Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.5.2 (NQO1)
 6,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oral administration of Prudhoe Bay crude or Hibernia crude to nestling herring gulls increased the hepatic cytochrome P-450 content 4-fold. Concomitantly, there was an increase in various mixed-function oxidase and phase II enzyme activities. 7-Ethoxyresorufin O-deethylase was elevated 19-fold, benzo(a)pyrene 3-hydroxylase 6-fold, aniline hydroxylase 3-fold, and aminopyrine N-demethylase and uridine diphosphate glucuronyl transferase 2-fold. There was no change in reduced glutathione S-transferase activity. Renal mixed-function oxidase activities were also elevated. Herring gull livers contained very low levels of DT-diaphorase activity which was inducible 3- to 5-fold by oil administration.
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PMID:Effects of ingestion of hibernia and Prudhoe Bay crude oils on hepatic and renal mixed function oxidase in nestling herring gulls (Larus argentatus). 396 42

Diaphorase was studied as a possible oxidoreductase participating in NO production from some vasorelaxants. In the presence of NADH or NADPH, diaphorase can convert selected NO donors, glycerol trinitrate (GTN) and formaldoxime (FAL) to nitrites and nitrates with NO as an intermediate. This activity of diaphorase was inhibited by diphenyleneiodonium (DPI) (inhibitor of some NADPH-dependent flavoprotein oxidoreductases), while it remained uninhibited by NG-nitro-L-arginine methyl ester (inhibitor of NO synthase) 7-Ethoxyresorufin (inhibitor of cytochrome P-450 1A1 and cytochrome P-450 NADPH-dependent reductase) inhibited the conversion of GTN only. Existence of NO as an intermediate of the reaction was supported by results of electron paramagnetic resonance spectroscopy. In addition to its ability to affect the above mentioned NO donors, diaphorase was able to reduce 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) and thus to eliminate its NO scavenging effect. This activity of diaphorase could also be inhibited by DPI. The reaction of diaphorase with GTN and PTIO was not affected by superoxide dismutase (SOD) or catalase. Reaction of FAL with diaphorase was lowered with SOD by 38 % indicating the partial participation of superoxide anion probably generated by the reaction of diaphorase with NADH or NADPH. Catalase had no effect. Diaphorase could apparently be one of the enzymes participating in the metabolism of studied NO donors to NO. The easy reduction and consequent elimination of PTIO by diaphorase could affect its use as an NO scavenger in biological tissues.
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PMID:Diaphorase can metabolize some vasorelaxants to NO and eliminate NO scavenging effect of 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO). 1558 29