| Name | cytochrome P450 (protein family or complex) |
|---|---|
| Synonyms | cytochrome P450; cytochrome P 450; CYP450; CYP 450 |
| Name | cyanamide |
|---|---|
| CAS | cyanamide |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 1608302 | Hu ML, Tappel AL: and antioxidants protect microsomes against lipid peroxidation and enzyme inactivation. Lipids. 1992 Jan;27(1):42-5. In microsomes incubated with 2.5 microM iron as ferric and 50 microM ALDH, glucose-6-phosphatase (G6Pase) and cytochrome P450 (Cyt-P450) levels decreased rapidly and concurrently with increased levels of thiobarbituric acid-reactive substances. Inhibition of ALDH by cyanamide injection of rats exacerbated the inactivation of G6Pase in microsomes incubated with 0.1 mM, but not 25 microM (4-HN). 4-HN did not stimulate lipid peroxidation. |
1(0,0,0,1) | Details |
| 10424762 | Clement B, Boucher JL, Mansuy D, Harsdorf A: Microsomal formation of and cyanamides from non-physiological N-hydroxyguanidines: N-hydroxydebrisoquine as a model substrate. Biochem Pharmacol. 1999 Aug 1;58(3):439-45. In conclusion, similarities (formation of a urea derivative) and differences (formation of a cyanamide derivative) between the physiological oxidation of N-- by synthases and non-physiological N-hydroxyguanidines by cytochrome P-450 were observed. |
82(1,1,1,2) | Details |
| 3426683 | Shirota FN, DeMaster EG, Kwon CH, Nagasawa HT: Metabolism of cyanamide to and an inhibitor of aldehyde dehydrogenase (ALDH) by rat liver microsomes. Alcohol Alcohol Suppl. 1987;1:219-23. These results suggest that while catalase is responsible in major part for the oxidation of cyanamide to by uninduced microsomes, the participation of the hepatic cytochrome P-450 enzymes cannot be ruled out in PB-induced microsomes. |
32(0,1,1,2) | Details |
| 8435094 | Khan S, Sood C, O'Brien PJ: Molecular mechanisms of dibromoalkane cytotoxicity in isolated rat hepatocytes. Biochem Pharmacol. 1993 Jan 26;45(2):439-47. Bromoaldehydic metabolites formed by cytochrome P450-dependent mixed-function oxidases were probably responsible for lipid peroxidation as deuterated 1,2-dibromoethane (d4-DBE) induced less lipid peroxidation and was less cytotoxic even though GSH was depleted as rapidly and as effectively. Furthermore, hepatocyte susceptibility to dibromoalkanes was increased markedly if aldehyde dehydrogenase was inactivated with disulfiram, cyanamide or chloral hydrate. |
4(0,0,0,4) | Details |
| 11258969 | Moali C, Boucher JL, Renodon-Corniere A, Stuehr DJ, Mansuy D: Oxidations of N (omega)-hydroxyarginine analogues and various N-hydroxyguanidines by NO synthase II: key role of in the reaction mechanism and substrate selectivity. Chem Res Toxicol. 2001 Feb;14(2):202-10. In the case of compound 8, formation of the corresponding urea and cyanamide was also detected besides that of NO2 (-) and NO3 (-). They exhibit characteristics very similar to those previously reported for microsomal cytochrome P450-catalyzed oxidation of N-hydroxyguanidines. |
1(0,0,0,1) | Details |
| 8394073 | Mattia CJ, Adams JD Jr, Bondy SC: Free radical induction in the brain and liver by products of toluene catabolism. Biochem Pharmacol. 1993 Jul 6;46(1):103-10. Thus, ROS generation during toluene catabolism may occur at two steps: cytochrome P450 oxidation and aldehyde dehydrogenase oxidation. Pretreatment of rats in vivo with 4-methylpyrazole, an alcohol dehydrogenase inhibitor, or cyanamide, an aldehyde dehydrogenase inhibitor, prior to exposure to toluene, caused a significant decrease and increase, respectively, in toluene-stimulated rates of ROS generation in the CNS and liver. |
1(0,0,0,1) | Details |
| 2886311 | Rikans LE: The oxidation of acrolein by rat liver aldehyde dehydrogenases. Drug Metab Dispos. 1987 May-Jun;15(3):356-62. The metabolism of acrolein by low Km aldehyde dehydrogenase activities was markedly depressed in mitochondrial or cytosolic fractions from rats pretreated with cyanamide (2 mg/kg for 1 hr) or disulfiram (100 mg/kg for 24 hr). Hepatotoxicity was assessed on the basis of elevated serum alanine aminotransferase and sorbitol dehydrogenase activities and the loss of microsomal cytochrome P-450. |
1(0,0,0,1) | Details |
| 1632841 | Aragon CM, Rogan F, Amit Z: metabolism in rat brain homogenates by a catalase-H2O2 system. Biochem Pharmacol. 1992 Jul 7;44(1):93-8. Homogenates of perfused brains of rats treated with 3-amino-1,2,4-triazole or cyanamide (another H2O2-dependent catalase blocker) also showed a dose-dependent reduction of the obtained. |
0(0,0,0,0) | Details |
| 6861004 | Loomis CW, Brien JF: Specificity of hepatic aldehyde dehydrogenase inhibition by carbimide cyanamide) in the rat. Can J Physiol Pharmacol. 1983 Apr;61(4):431-5. |
0(0,0,0,0) | Details |
| 9860831 | Jousserandot A, Boucher JL, Henry Y, Niklaus B, Clement B, Mansuy D: Microsomal cytochrome P450 dependent oxidation of N-hydroxyguanidines, amidoximes, and ketoximes: mechanism of the oxidative cleavage of their C=N (OH) bond with formation of oxides. Biochemistry. 1998 Dec 8;37(49):17179-91. Oxidation of N-(4-chlorophenyl)-N'-- led to the formation of the corresponding urea and cyanamide in addition to NO, NO2-, and NO3-. |
0(0,0,0,0) | Details |
| 1443429 | Gill K, Menez JF, Lucas D, Deitrich RA: Enzymatic production of from in rat brain tissue. Alcohol Clin Exp Res. 1992 Oct;16(5):910-5. On the other hand, treatment with the catalase inhibitors azide, cyanamide, or 3-amino-1,2,4-triazole blocked the production of AcHO while the addition of exogenous peroxide or a peroxide-generating system enhanced the production of AcHO. |
0(0,0,0,0) | Details |