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Literature summary for 2.3.1.12 extracted from
- The catalytic domain of dihydrolipoyl acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Expression, purification and reversible denaturation (1997), FEBS Lett., 413, 339-343.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| catalytic domain, residues 173-427 | Geobacillus stearothermophilus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.013 | - |
acetyl-CoA | catalytic domain after expression in Escherichia coli | Geobacillus stearothermophilus |  |
| 1.2 | - |
dihydrolipoamide | catalytic domain after expression in Escherichia coli | Geobacillus stearothermophilus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
high molecular mass species in the absence of guanidinium hydrochloride | Geobacillus stearothermophilus |
| 30000 | - |
gel filtration in the presence of guanidinium hydrochloride | Geobacillus stearothermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dihydrolipoamide + acetyl-CoA | Geobacillus stearothermophilus | - |
S-acetyldihydrolipoamide + CoA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Geobacillus stearothermophilus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Geobacillus stearothermophilus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine | reaction mechanism | Geobacillus stearothermophilus |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| treatment with guanidine hydrochloride results in dissociation into subunits, removal of guanidine hydrochloride results in refolding of the enzyme with 95% of the original activity | Geobacillus stearothermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dihydrolipoamide + acetyl-CoA | - |
Geobacillus stearothermophilus | S-acetyldihydrolipoamide + CoA | - |
? | |
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Release 2023.1 (January 2023)
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