1DQU
CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS
1DQU の概要
エントリーDOI | 10.2210/pdb1dqu/pdb |
分子名称 | ISOCITRATE LYASE (1 entity in total) |
機能のキーワード | beta barrel, lyase |
由来する生物種 | Emericella nidulans |
細胞内の位置 | Glyoxysome : P28298 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 60398.34 |
構造登録者 | Britton, K.L.,Langridge, S.J.,Baker, P.J.,Weeradechapon, K.,Sedelnikova, S.E.,De Lucas, J.R.,Rice, D.W.,Turner, G. (登録日: 2000-01-05, 公開日: 2000-05-10, 最終更新日: 2024-02-07) |
主引用文献 | Britton, K.,Langridge, S.,Baker, P.J.,Weeradechapon, K.,Sedelnikova, S.E.,De Lucas, J.R.,Rice, D.W.,Turner, G. The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans. Structure Fold.Des., 8:349-362, 2000 Cited by PubMed Abstract: Isocitrate lyase catalyses the first committed step of the carbon-conserving glyoxylate bypass, the Mg(2+)-dependent reversible cleavage of isocitrate into succinate and glyoxylate. This metabolic pathway is an inviting target for the control of a number of diseases, because the enzymes involved in this cycle have been identified in many pathogens including Mycobacterium leprae and Leishmania. PubMed: 10801489DOI: 10.1016/S0969-2126(00)00117-9 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
構造検証レポート
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