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Literature summary for 2.7.3.3 extracted from

  • Liu, W.Q.; Rao, X.M.; Yu, Z.H.
    Alkaline unfolding and salt-induced folding of arginine kinase from shrimp Feneropenaeus chinensis under high pH conditions (2006), Int. J. Biol. Macromol., 38, 211-215.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Penaeus chinensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
2 * 40000, SDS-PAGE Penaeus chinensis
80000
-
SDS-PAGE Penaeus chinensis

Organism

Organism UniProt Comment Textmining
Penaeus chinensis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
Penaeus chinensis ADP + Nomega-phospho-L-Arg
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 40000, SDS-PAGE Penaeus chinensis

Synonyms

Synonyms Comment Organism
ATP: L-arginine phosphotransferase
-
Penaeus chinensis

pH Stability

pH Stability pH Stability Maximum Comment Organism
10 11 at pH 10.0, the relative activity is slightly reduced, in the pH range of 10–10.5, the relative activity decreases by almost 60% and above pH 11.0 the enzyme fully loses activity Penaeus chinensis
11 13 pH 11.0 is required to cause the complete loss of AK activity of the alkaline unfolded enzyme, the high pH denatured enzyme has some residual secondary and tertiary structure even at pH 13 Penaeus chinensis

Cofactor

Cofactor Comment Organism Structure
ATP
-
Penaeus chinensis