title: The detoxification of xenobiotic compounds by Onchocerca gutturosa (Nematoda: Filarioidea).
abstract: In common with other helminths O. gutturosa appears to lack cytochrome P450 linked phase 1 enzymes and so its ability to metabolize aromatic nuclei may be severely restricted. The parasite could reduce azo- but not nitro-compounds and low levels of epoxide hydrolase activity were also detected. Glutathione S-transferase was the only phase 2 enzyme which could be demonstrated in O. gutturosa. High levels of glyoxalase I and in particular glyoxalase II were found in the parasite, suggesting an important role for these enzymes in detoxification.
authors.forename: K D
authors.initials: KD
authors.lastname: Pemberton
authors.forename: J
authors.initials: J
authors.lastname: Barrett
mesh_terms: D000818:Animals; D004851:Epoxide Hydrolases / Q000378:metabolism; D005260:Female; D005982:Glutathione Transferase / Q000378:metabolism; D008658:Inactivation, Metabolic; D007791:Lactoylglutathione Lyase / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D009601:Nitroreductases; D009854:Onchocerca / Q000201:enzymology*; D013869:Thiolester Hydrolases / Q000378:metabolism; D015262:Xenobiotics / Q000493:pharmacokinetics*; D000099301:Hydroxyacylglutathione Hydrolase
chemical_list: D004851:Epoxide Hydrolases; D005982:Glutathione Transferase; D007791:Lactoylglutathione Lyase; D009247:NADH, NADPH Oxidoreductases; D009601:Nitroreductases; D013869:Thiolester Hydrolases; D015262:Xenobiotics; D000099301:Hydroxyacylglutathione Hydrolase; C021106:azoreductase