2W4D
Acylphosphatase variant G91A from Pyrococcus horikoshii
2W4D の概要
| エントリーDOI | 10.2210/pdb2w4d/pdb |
| 関連するPDBエントリー | 1V3Z 1W2I 2W4C |
| 分子名称 | ACYLPHOSPHATASE, POTASSIUM ION, PHOSPHATE ION, ... (4 entities in total) |
| 機能のキーワード | hydrolase |
| 由来する生物種 | PYROCOCCUS HORIKOSHII |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 61857.48 |
| 構造登録者 | |
| 主引用文献 | Lam, S.Y.,Yeung, R.C.Y.,Yu, T.,Sze, K.,Wong, K.B. A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity. Plos Biol., 9:1027-, 2011 Cited by PubMed Abstract: Thermophilic enzymes are often less active than their mesophilic homologues at low temperatures. One hypothesis to explain this observation is that the extra stabilizing interactions increase the rigidity of thermophilic enzymes and hence reduce their activity. Here we employed a thermophilic acylphosphatase from Pyrococcus horikoshii and its homologous mesophilic acylphosphatase from human as a model to study how local rigidity of an active-site residue affects the enzymatic activity. PubMed: 21423654DOI: 10.1371/JOURNAL.PBIO.1001027 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 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






