Inhibiting sperm pyruvate dehydrogenase complex and its E3 subunit, dihydrolipoamide dehydrogenase affects fertilization in Syrian hamsters. [PDF]
BACKGROUND/AIMS: The importance of sperm capacitation for mammalian fertilization has been confirmed in the present study via sperm metabolism.
Archana B Siva+5 more
doaj +3 more sources
Large yellow croaker (Larimichthys crocea), an economically important marine fish in China, has suffered from serious vibriosis, which has resulted in great economic losses for the large yellow croaker industry.
Xiaomeng Li+6 more
doaj +2 more sources
Rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3. [PDF]
Drugs targeting MDM2's hydrophobic pocket activate p53. However, these agents act allosterically and have agonist effects on MDM2's protein interaction landscape. Dominant p53-independent MDM2-drug responsive-binding proteins have not been stratified. We
Way L+7 more
europepmc +4 more sources
The natural history of dihydrolipoamide dehydrogenase deficiency in Israel
Dihydrolipoamide dehydrogenase (DLD) deficiency is an ultra‐rare autosomal‐recessive inborn error of metabolism, affecting no less than five mitochondrial multienzyme complexes.
B. Pode-Shakked+11 more
semanticscholar +3 more sources
A pH-dependent kinetic model of dihydrolipoamide dehydrogenase from multiple organisms. [PDF]
Dihydrolipoamide dehydrogenase is a flavoenzyme that reversibly catalyzes the oxidation of reduced lipoyl substrates with the reduction of NAD+ to NADH.
Moxley MA, Beard DA, Bazil JN.
europepmc +2 more sources
The Pyruvate and α-Ketoglutarate Dehydrogenase Complexes of Pseudomonas aeruginosa Catalyze Pyocyanin and Phenazine-1-carboxylic Acid Reduction via the Subunit Dihydrolipoamide Dehydrogenase. [PDF]
Phenazines are a class of redox-active molecules produced by diverse bacteria and archaea. Many of the biological functions of phenazines, such as mediating signaling, iron acquisition, and redox homeostasis, derive from their redox activity.
Glasser NR, Wang BX, Hoy JA, Newman DK.
europepmc +3 more sources
An Updated View on the Molecular Pathomechanisms of Human Dihydrolipoamide Dehydrogenase Deficiency in Light of Novel Crystallographic Evidence. [PDF]
Dihydrolipoamide dehydrogenase (LADH, E3) deficiency is a rare (autosomal, recessive) genetic disorder generally presenting with an onset in the neonatal age and early death; the highest carrier rate has been found among Ashkenazi Jews.
Ambrus A.
europepmc +2 more sources
Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants. [PDF]
Human dihydrolipoamide dehydrogenase (hLADH, hE3) deficiency (OMIM# 246900) is an often prematurely lethal genetic disease usually caused by inactive or partially inactive hE3 variants.
Szabo E+14 more
europepmc +2 more sources
Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis. [PDF]
Metabolic control of gene expression coordinates the levels of specific gene products to meet cellular demand for their activities. This control can be exerted by metabolites acting as regulatory signals and/or a class of metabolic enzymes with dual ...
Alexandra-Viola Bohne+6 more
doaj +5 more sources
Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component of human ketoacid dehydrogenase complexes [PDF]
cDNA clones comprising the entire coding region for human dihydrolipoamide dehydrogenase (dihydrolipoamide:NAD+ oxidoreductase, EC 1.8.1.4) have been isolated from a human liver cDNA library.
Carothers, Donna J.+8 more
core +2 more sources