| Name | alcohol dehydrogenase (protein family or complex) |
|---|---|
| Synonyms | ADH; alcohol dehydrogenase; alcohol dehydrogenases |
| Name | sodium azide |
|---|---|
| CAS | sodium azide |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 17597213 | Jamal M, Ameno K, Uekita I, Kumihashi M, Wang W, Ijiri I: Catalase mediates formation in the striatum of free-moving rats. Neurotoxicology. 2007 Nov;28(6):1245-8. Epub 2007 May 13. Rats received intraperitoneal EtOH (1g/kg) alone or in combination with 4-methylpyrazole (MP, 82 mg/kg, an alcohol dehydrogenase inhibitor), and/or catalase inhibitor sodium azide (AZ, 10mg/kg) or 3-amino-1,2,4-triazole (AT, 1g/kg), and/or cyanamide (CY, 50mg/kg, an aldehyde dehydrogenase inhibitor). |
31(0,1,1,1) | Details |
| 18494879 | Vicente C, Fontaniella B, Millanes AM, Sebastian B, Legaz ME: Enzymatic production of atranorin: a component of the oak moss absolute by immobilized lichen cells. Int J Cosmet Sci. 2003 Apr;25(1-2):25-9. This enhancement suggested the participation of an oxidase and an alcohol dehydrogenase to produce an -substituted phenolic acid, hematommic acid, as the most probable precursor of atranorin. The participation of both enzymes was confirmed by loading immobilized cells with sodium azide, an inhibitor of several metallo-oxidases, and pyrazole, an inhibitor of alcohol dehydrogenase, which impeded atranorin production and accumulated beta-methyl orsellinate (after azide loading) or its derivative (after pirazole treatment). |
2(0,0,0,2) | Details |
| 9546603 | Leskovac V, Trivic S, Anderson BM: Use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase. Mol Cell Biochem. 1998 Jan;178(1-2):219-27. In this study, we have reported the pH-dependence of dissociation constants for several competitive dead-end inhibitors of yeast enzyme froin their binary complexes with enzyme, or their ternary complexes with enzyme and NAD+ or inhibitors include: pyrazole, acetamide, sodium azide, 2-fluoroethanol, and 2,2,2-trifluorethanol. |
2(0,0,0,2) | Details |
| 16930212 | Zimatkin SM, Pronko SP, Vasiliou V, Gonzalez FJ, Deitrich RA: Enzymatic mechanisms of oxidation in the brain. . Alcohol Clin Exp Res. 2006 Sep;30(9):1500-5. Alcohol dehydrogenase plays a minor role, if any, in this process. RESULTS: The catalase inhibitors sodium azide (5 mM) and aminotriazole (5 mM) as well as CYP2E1 inhibitors diallyl sulfide (2 mM) and beta-phenethyl isothiocyanate (0.1 mM) lowered significantly the accumulation of the -derived AC and in brain homogenates. |
1(0,0,0,1) | Details |
| 11248219 | Miura T, Muraoka S, Fujimoto Y: Inactivation of kinase during the interaction of indomethacin with horseradish peroxidase and peroxide: involvement of indomethacin radicals. Chem Biol Interact. 2001 Mar 14;134(1):13-25. Other sulfhydryl enzymes, including alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase, were also readily inactivated during the interaction with HRP-H2O2. Sodium azide also blocked the formation of yellow substance and the inactivation of CK. |
1(0,0,0,1) | Details |
| 7814397 | Sakuraba H, Noguchi T: Alcohol:NAD+ oxidoreductase is present in rat liver peroxisomes. . J Biol Chem. 1995 Jan 6;270(1):37-40. The evidence was obtained that the enzyme differed from alcohol dehydrogenases and oxidizing systems found previously. The enzyme activity was not affected by pyrazole, an inhibitor of alcohol dehydrogenase and sodium azide, an inhibitor of catalase. |
1(0,0,0,1) | Details |
| 9726283 | Tillonen J, Kaihovaara P, Jousimies-Somer H, Heine R, Salaspuro M: Role of catalase in in vitro formation by human colonic contents. Alcohol Clin Exp Res. 1998 Aug;22(5):1113-9. It is believed that bacterial formation is mediated via microbial alcohol dehydrogenases (ADHs). The catalase inhibitors sodium azide and 3-amino-1,2,4-triazole (3-AT) markedly reduced the amount of produced from 22 mM in a concentration dependent manner compared with the control samples (0.1 mM sodium azide to 73% and 10 mM 3-AT to 67% of control). |
1(0,0,0,1) | Details |
| 9794700 | Haber PS, Apte MV, Applegate TL, Norton ID, Korsten MA, Pirola RC, Wilson JS: Metabolism of by rat pancreatic acinar cells. J Lab Clin Med. 1998 Oct;132(4):294-302. Phenanthroline (an inhibitor of classes I through III isoenzymes of alcohol dehydrogenase (ADH)) inhibited pancreatic oxidation by 90%, but 4-methylpyrazole (a class I and II ADH inhibitor), (a cytochrome P450 inhibitor), and sodium azide (a catalase inhibitor) had no effect. |
0(0,0,0,0) | Details |
| 8831581 | Haber PS, Gentry RT, Mak KM, Mirmiran-Yazdy SA, Greenstein RJ, Lieber CS: Metabolism of by human gastric cells: relation to first-pass metabolism. Gastroenterology. 1996 Oct;111(4):863-70. production was inhibited by 4-methylpyrazole (a class I alcohol dehydrogenase [ADH] inhibitor) and by m-nitrobenzaldehyde (a selective substrate for class IV ADH isoenzyme) but not by sodium azide (a catalase inhibitor). |
0(0,0,0,0) | Details |
| 9309319 | Hamby-Mason R, Chen JJ, Schenker S, Perez A, Henderson GI: Catalase mediates formation from in fetal and neonatal rat brain. Alcohol Clin Exp Res. 1997 Sep;21(6):1063-72. When incubated with CAT inhibitors (sodium azide or 3-aminotriazole), AcHO formation was blocked, whereas neither the alcohol dehydrogenase inhibitor, 4-methylpyrazole, nor P-450 inhibitors decreased AcHO production. |
0(0,0,0,0) | Details |
| 8892520 | Salmela KS, Kaihovaara P, Salaspuro M, Roine RP: Role of catalase in rat gastric mucosal metabolism in vitro. Alcohol Clin Exp Res. 1996 Sep;20(6):1011-5. Both formation and catalase activity peaked around the physiological pH, whereas alcohol dehydrogenase (ADH) activity was in that pH range low and reached peak values only at a higher pH of 9 to 10. Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE). 4-Methylpyrazole decreased ADH activity significantly, but did not affect formation. |
1(0,0,0,1) | Details |