Jeerang WongtrakulSaengtong PongjaroenkitPosri LeelapatWoottichai NachaiwiengLa Aied PrapanthadaraAlbert J. KettermanChiang Mai UniversityMaejo UniversityMahidol University2018-09-242018-09-242010-02-01Journal of Medical Entomology. Vol.47, No.2 (2010), 162-171002225852-s2.0-77949302356https://repository.li.mahidol.ac.th/handle/123456789/28539Glutathione transferases (GSTs) (E.C.2.5.1.18) are multifunctional enzymes involved in the detoxification of many exogenous and endogenous compounds. This study aimed to characterize several new GSTs from Anopheles cracens, a major Thai malaria vector formerly known as Anopheles dirus. The three recombinant enzymes obtained were from the epsilon, theta and omega classes. They showed 8093% identity to orthologous An. gambiae GSTs. AcGSTE2-2 possessed peroxidase activity that cannot be detected for the An. gambiae AgGSTE2-2. AcGSTT1-1 had high activity toward several substrates that are specific for mammalian theta class. The AcGSTO1-1 can use 1-chloro-2,4-dinitrobenzene, dichloroacetic acid, and hydroxyethyl disulfide substrates. The enzymes bound but did not metabolize the organophosphate temephos. The epsilon AcGSTE2-2 functioned as a peroxidase and DDT metabolizing enzyme. The theta AcGSTT1-1 functioned not only as peroxidase but also acted as a binding protein for organophosphates. The omega GST had thiol transferase activity suggesting a role in oxidative stress response. © 2010 Entomological Society of America.Mahidol UniversityAgricultural and Biological SciencesImmunology and MicrobiologyMedicineArticleSCOPUS10.1603/ME09132