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Details on Person Dihydrolipoyl dehydrogenase (DLD), the E3 component of the 2...
| Class:Id | Summation:9853984 |
|---|---|
| _displayName | Dihydrolipoyl dehydrogenase (DLD), the E3 component of the 2... |
| _timestamp | 2023-12-06 11:56:15 |
| created | [InstanceEdit:9853986] Stephan, Ralf, 2023-11-22 |
| modified | [InstanceEdit:9855644] Stephan, Ralf, 2023-12-06 [InstanceEdit:9855645] Stephan, Ralf, 2023-12-06 |
| text | Dihydrolipoyl dehydrogenase (DLD), the E3 component of the 2-oxoglutarate dehydrogenase metabolon, forms a homodimer that catalyzes the dehydrogenation of dihydrolipoyllysine residues by producing NADH from NAD+, with the help of the FAD cofactor (Brautigam et al., 2005). This reaction, in a side reaction not annotated here, is the main source of reactive oxygen species (ROS) in mitochondria (Ambrus et al., 2015). Deficiency of DLD activity due to mutations is a rare genetic disease (DLDD; MIM:246900; see Wongkittichote et al., 2023; reviewed in Ambrus & Adam-Viz, 2017). |
| (summation) | [Reaction:9853499] DLD dimer dehydrogenates dihydrolipoyl [Homo sapiens] [Reaction:9861616] DLD dimer dehydrogenates dihydrolipoyl [Homo sapiens] |
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No pathways have been reviewed or authored by Dihydrolipoyl dehydrogenase (DLD), the E3 component of the 2... (9853984)
