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

abstract

• 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 (IC(50)=1.45 microM), suggesting that this enzyme may be explored as a drug target against coccidiosis.

authors

• Sacchettini, James
• Zhu, Guan

published proceedings

• FEMS Microbiol Lett

author list (cited authors)

• Cai, X., Lorraine Fuller, A., McDougald, L. R., Tan, X., Cai, J., Wang, F., Sacchettini, J. C., & Zhu, G.

citation count

• 6

complete list of authors

• Cai, Xiaomin||Lorraine Fuller, A||McDougald, Larry R||Tan, Xiangshi||Cai, Jianping||Wang, Feng||Sacchettini, James C||Zhu, Guan

publication date

• July 2007

publisher

• Oxford University Press (OUP)  Publisher

published in

• FEMS Microbiology Letters  Journal

keywords

• Animals
• Cloning, Molecular
• Coenzyme A
• Coenzymes
• DNA, Protozoan
• Eimeria Tenella
• Enzyme Inhibitors
• Fatty Acid Desaturases
• Gene Expression
• Microscopy, Confocal
• Molecular Sequence Data
• NAD
• Organelles
• Recombinant Proteins
• Sequence Analysis, DNA
• Triclosan

PubMed Central ID

• 17559403

Digital Object Identifier (DOI)

• 10.1111/j.1574-6968.2007.00767.x

start page

• 238

end page

• 244

volume

• 272

issue

• 2

URL

• http://dx.doi.org/10.1111/j.1574-6968.2007.00767.x