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Conformational and functional significance of residue proline 17 in chicken muscle adenylate kinase
Author(s) -
Sheng Xiangrong,
Pan Xianming,
Wang Chu,
Zhang Yu,
Jing Guozhong
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03092-7
Subject(s) - proline , adenylate kinase , chemistry , valine , biochemistry , mutant , enzyme , substrate (aquarium) , residue (chemistry) , stereochemistry , amino acid , biology , ecology , gene
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.