Syntrophotalea carbinolica | - |
S-acetyldihydrolipoamide + CoA | - |
? | |
| 2.3.1.12 | additional information | Syntrophotalea carbinolica | protein bound acetyldihydrolipoyl moiety + CoA | ? | - |
? | |
| 2.3.1.190 | additional information | Syntrophotalea carbinolica | The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+ | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.4 | Syntrophotalea carbinolica | - |
- |
- |
| 2.3.1.12 | Syntrophotalea carbinolica | - |
- |
- |
| 2.3.1.190 | Syntrophotalea carbinolica | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.1.4 | - |
Syntrophotalea carbinolica |
| 2.3.1.12 | - |
Syntrophotalea carbinolica |
| 2.3.1.12 | homogeneity | Syntrophotalea carbinolica |
| 2.3.1.190 | from acetoin-grown cells | Syntrophotalea carbinolica |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 2.3.1.12 | reconstitution of pyruvate dehydrogenase complex | Syntrophotalea carbinolica |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.4 | 25.7 | - |
- |
Syntrophotalea carbinolica |
| 2.3.1.12 | 509 | - |
- |
Syntrophotalea carbinolica |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.8.1.4 | stable for months if stored in liquid nitrogen | Syntrophotalea carbinolica |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.4 | 2 ferricyanide + NADH | 31.1% of the activity with lipoamide | Syntrophotalea carbinolica | 2 ferrocyanide + NAD+ + H+ | - |
? | |
| 1.8.1.4 | 5-nitroblue tetrazolium chloride + NADH | 5.1% of the activity with lipoamide | Syntrophotalea carbinolica | ? + NAD+ | - |
? | |
| 1.8.1.4 | benzyl viologen + NADH | 2.9% of the activity with lipoamide | Syntrophotalea carbinolica | ? + NAD+ | - |
? | |
| 1.8.1.4 | dihydrolipoamide + NAD+ | - |
Syntrophotalea carbinolica | lipoamide + NADH | - |
r | |
| 1.8.1.4 | menadione + NADH | 13.6% of the activity with lipoamide | Syntrophotalea carbinolica | ? + NAD+ | - |
? | |
| 1.8.1.4 | methylene blue + NADH | 9.4% of the activity with lipoamide | Syntrophotalea carbinolica | ? + NAD+ | - |
? | |
| 1.8.1.4 | oxidized 2,6-dichlorophenolindophenol + NADH | 12.3% of the activity with lipoamide | Syntrophotalea carbinolica | ? + NAD+ | - |
? | |
| 2.3.1.12 | dihydrolipoamide + acetyl-CoA | - |
Syntrophotalea carbinolica | S-acetyldihydrolipoamide + CoA | - |
? | |
| 2.3.1.12 | additional information | protein bound acetyldihydrolipoyl moiety + CoA | Syntrophotalea carbinolica | ? | - |
? | |
| 2.3.1.190 | acetoin + 2,6-dichlorophenolindophenol | - |
Syntrophotalea carbinolica | acetaldehyde + ? | - |
? | |
| 2.3.1.190 | diacetyl + 2,6-dichlorophenolindophenol | - |
Syntrophotalea carbinolica | ? | - |
? | |
| 2.3.1.190 | methyl acetoin + 2,6-dichlorophenolindophenol | - |
Syntrophotalea carbinolica | ? + ? | - |
? | |
| 2.3.1.190 | additional information | The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+ | Syntrophotalea carbinolica | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.1.4 | dimer | 2 * 54000, SDS-PAGE | Syntrophotalea carbinolica |
| 2.3.1.12 | polymer | x * 60000, SDS-PAGE | Syntrophotalea carbinolica |
| 2.3.1.12 | polymer | 24 * 60000, SDS-PAGE | Syntrophotalea carbinolica |
| 2.3.1.190 | More | component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 37500 Da, and beta, 38500 Da, SDS-PAGE | Syntrophotalea carbinolica |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.3.1.190 | Ao:DCPIP OR | - |
Syntrophotalea carbinolica |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.4 | 7.2 | - |
NADH-dependent reduction of lipoamide | Syntrophotalea carbinolica |
| 2.3.1.12 | additional information | - |
reactivity depending on buffer system | Syntrophotalea carbinolica |
| 2.3.1.12 | 6.7 | - |
- |
Syntrophotalea carbinolica |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.4 | FAD | contains one noncovalently bound FAD per subunit | Syntrophotalea carbinolica | |
| 1.8.1.4 | NAD+ | highly specific for | Syntrophotalea carbinolica | |
| 1.8.1.4 | NADH | highly specific for | Syntrophotalea carbinolica | |
| 1.8.1.4 | NADP+ | no activity | Syntrophotalea carbinolica | |
| 1.8.1.4 | NADPH | no activity | Syntrophotalea carbinolica | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 2.3.1.190 | Syntrophotalea carbinolica | the enzymes Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase are induced during growth on acetoin, whereas they are absent or scarcely present in cells grown on a nonacetoinogenic substrate | up |
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