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Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction |
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| Authors: | Yoshihisa Tomonaga Ryosuke Kaneko Masaru Goto Toshihisa Ohshima Kazuaki Yoshimune |
| Affiliation: | 1. Department of Applied Molecular Chemistry, Graduate School of Industrial Technology, Nihon University, 1-2-1, Izumichou, Narashino, Chiba 275-8575, Japan;2. Department of Biomolecular Science, Graduate School of Science, Toho University, 2-2-1, Miyama, Funabashi, Chiba 274-8510, Japan;3. Department of Biomedical Engineering, Osaka Institute of Technology, 5-16-1, Ohmiya, Asahi-ku, Osaka 535-8585, Japan |
| Abstract: | Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon Sulfolobus tokodaii was markedly activated (2.5-fold) by the addition of 0.8 mM dithiothreitol. The crystal structure of the homodimer indicated that the activation was caused by cleavage of the disulfide bond formed between two cysteine residues (C303) in the C-terminal regions of the two subunits. |
| Keywords: | Hyperthermophilic archaea Homoserine dehydrogenase Crystal structure Disulfide bond Activation |
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