title: Val65 plays an important role in the substrate synergism, structural stability and activity of arginine kinase.
abstract: Arginine kinase, a member of phosphagen kinase, is a key enzyme in the cellular energy metabolism of invertebrates. A series mutation of conserved amino acid residue V65 was constructed to investigate its role in AK substrate synergism, structural stability and activity. Our study revealed that mutation in this conserved site could cause pronounced loss of activity, conformational changes and distinct substrate synergism alteration. Spectroscopic experiments indicated that these mutations influenced transition from the molten globule intermediate to the native state in folding process. These results provided herein suggest that amino acid residue V65 played a relatively important role in AK substrate synergism, structural stability and activity.
authors.affiliation: College of Life Science, Shandong Agricultural University, Tai'an, Shandong 271018, People's Republic of China.
authors.forename: Qing-Yun
authors.initials: QY
authors.lastname: Wu
authors.forename: Feng
authors.initials: F
authors.lastname: Li
authors.forename: Xiao-Yun
authors.initials: XY
authors.lastname: Wang
mesh_terms: D001122:Arginine Kinase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004795:Enzyme Stability; D007700:Kinetics; D009154:Mutation; D011489:Protein Denaturation; D020673:Protein Renaturation; D013696:Temperature; D014633:Valine
chemical_list: D001122:Arginine Kinase; D014633:Valine