additional information |
deletion mutants of arginine kinase are constructed. The first 4, 6, 8 and 10 amino acids of the N-terminal are deleted. The deletion mutants assume less compact conformations compared to the wild-type, whereas no significant changes of the secondary or the quaternary structures are observed, implying that the deletions cause a perturbation in the tertiary structure or the hydrodynamic properties of the enzyme. The enzymatic and denaturing measurements show that removal of the N-terminal residues decrease the activity and stability of the enzyme markedly. The instability increases in accord with the increased number of amino acid residues removed from the N-terminal of the enzyme |
Apostichopus japonicus |