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Literature summary for 2.3.1.12 extracted from
- Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase (2003), Protein Expr. Purif., 28, 140-150.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| functional overexpression of the enzyme E2 with a single hybrid lipoyl domain per subunit, i.e. 1-lip E2, in strain JRG1342 and BL21(DE3), overexpression of the isolated hybrid lipoyl domain in strain JM 101 | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 8982 | - |
x * 45953, recombinant 1-lip E2, mass spectrometry, x * 8982, recombinant unacetylated hybrid lipoyl domain, mass spectrometry, x * 9019, recombinant fully acetylated hybrid lipoyl domain, mass spectrometry | Escherichia coli |
| 9019 | - |
x * 45953, recombinant 1-lip E2, mass spectrometry, x * 8982, recombinant unacetylated hybrid lipoyl domain, mass spectrometry, x * 9019, recombinant fully acetylated hybrid lipoyl domain, mass spectrometry | Escherichia coli |
| 45953 | - |
x * 45953, recombinant 1-lip E2, mass spectrometry, x * 8982, recombinant unacetylated hybrid lipoyl domain, mass spectrometry, x * 9019, recombinant fully acetylated hybrid lipoyl domain, mass spectrometry | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant 1-lip E2 and recombinant hybrid lipoyl domain by ammonium sulfate fractionation, ion exchange and hydrophobic interaction chromatography | Escherichia coli |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| reconstitution of the active multienzyme complex with recombinant components | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 34.1 | - |
purified 1-lip E2 | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine | reductive acetylation of the enzyme | Escherichia coli | CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 45953, recombinant 1-lip E2, mass spectrometry, x * 8982, recombinant unacetylated hybrid lipoyl domain, mass spectrometry, x * 9019, recombinant fully acetylated hybrid lipoyl domain, mass spectrometry | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoamide acetyltransferase | - |
Escherichia coli |
| E2 | - |
Escherichia coli |
| More | the enzyme is a subunit of the pyruvate dehydrogenase multienzyme complex | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
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