EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.12 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.12 | Mg2+ | - |
Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.12 | 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 |
2.3.1.12 | 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 |
2.3.1.12 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.12 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.12 | recombinant 1-lip E2 and recombinant hybrid lipoyl domain by ammonium sulfate fractionation, ion exchange and hydrophobic interaction chromatography | Escherichia coli |
EC Number | Renatured (Comment) | Organism |
---|---|---|
2.3.1.12 | reconstitution of the active multienzyme complex with recombinant components | Escherichia coli |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.3.1.12 | 34.1 | - |
purified 1-lip E2 | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.12 | acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine | reductive acetylation of the enzyme | Escherichia coli | CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.12 | ? | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.12 | dihydrolipoamide acetyltransferase | - |
Escherichia coli |
2.3.1.12 | E2 | - |
Escherichia coli |
2.3.1.12 | More | the enzyme is a subunit of the pyruvate dehydrogenase multienzyme complex | Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.12 | 25 | - |
assay at | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.12 | 8 | - |
assay at | Escherichia coli |