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.