Literature summary extracted from
Liu, T.T.; Wang, X.C.
Effects of N-terminal deletion mutation on arginine kinase from the sea cucumber Stichopus japonicus (2008), Int. J. Biol. Macromol., 42, 68-74.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.3.3 |
expression in Escherichia coli BL21 |
Apostichopus japonicus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.3.3 |
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 |
General Stability
EC Number |
General Stability |
Organism |
---|
2.7.3.3 |
the N-terminal of arginine kinase plays an important role in maintaining the conformational stability and catalytic function of the enzyme |
Apostichopus japonicus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.3.3 |
Apostichopus japonicus |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.3.3 |
- |
Apostichopus japonicus |