Publication: Expression and characterization of three new glutathione transferases, an epsilon (AcGSTE2-2), Omega (AcGSTO1-1), and Theta (AcGSTT1-1) from anopheles cracens (Diptera: Culicidae), a major thai malaria vector
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Issued Date
2010-02-01
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00222585
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2-s2.0-77949302356
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Medical Entomology. Vol.47, No.2 (2010), 162-171
Suggested Citation
Jeerang Wongtrakul, Saengtong Pongjaroenkit, Posri Leelapat, Woottichai Nachaiwieng, La Aied Prapanthadara, Albert J. Ketterman Expression and characterization of three new glutathione transferases, an epsilon (AcGSTE2-2), Omega (AcGSTO1-1), and Theta (AcGSTT1-1) from anopheles cracens (Diptera: Culicidae), a major thai malaria vector. Journal of Medical Entomology. Vol.47, No.2 (2010), 162-171. doi:10.1603/ME09132 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/28539
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Title
Expression and characterization of three new glutathione transferases, an epsilon (AcGSTE2-2), Omega (AcGSTO1-1), and Theta (AcGSTT1-1) from anopheles cracens (Diptera: Culicidae), a major thai malaria vector
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Abstract
Glutathione 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.