| Name | diaphorase |
|---|---|
| Synonyms | Diaphorase; DHQU; DIA 4; DIA4; DT diaphorase; DTD; Diaphorase (NADH/NADPH); Diaphorase (NADH/NADPH) (cytochrome b 5 reductase)… |
| Name | sodium arsenite |
|---|---|
| CAS | sodium arsenenite |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 11979426 | Seubert JM, Webb CD, Bend JR: Acute sodium arsenite treatment induces Cyp2a5 but not Cyp1a1 in the C57Bl/6 mouse in a tissue (kidney) selective manner. J Biochem Mol Toxicol. 2002;16(2):96-106. Modulation of hepatic and extrahepatic detoxication enzymes Cyp1a1, Cyp2a5, S-transferse Ya (GSTYa) and NAD (P) H:quinone oxidoreductase (QOR) dependent catalytic activity and mRNA levels were investigated at 1, 2, or 4 days in liver, lung, or kidney of male, adult CD57 Bl/6 mice treated sc with a single dose (85 micromol/kg) of sodium arsenite (As3+). |
31(0,1,1,1) | Details |
| 18474416 | Elbekai RH, El-Kadi AO: Arsenite and cadmium, but not induce NAD (P) H:quinone oxidoreductase 1 through transcriptional mechanisms, in spite of post-transcriptional modifications. Toxicol In Vitro. 2008 Aug;22(5):1184-90. Epub 2008 Mar 31. NAD (P) H:quinone oxidoreductase (Nqo1)-mediated detoxification of quinones plays a critical role in cancer prevention. |
1(0,0,0,1) | Details |
| 3896786 | Pinto MC, Mata AM, Lopez-Barea J: The redox interconversion mechanism of Saccharomyces cerevisiae glutathione reductase. Eur J Biochem. 1985 Sep 2;151(2):275-81. The glutathione reductase and transhydrogenase activities were similarly inactivated by and reactivated by GSH, while the diaphorase activity remained unaltered during redox interconversion of glutathione reductase. |
1(0,0,0,1) | Details |
| 9238525 | Kitamura S, Tatsumi K: -dependent reduction of tertiary amine N-oxide by rat liver cytosol. Biochem Mol Biol Int. 1997 Jun;42(2):271-6. is converted to its reduced form by a -reducing enzyme such as DT-diaphorase and the reduced nucleotide, followed by reduction of the tertiary amine N-oxide to the amine by the heme group of catalytic hemoproteins in the presence of reduced as an electron donor. |
1(0,0,0,1) | Details |
| 9143318 | Marcinkeviciene J, Blanchard JS: Catalytic properties of dehydrogenase from Mycobacterium smegmatis. Arch Biochem Biophys. 1997 Apr 15;340(2):168-76. The -reducing reaction was reversibly inactivated by sodium arsenite, but no decrease in diaphorase activity was observed under these conditions. |
0(0,0,0,0) | Details |