3B46
Crystal Structure of Bna3p, a Putative Kynurenine Aminotransferase from Saccharomyces cerevisiae
3B46 の概要
| エントリーDOI | 10.2210/pdb3b46/pdb |
| 分子名称 | Aminotransferase BNA3 (2 entities in total) |
| 機能のキーワード | kynurenine aminotransferase, llp, plp, cytoplasm, mitochondrion, pyridoxal phosphate, transferase |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
| 細胞内の位置 | Cytoplasm: P47039 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 101261.02 |
| 構造登録者 | |
| 主引用文献 | Wogulis, M.,Chew, E.R.,Donohoue, P.D.,Wilson, D.K. Identification of Formyl Kynurenine Formamidase and Kynurenine Aminotransferase from Saccharomyces cerevisiae Using Crystallographic, Bioinformatic and Biochemical Evidence. Biochemistry, 47:1608-1621, 2008 Cited by PubMed Abstract: The essential enzymatic cofactor NAD+ can be synthesized in many eukaryotes, including Saccharomyces cerevisiae and mammals, using tryptophan as a starting material. Metabolites along the pathway or on branches have important biological functions. For example, kynurenic acid can act as an NMDA antagonist, thereby functioning as a neuroprotectant in a wide range of pathological states. N-Formyl kynurenine formamidase (FKF) catalyzes the second step of the NAD+ biosynthetic pathway by hydrolyzing N-formyl kynurenine to produce kynurenine and formate. The S. cerevisiae FKF had been reported to be a pyridoxal phosphate-dependent enzyme encoded by BNA3. We used combined crystallographic, bioinformatic and biochemical methods to demonstrate that Bna3p is not an FKF but rather is most likely the yeast kynurenine aminotransferase, which converts kynurenine to kynurenic acid. Additionally, we identify YDR428C, a yeast ORF coding for an alpha/beta hydrolase with no previously assigned function, as the FKF. We predicted its function based on our interpretation of prior structural genomics results and on its sequence homology to known FKFs. Biochemical, bioinformatics, genetic and in vivo metabolite data derived from LC-MS demonstrate that YDR428C, which we have designated BNA7, is the yeast FKF. PubMed: 18205391DOI: 10.1021/bi701172v 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






