Conformational and functional significance of residue proline 17 in chicken muscle adenylate kinase

FEBS Letters

Pan, Xianming¹  Wang, Chu¹  Zhang, Yu¹  Sheng, Xiangrong¹  Jing, Guozhong¹ 

[1] National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, PR China

关键词: Adenylate kinase;    Proline residue;    Multiple conformation;    Kinetics;    AK;    adenylate kinase;    ANS;    8-anilino-1-naphthalene sulfonic acid;    Ap5A;    P1;    P5-bis(adenosine-5′-)pentaphosphate;   

DOI  :  10.1016/S0014-5793(01)03092-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of mutation proline 17 on the multiple conformations and catalytic function in chicken muscle adenylate kinase (AK) has been studied. The substitution of proline 17 with glycine or valine altered the distribution of multiple conformations. Compared with the wild-type enzyme, the P17G and P17V mutants contained decreased fraction of minor conformer from 18% to 9% and 11%, respectively. Due to the mutation, the enzyme showed lower secondary structural content, poorer affinity to substrates or substrate analogues, and reduced catalytic efficiency. The results revealed the significance of proline 17 in the conformation and function of AK.

【 授权许可】

Unknown