3PD6
Crystal structure of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV
3PD6 の概要
| エントリーDOI | 10.2210/pdb3pd6/pdb |
| 関連するPDBエントリー | 3PDB |
| 分子名称 | Aspartate aminotransferase, mitochondrial, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, GLYCEROL, ... (6 entities in total) |
| 機能のキーワード | alpha & beta protein, aminotransferase, plp-binding, mitochondrion, transferase |
| 由来する生物種 | Mus musculus (mouse) 詳細 |
| 細胞内の位置 | Mitochondrion matrix: P05202 P05202 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 180909.92 |
| 構造登録者 | Han, Q.,Robinson, H.,Cai, T.,Tagle, D.A.,Li, J. (登録日: 2010-10-22, 公開日: 2010-11-10, 最終更新日: 2023-12-06) |
| 主引用文献 | Han, Q.,Robinson, H.,Cai, T.,Tagle, D.A.,Li, J. Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV. Biosci.Rep., 31:323-332, 2011 Cited by PubMed Abstract: Mammalian mAspAT (mitochondrial aspartate aminotransferase) is recently reported to have KAT (kynurenine aminotransferase) activity and plays a role in the biosynthesis of KYNA (kynurenic acid) in rat, mouse and human brains. This study concerns the biochemical and structural characterization of mouse mAspAT. In this study, mouse mAspAT cDNA was amplified from mouse brain first stand cDNA and its recombinant protein was expressed in an Escherichia coli expression system. Sixteen oxo acids were tested for the co-substrate specificity of mouse mAspAT and 14 of them were shown to be capable of serving as co-substrates for the enzyme. Structural analysis of mAspAT by macromolecular crystallography revealed that the cofactor-binding residues of mAspAT are similar to those of other KATs. The substrate-binding residues of mAspAT are slightly different from those of other KATs. Our results provide a biochemical and structural basis towards understanding the overall physiological role of mAspAT in vivo and insight into controlling the levels of endogenous KYNA through modulation of the enzyme in the mouse brain. PubMed: 20977429DOI: 10.1042/BSR20100117 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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