Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.1 (NADPH-diaphorase)
 3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a series of 3 experiments, beagle dogs were dosed orally with lead carbonate and the histochemical and histological changes in the liver and kidney assessed. Dosing at 50 mg/kg per day for 5 weeks resulted in well documented histological changes in the kidney and hydropic degeneration in the liver; significant alterations in the activity of the majority of enzymes studied were also seen in both organs. In dogs dosed for one week at 50 or 100 mg/kg no histological changes were seen and histochemical alterations were mainly confined to the dehydrogenases and NADPH diaphorase. A third group of dogs were dosed for 3 weeks; during a subsequent recovery period of almost 2 months the mild clinical effects produced by lead during the dosing period were quickly reversible except in 2 dogs. At the end of the recovery period histochemical alterations were evident in both organs of these 2 dogs principally shown by a reduction in the dehydrogenases of the liver. The findings are interpreted as an effect by lead on a range of cellular enzymes particularly those involved in energy production, these effects being still demonstrable after an extended recovery period.
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PMID:Histochemical and histological effects of lead on the liver and kidney of the dog. 18 94

Eleven flavoproteins from the old yellow enzyme family were found to catalyze the disproportionation ("dismutation") of conjugated enones. Incomplete conversions, which were attributed to enzyme inhibition by the co-product phenol could be circumvented via in situ co-product removal by scavenging the phenol using the polymeric adsorbent MP-carbonate. The optimized system allowed to reduce an alkene activated by ester groups in a "coupled-substrate" approach via nicotinamide-free hydrogen transfer with >90% conversion and complete stereoselectivity.
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PMID:Overcoming co-product inhibition in the nicotinamide independent asymmetric bioreduction of activated C=C-bonds using flavin-dependent ene-reductases. 2379 4