| Name | cytochrome P450 (protein family or complex) |
|---|---|
| Synonyms | cytochrome P450; cytochrome P 450; CYP450; CYP 450 |
| Name | phorate |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 3354230 | Levi PE, Hodgson E: Stereospecificity in the oxidation of phorate and phorate sulphoxide by purified FAD-containing mono-oxygenase and cytochrome P-450 isozymes. Xenobiotica. 1988 Jan;18(1):29-39. Using purified FAD-containing mono-oxygenase and purified cytochrome P-450 isozymes isolated from mouse liver microsomes, the stereospecificity of the oxidation of phorate to (+)-and (-)-phorate sulphoxide and the further oxidations of the (+)-and (-)-phorate sulphoxides to the sulphone, the oxon sulphoxide and the oxon sulphone were examined. 2. |
227(2,4,4,7) | Details |
| 15294458 | Henderson MC, Krueger SK, Siddens LK, Stevens JF, Williams DE: S-oxygenation of the thioether organophosphate insecticides phorate and disulfoton by human lung flavin-containing monooxygenase 2. Biochem Pharmacol. 2004 Sep 1;68(5):959-67. As the sulfoxide of phorate is a markedly less effective acetylcholinesterase inhibitor than the cytochrome P450 metabolites (oxon, oxon sulfoxide or oxon sulfone), humans possessing the FMO2*1 allele may be more resistant to organophosphate-mediated toxicity when pulmonary metabolism is an important route of exposure or disposition. |
81(1,1,1,1) | Details |
| 3078287 | Hodgson E, Levi PE: Species, organ and cellular variation in the flavin-containing monooxygenase. Drug Metabol Drug Interact. 1988;6(3-4):219-33. The role of the FMO relative to cytochrome P-450 in the oxidation of the atoms of organosulfur compounds is considered with particular reference to the hepatatoxicant thiobenzamide, the insecticide phorate and the drug, thioridazine. |
31(0,1,1,1) | Details |
| 2859168 | Osimitz TG, Kulkarni AP: Polyamine effects on cytochrome P-450- and flavin-containing monooxygenase-mediated oxidation of xenobiotics. Drug Metab Dispos. 1985 Mar-Apr;13(2):197-203. Total phorate S-oxidation was stimulated by all the polyamines tested. |
3(0,0,0,3) | Details |
| 8571358 | Hodgson E, Ryu DY, Adams N, Levi PE: Biphasic responses in synergistic interactions. . Toxicology. 1995 Dec 28;105(2-3):211-6. These compounds may function as cytochrome P450 substrates, inhibitors and/or inducers. |
2(0,0,0,2) | Details |
| 7161848 | Hodgson E: Production of pesticide metabolites by oxidative reactions. J Toxicol Clin Toxicol. 1982 Aug;19(6-7):609-21. The cytochrome P-450-dependent monooxygenase system catalyzes a wide variety of oxidations of pesticide chemicals and related compounds. These include sulfoxidation of organophosphorus insecticides such as phorate and disulfoton, oxidative desulfuration of phosphonate insecticides such as fonofos and oxidation at the atom in such compounds as the cotton defoliant, folex. |
2(0,0,0,2) | Details |
| 14977868 | Usmani KA, Karoly ED, Hodgson E, Rose RL: In vitro sulfoxidation of thioether compounds by human cytochrome P450 and flavin-containing monooxygenase isoforms with particular reference to the CYP2C subfamily. Drug Metab Dispos. 2004 Mar;32(3):333-9. The sulfoxidation of the thioether pesticides, phorate, disulfoton, sulprofos, and methiocarb, was investigated. |
2(0,0,0,2) | Details |
| 10188187 | Hodgson E: Induction and inhibition of pesticide-metabolizing enzymes: roles in synergism of pesticides and pesticide action. Toxicol Ind Health. 1999 Jan-Mar;15(1-2):6-11. MDP compounds function as both inhibitors and inducers of cytochrome P450 isoforms, the two processes proceeding, in vivo, at different rates. The significance of this biphasic effect on multienzyme xenobiotic metabolizing systems is illustrated by considerations of the insecticide phorate. |
1(0,0,0,1) | Details |
| 1441608 | Hodgson E, Levi PE: The role of the flavin-containing monooxygenase (EC 1.14.13.8) in the metabolism and mode of action of agricultural chemicals. Xenobiotica. 1992 Sep-Oct;22(9-10):1175-83. The substrate specificity relative to agricultural chemicals is discussed and compared with that of the cytochrome P-450-dependent monooxygenase system. The relative activity of these two enzymes towards common substrates varies from substrate to substrate and from tissue to tissue as is shown in the case of the insecticide, phorate and the hepatotoxicant, thiobenzamide. 3. |
1(0,0,0,1) | Details |
| 12642463 | Usmani KA, Rose RL, Hodgson E: Inhibition and activation of the human liver microsomal and human cytochrome P450 3A4 metabolism of by deployment-related chemicals. Drug Metab Dispos. 2003 Apr;31(4):384-91. Cytochrome P450 (P450) enzymes are major catalysts involved in the metabolism of xenobiotics and endogenous substrates such as testosterone (TST). The greatest inhibition of TST metabolism in HLM was following preincubation with organophosphorus compounds, including chlorpyrifos, phorate, and fonofos, with up to 80% inhibition noticed for several metabolites including 6beta-OHTST. |
1(0,0,0,1) | Details |
| 7082342 | Hajjar NP, Hodgson E: Sulfoxidation of thioether-containing pesticides by the - dependent monooxygenase of pig liver microsomes. Biochem Pharmacol. 1982 Mar 1;31(5):745-52. The stoichiometric relationship between and substrate during the course of the reaction was 1:1, and the product, in the case of disulfoton and phorate, was the sulfoxide. |
0(0,0,0,0) | Details |