1B9L
7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE
1B9L の概要
| エントリーDOI | 10.2210/pdb1b9l/pdb |
| 分子名称 | PROTEIN (EPIMERASE) (1 entity in total) |
| 機能のキーワード | epimerase, isomerase |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 112824.19 |
| 構造登録者 | Ploom, T.,Haussmann, C.,Hof, P.,Steinbacher, S.,Bacher, A.,Richardson, J.,Huber, R. (登録日: 1999-02-11, 公開日: 2000-02-18, 最終更新日: 2023-12-27) |
| 主引用文献 | Ploom, T.,Haussmann, C.,Hof, P.,Steinbacher, S.,Bacher, A.,Richardson, J.,Huber, R. Crystal structure of 7,8-dihydroneopterin triphosphate epimerase. Structure Fold.Des., 7:509-516, 1999 Cited by PubMed Abstract: Dihydroneopterin triphosphate (H2NTP) is the central substrate in the biosynthesis of folate and tetrahydrobiopterin. Folate serves as a cofactor in amino acid and purine biosynthesis and tetrahydrobiopterin is used as a cofactor in amino acid hydroxylation and nitric oxide synthesis. In bacteria, H2NTP enters the folate biosynthetic pathway after nonenzymatic dephosphorylation; in vertebrates, H2NTP is used to synthesize tetrahydrobiopterin. The dihydroneopterin triphosphate epimerase of Escherichia coli catalyzes the inversion of carbon 2' of H2NTP. PubMed: 10378270DOI: 10.1016/S0969-2126(99)80067-7 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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