2VH7

Crystal structure of human common-type acylphosphatase

2VH7 の概要

• エントリーDOI: 10.2210/pdb2vh7/pdb
• 分子名称: ACYLPHOSPHATASE-1 (2 entities in total)
• 機能のキーワード: hydrolase, acetylation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11277.84

構造登録者

Yeung, R.C.Y.,Lam, Y.,Wong, K.B. (登録日: 2007-11-19, 公開日: 2009-03-17, 最終更新日: 2023-12-13)

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

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: 21423654
DOI: 10.1371/JOURNAL.PBIO.1001027

実験手法

X-RAY DIFFRACTION (1.45 Å)