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Biochemical characterization of enoyl reductase involved in Type II fatty acid synthesis in the intestinal coccidium Eimeria tenella (Phylum Apicomplexa)

文献类型： 外文期刊

作者： Cai, Xiaomin 1 ; Fuller, A. Lorraine 2 ; McDougald, Larry R. 2 ; Tan, Xiangshi 3 ; Cai, Jianping; Wang, Feng; Sa 1 ;

作者机构： 1.Texas A&M Univ, Dept Vet Pathobiol, College Stn, TX 77843 USA

2.Texas A&M Univ, Dept Vet Pathobiol, College Stn, TX 77843 USA; Univ Georgia, Dept Poultry Sci, Athens, GA 30602 USA; Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA; Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA; Texas A&M Univ, Fac Genet Program, College Stn, TX 77843 USA; Guangdong Acad Agr Sci, Inst Vet Med, Guangzhou, Peoples R China

3.Texas A&M Univ, Dept Vet Pathobiol, College Stn, TX 77843 USA; Univ Georgia, Dept Poultry Sci, Athens, GA 30602 USA; Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA; Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77

关键词： Apicomplexa;Eimeria tenella;enoyl reductase;kinetics;apicoplast;CARRIER PROTEIN REDUCTASE;PLASMODIUM-FALCIPARUM;ACP REDUCTASE;CRYPTOSPORIDIUM-PARVUM;ESCHERICHIA-COLI;DRUG TARGETS;INHIBITION;TRICLOSAN;APICOPLAST;BIOSYNTHESIS

期刊名称：FEMS MICROBIOLOGY LETTERS （ 影响因子：2.742； 五年影响因子：2.856 ）

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收录情况： SCI

摘要： An enoyl reductase (EtENR) closely related to those of green algae and involved in Type II fatty acid synthesis was characterized and localized to the apicoplast in the coccidium Eimeria tenella. Biochemical analysis using native EtENR protein extracted from parasites confirmed its function as an enoyl reductase using NADH as a cofactor. However, the recombinant form (rEtENR) expressed in bacteria was only able to oxidize NADH, but unable to transfer the electron to enoyl-CoA, possibly due to the inappropriate folding of rEtENR expressed in bacteria. The functions of both native and recombinant EtENR could be inhibited by triclosan (IC50=1.45 mu M), suggesting that this enzyme may be explored as a drug target against coccidiosis.

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