EC Number   |
General Information |
Reference |
|---|
    1.8.1.4 | evolution |
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family |
742087 |
| 1.8.1.4 | evolution |
E3 belongs to the pyridine nucleotide-disulfide oxidoreductase family along with glutathione reductase (GR), thioredoxin reductase, mercuric reductase and trypanothione reductase |
742221 |
| 1.8.1.4 | evolution |
residue Cys50 is absolutely conserved, Cys50 is a component of the very long a-helix structure 2, which is composed of 25 amino acids. Residue Cys50 forms an active disulfide center with Cys45 |
743051 |
| 1.8.1.4 | evolution |
residue H329 is absolutely conserved, H329 329 is a part of the long alpha-helix 8, which is composed of 16 amino acids and is a component of the central domain. His329 is also located near FAD and the active disulfide center between Cys45 and Cys50, which are essential to the catalytic activity of human E3 |
743052 |
| 1.8.1.4 | evolution |
residues Pro156 and Pro303 are highly conserved |
743050 |
| 1.8.1.4 | malfunction |
as a common component in three 2-oxo acid dehydrogenase, a decrease in E3 activity affects the activities of all three complexes, which leads to increased urinary excretion of 2-oxo acids, elevated blood lactate, pyruvate, and branched chain amino acids. Patients with an E3 deficiency normally die young because an E3 deficiency is a critical genetic defect affecting the central nervous system. A deficiency in E3 results in Leigh syndrome with recurrent episodes of hypoglycemia and ataxia, permanent lactic acidaemia, and mental retardation. A C45A mutation results in a large decrease in human E3 activity and changes in the spectroscopic properties of human E3 |
743051 |
| 1.8.1.4 | malfunction |
chronic inhibition of the enzyme can attenuate oxidative stress in type 2 diabetes |
763920 |
| 1.8.1.4 | malfunction |
enhanced arsenate and arsenite sensitivity is due to the disruption of the plastidial LPD1 and LPD2 genes |
713314 |
| 1.8.1.4 | malfunction |
metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial lipoamide dehydrogenase2. Both arsenate and arsenite inhibit root elongation, decreased seedling size and increase anthocyanin production more profoundly in knockout mutants than in wild-type seedlings, arsenite seems to be the mediator of the observed phenotypes |
743450 |
| 1.8.1.4 | malfunction |
pathogenic amino acid substitutions of the common E3 component (hE3) of the human 2-oxoglutarate dehydrogenase and the pyruvate dehydrogenase complexes lead to severe metabolic diseases (E3 deficiency), which usually manifest themselves in cardiological and/or neurological symptoms and often cause premature death. Determination of structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase involved in E3 deficiency, using hydrogen/deuterium-exchange mass spectrometry |
741998 |
