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

被引：7
作者：
Cai, Xiaomin
Fuller, A. Lorraine
McDougald, Larry R.
Tan, Xiangshi
Cai, Jianping
Wang, Feng
Sacchettini, James C.
Zhu, Guan [1 ]
机构：
[1] Texas A&M Univ, Dept Vet Pathobiol, College Stn, TX 77843 USA
[2] Univ Georgia, Dept Poultry Sci, Athens, GA 30602 USA
[3] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA
[4] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
[5] Texas A&M Univ, Fac Genet Program, College Stn, TX 77843 USA
[6] Guangdong Acad Agr Sci, Inst Vet Med, Guangzhou, Peoples R China
来源：
FEMS MICROBIOLOGY LETTERS | 2007年 / 272卷 / 02期
关键词：
Apicomplexa; Eimeria tenella; enoyl reductase; kinetics; apicoplast;
D O I：
10.1111/j.1574-6968.2007.00767.x
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
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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收藏
页码：238 / 244
页数：7
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