| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8298284 | Biochemical and Biophysical Research Communications | 2009 | 5 Pages |
Abstract
MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate) synthase belongs to the superfamily of thiamin diphosphate-dependent decarboxylases, which converts isochorismate and 2-oxoglutarate to SHCHC, pyruvate, and carbon dioxide. Here, we report the first crystal structure of apo-MenD from Escherichia coli determined in tetragonal crystal form. The subunit displays the typical three-domain structure observed for ThDP-dependent enzymes. Analytical gel filtration shows that EcMenD behaves as a dimer as well as a tetramer. Circular dichroism and isothermal calorimetry results confirm EcMenD dependency on ThDP, which concomitantly helps to stabilize with better configuration.
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Authors
Amit Priyadarshi, Yasar Saleem, Ki Hyun Nam, Key-Sun Kim, Sam-Yong Park, Eunice EunKyeong Kim, Kwang Yeon Hwang,