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Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase

Journal of Microbiology 2020년 58권 7호 p.606 ~ 613
황지섭 ( Hwang Ji-Sub ) - Korea Polar Research Institute Unit of Research for Practical Application

 ( Jeong Chang-Sook ) - Korea Polar Research Institute Unit of Research for Practical Application
이창우 ( Lee Chang-Woo ) - Korea Polar Research Institute Unit of Research for Practical Application
신승철 ( Shin Seung-Chul ) - Korea Polar Research Institute Division of Life Sciences
김한우 ( Kim Han-Woo ) - Korea Polar Research Institute Unit of Research for Practical Application
이성구 ( Lee Sung-Gu ) - Korea Polar Research Institute Unit of Research for Practical Application
윤의정 ( Youn Ui-Joung ) - Korea Polar Research Institute Division of Life Sciences
이창섭 ( Lee Chang-Sup ) - Gyeongsang National University College of Pharmacy
오태진 ( Oh Tae-Jin ) - Sunmoon University Graduate School Department of Life Science and Biochemical Engineering
김학준 ( Kim Hak-Jun ) - Pukyong National University Department of Chemistry
 ( Park Hyun ) - Korea University College of Life Sciences and Biotechnology Division of Biotechnology
박현호 ( Park Hyun-Ho ) - Chung-Ang University College of Pharmacy
이준혁 ( Lee Jun-Hyuck ) - Korea Polar Research Institute Unit of Research for Practical Application

Abstract


Crystal structures of enoyl-coenzyme A (CoA) isomerase from Bosea sp. PAMC 26642 (BoECI) and enoyl-CoA hydratase from Hymenobacter sp. PAMC 26628 (HyECH) were determined at 2.35 and 2.70 A resolution, respectively. BoECI and HyECH are members of the crotonase superfamily and are enzymes known to be involved in fatty acid degradation. Structurally, these enzymes are highly similar except for the orientation of their C-terminal helix domain. Analytical ultracentrifugation was performed to determine the oligomerization states of BoECI and HyECH revealing they exist as trimers in solution. However, their putative ligand-binding sites and active site residue compositions are dissimilar. Comparative sequence and structural analysis revealed that the active site of BoECI had one glutamate residue (Glu135), this site is occupied by an aspartate in some ECIs, and the active sites of HyECH had two highly conserved glutamate residues (Glu118 and Glu138). Moreover, HyECH possesses a salt bridge interaction between Glu98 and Arg152 near the active site. This interaction may allow the catalytic Glu118 residue to have a specific conformation for the ECH enzyme reaction. This salt bridge interaction is highly conserved in known bacterial ECH structures and ECI enzymes do not have this type of interaction. Collectively, our comparative sequential and structural studies have provided useful information to distinguish and classify two similar bacterial crotonase superfamily enzymes.

키워드

crystal structure; enoyl-CoA isomerase; enoyl-CoA hydratase; X-ray crystallography
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