Evidence that the amino acid residue P272 of arginine kinase is involved in its activity, structure and stability.
In this research, the role of amino acid residue P272 of arginine kinase (AK) was investigated by site-directed mutagenesis. When the structure of AK was impaired by mutation, AK was in a partially unfolded state with more hydrophobic exposure, which was prone to aggregate under environmental stresses. Mutation at this position influences transition from the molten globule intermediate to the native state in folding process. The results provided herein may suggest that some residues near the active site may play a relatively important role in keeping AK activity and structural stability.
Wu
Qing-Yun
QY
College of Life Science, Shandong Agricultural University, Tai'an, Shandong 271018, PR China.
Li
Feng
F
Wang
Xiao-Yun
XY
D000818:Animals; D001122:Arginine Kinase / Q000737:chemistry* / Q000378:metabolism*; D004795:Enzyme Stability; D006110:Grasshoppers / Q000201:enzymology*; D019791:Guanidine / Q000494:pharmacology; D009154:Mutation / Q000235:genetics; D011392:Proline / Q000378:metabolism*; D017510:Protein Folding / Q000187:drug effects; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D013696:Temperature
D011392:Proline; D001122:Arginine Kinase; D019791:Guanidine