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Molecular characterization of dihydrolipoamide dehydrogenase binding sites to titanium dioxide has been reported.
study found that individuals infected with HBV withwith basal core promoter (BCP) double mutations (A1762T, G1764A)have lower concentrations of serum DLD than those with the wild-type BCP
Mitochondrial dihydrolipoamide dehydrogenase is upregulated in response to the brain intermittent hypoxic preconditioning.
IgA autoantibody against DLD could be a novel diagnostic marker for endometrial cancer.
Case Report: novel mutation in the DLD interface giving rise to DLD deficiency.
Human, mouse, and pig Dld has moonlighting function as a protease in addition to its canonical function as a a dehydrogenase.
This molecular dynamics study proposes the structural changes that may lead to the modulation in reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase.
ATP consumption is demonstrated in respiration-impaired isolated and in situ neuronal somal mitochondria from transgenic mice that exhibit a 20-48% decrease in alpha-ketoglutarate dehydrogenase activity.
the cryptic activities of DLD promote oxidative damage to neighboring molecules and thus contribute to the clinical severity of DLD mutations
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex.
the E3 binding protein component of the pyruvate dehydrogenase complex appear to be a rare cause of pyruvate dehydrogenase deficiency
Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD-binding region to valine.
model of the pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and binding of the E1 and E3 components
A c.1444A>G substitution in E3 exon 13, predictive of a p.R482G (or R447G in the processed gene product) substitution in a highly conserved domain of the protein was found.
Asparagine-473 residue is important for the catalytic function of dihydrolipoamide dehydrogenase.
the disease-causing mutations of E3 occur at three locations in the human enzyme: the dimer interface, the active site, and the FAD and NAD(+)-binding sites
specificity of pairing for human E3BP with E3 from its subcomplex structure to be most likely due to conformational rigidity of the binding fragment of the E3-binding domain of E3BP and its exquisite amino acid match with the E3 target interface
The conservation of the Ile-51 residue with Ala using site-directed mutagenesis in human Dihydrolipoamide dehydrogenase(E3) was very important to the efficient catalytic function of the enzyme.
These results suggest that N286 and D320 play a role in the catalytic function of the E3.
DLD, malic acid, and fumaric acid can be used for development of cosmeceuticals and nutraceuticals regulating the change of skin metabolism induced by the UVB overexposure.
Data show that mitochondrial diaphorases (dihydrolipoamide dehydrogenase) in the liver contribute up to 81% to the NAD(+) pool during respiratory inhibition.
ATP consumption is demonstrated in respiration-impaired isolated mice and in situ neuronal mitochondria from transgenic mice with dihydrolipoyl succinyltransferase deficiency.
Mice that are deficient in dihydrolipoamide dehydrogenase show increased vulnerability to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), malonate and 3-nitropropionic acid, which have been used in models of Parkinson disease and Huntington disease
These findings show that the plastidial LIPOAMIDE DEHYDROGENASE, ptLPD, isoforms are critical in vivo determinants of arsenite-mediated arsenic sensitivity in Arabidopsis and possible strategic targets for increasing arsenic tolerance. [ptLPD2]
Lipoamide dehydrogenase significantly accelerates the conversion of a defined subset of NO donors to NO.
This gene encodes the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.
E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex
, dihydrolipoyl dehydrogenase, mitochondrial
, glycine cleavage system L protein
, glycine cleavage system protein L
, lipoamide dehydrogenase
, lipoamide reductase
, lipoyl dehydrogenase
, branched chain alpha-keto acid dehydrogenase complex subunit E3
, dihydrolipoamide dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex)
, dihydrolipoamide dehydrogenase
, dihydrolipoyl dehydrogenase
, protein BfmBC
, dihydrolipoamide:NAD oxidoreductase
, glycine cleavage system L-protein
, dihydrolipoamide: NAD+ oxidoreductase
, Dihydrolipoyl dehydrogenase, mitochondrial