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Literature summary for 1.8.1.4 extracted from
- Structural investigations of E. coli dihydrolipoamide dehydrogenase in solution small-angle X-ray scattering and molecular docking (2016), Crystallogr. Rep., 61, 414-420 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene lpd, recombinant expression in Escherichia coli strain BL21(DE3) | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified enzyme, X-ray diffraction structure determination and analysis, small-angle X-ray scattering of the enzyme in solution, measurements in 50 mM Tris buffer, pH 7.5, at 10°C, molecular docking and modeling | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and hydrophobic interaction chromatography to over 98% purity | Escherichia coli |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Escherichia coli |
| More | in solution LpD exists as an equilibrium mixture of a dimer and a tetramer, small-angle X-ray scattering and analytical ultracentrifugation | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoamide dehydrogenase | - |
Escherichia coli |
| LPD | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | all of the E3 enzymes function as dimers, and their active site contains the reactive disulfide bridge, which is directly involved in catalysis | Escherichia coli |
| physiological function | dihydrolipoamide dehydrogenase of Escherichia coli is a bacterial enzyme that is involved in the central metabolism and shared in common between the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. The presence of oligomeric forms of the enzyme is determined by the multifunctionality of LpD in the cell, in particular, the required stoichiometry in the complexes. The E3 enzyme activity is essential for aerobic respiration. Dihydrolipoamide dehydrogenase plays an equally important role in anaerobic organisms, since this enzyme is involved in the synthesis of branched-chain keto and amino acids | Escherichia coli |
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