Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.3.3 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Apostichopus japonicus

Protein Variants

Protein Variants Comment Organism
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

General Stability Organism
the N-terminal of arginine kinase plays an important role in maintaining the conformational stability and catalytic function of the enzyme Apostichopus japonicus

Organism

Organism UniProt Comment Textmining
Apostichopus japonicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Apostichopus japonicus