Domain movement in rabbit muscle adenylate kinase might involve proline isomerization

FEBS Letters

Sheng, X.R¹  Zhang, H.J¹  Li, X.F¹  Pan, X.M¹  Zhou, J.M¹ 

[1] National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica Beijing, Beijing 100101, China

关键词: Rabbit muscle adenylate kinase;    Proline isomerization;    8-Anilino-1-naphthalenesulfonic acid;    Domain movement;    AK;    rabbit muscle adenylate kinase;    ANS;    8-anilino-1-naphthalenesulfonic acid;    PPIase;    peptidyl prolyl cis/trans-isomerases;    CK;    creatine kinase;   

DOI  :  10.1016/S0014-5793(97)00951-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The fluorescence probe, 8-anilino-1-naphthalenesulfonic acid (ANS), was used to monitor the induced-fit conformational movement in rabbit muscle adenylate kinase. In 50 mM Tris-HCl buffer (pH 8.1), the time course of ANS binding to rabbit muscle adenylate kinase is a biphasic process. The fast phase completes within the dead-time of the stopped-flow equipment used (about 15 ms), while the slow phase ends in about 10 minutes. In the presence of 2.0 μM peptidyl prolyl cis/trans-isomerase, the rate constant of the slow phase reaction is accelerated about 2.4-fold, suggesting that the domain movement during ANS binding to rabbit muscle adenylate kinase may involve proline isomerization. The activation energy of the slow phase was determined to be 74.6 kJ/mol, which is comparable to the activation energy of proline cis/trans-isomerization (about 80 kJ/mol).

【 授权许可】

Unknown