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

Citation
Xr. Sheng et al., Conformational and functional significance of residue proline 17 in chicken muscle adenylate kinase, FEBS LETTER, 508(3), 2001, pp. 318-322
Citations number
25
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
508
Issue
3
Year of publication
2001
Pages
318 - 322
Database
ISI
SICI code
0014-5793(20011123)508:3<318:CAFSOR>2.0.ZU;2-G
Abstract
The effect of mutation proline 17 on the multiple conformations and catalyt ic function in chicken muscle aden) late 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 secon dary structural content, poorer affinity to substrates or substrate analogu es, and reduced catalytic efficiency. The results revealed the significance of proline 17 in the conformation and function of AK. (C) 2001 Published b y Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.