Results 21 to 30 of about 9,205 (218)

Localization of the human dihydrolipoamide dehydrogenase gene (DLD) to 7q31→q32 [PDF]

open access: yesCytogenetic and Genome Research, 1991
The gene for human dihydrolipoamide dehydrogenase (DLD) has been localized to the long arm of chromosome 7, within bands q31→q32, by gel-blot hybridization analysis with DNA from a panel of somatic cell hybrids containing various portions of human ...
Otulakowski, G   +3 more
core   +6 more sources

Targeted Redox Regulation α-Ketoglutarate Dehydrogenase Complex for the Treatment of Human Diseases [PDF]

open access: yesCells
α-ketoglutarate dehydrogenase complex (KGDHc) is a crucial enzyme in the tricarboxylic acid (TCA) cycle that intersects monosaccharides, amino acids, and fatty acid catabolism with oxidative phosphorylation (OxPhos). A key feature of KGDHc is its ability
Ryan J. Mailloux
doaj   +2 more sources

Roles of Dihydrolipoamide Dehydrogenase in Health and Disease. [PDF]

open access: yesAntioxid Redox Signal, 2023
Significance: Dihydrolipoamide dehydrogenase (DLDH) is a flavin-dependent disulfide oxidoreductase. The active form of DLDH is a stable homodimer, and its deficiencies have been linked to numerous metabolic disorders. A better understanding of redox and nonredox features of DLDH may reveal druggable targets for disease interventions or preventions ...
Yan LJ, Wang Y.
europepmc   +3 more sources

The Effects of a Ketogenic Diet on Patients with Dihydrolipoamide Dehydrogenase Deficiency. [PDF]

open access: yesNutrients, 2021
Background: Dihydrolipoamide dehydrogenase (DLD lipoamide dehydrogenase, the E3 subunit of the pyruvate dehydrogenase complex (PDHC)) is the third catalytic enzyme of the PDHC, which converts pyruvate to acetyl-CoA catalyzed with the introduction of acetyl-CoA to the tricyclic acid (TCA) cycle.
Staretz-Chacham O   +7 more
europepmc   +4 more sources

Cryptic proteolytic activity of dihydrolipoamide dehydrogenase [PDF]

open access: greenProceedings of the National Academy of Sciences, 2007
The mitochondrial enzyme, dihydrolipoamide dehydrogenase (DLD), is essential for energy metabolism across eukaryotes. Here, conditions known to destabilize the DLD homodimer enabled the mouse, pig, or human enzyme to function as a protease. A catalytic dyad (S456–E431) buried at the homodimer interface was identified.
Ngolela Esther Babady   +3 more
openalex   +3 more sources

GLS2 inhibition synergizes with copper to reprogram TCA cycle for cuproptosis-driven radiosensitization in esophageal cancer [PDF]

open access: yesExperimental Hematology & Oncology
Esophageal squamous cell carcinoma (ESCC) is notorious for its poor prognosis. In the present study, the role of glutaminase 2 (GLS2) and copper (Cu) in the radiosensitivity of ESCC was explored.
Wang Jing   +7 more
doaj   +2 more sources

Engineering the 2-Oxoglutarate Dehydrogenase Complex to Understand Catalysis and Alter Substrate Recognition

open access: yesReactions, 2022
The E. coli 2-oxoglutarate dehydrogenase complex (OGDHc) is a multienzyme complex in the tricarboxylic acid cycle, consisting of multiple copies of three components, 2-oxoglutarate dehydrogenase (E1o), dihydrolipoamide succinyltransferase (E2o) and ...
Joydeep Chakraborty   +7 more
doaj   +1 more source

Hamster Sperm Capacitation: Role of Pyruvate Dehydrogenase A and Dihydrolipoamide Dehydrogenase1 [PDF]

open access: bronzeBiology of Reproduction, 2008
Recently, we demonstrated that pyruvate dehydrogenase A2 (PDHA2) is tyrosine phosphorylated in capacitated hamster spermatozoa. In this report, using bromopyruvate (BP), an inhibitor of PDHA, we demonstrated that hamster sperm hyperactivation was blocked regardless of whether PDHA was inhibited prior to or after the onset of hyperactivation, but the ...
Vivek Kumar, Venkatesh Kota, S. Shivaji
openalex   +4 more sources

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