Conformational and functional significance of residue proline 17 in chicken muscle adenylate kinase
Year: 2001
Type: article
Abstract: 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.
Source: FEBS Letters
Authors: Xiangrong Sheng, Xianming Pan, Chu Wang, Yu Zhang, Guozhong Jing
Institutions: Chinese Academy of Sciences, Institute of Biophysics
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Award: 腺苷酸激酶天然态构象多型性及其生物功能
OpenAlex ID: W2135350245
