通过还原对古菌高丝氨酸脱氢酶激活的结构洞察。
Structural insight into activation of homoserine dehydrogenase from the archaeon via reduction.
作者信息
Tomonaga Yoshihisa, Kaneko Ryosuke, Goto Masaru, Ohshima Toshihisa, Yoshimune Kazuaki
机构信息
Department of Applied Molecular Chemistry, Graduate School of Industrial Technology, Nihon University, 1-2-1, Izumichou, Narashino, Chiba 275-8575, Japan.
Department of Biomolecular Science, Graduate School of Science, Toho University, 2-2-1, Miyama, Funabashi, Chiba 274-8510, Japan.
出版信息
Biochem Biophys Rep. 2015 Jul 15;3:14-17. doi: 10.1016/j.bbrep.2015.07.006. eCollection 2015 Sep.
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 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.
高丝氨酸脱氢酶（HSD；305个氨基酸残基）催化L-高丝氨酸和天冬氨酸4-半醛之间依赖NAD(P)的可逆反应，并参与天冬氨酸途径。嗜热古菌的HSD通过添加0.8 mM二硫苏糖醇而被显著激活（2.5倍）。同源二聚体的晶体结构表明，这种激活是由两个亚基C端区域中两个半胱氨酸残基（C303）之间形成的二硫键断裂引起的。
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