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Literature summary for 2.7.3.3 extracted from

  • Wang, W.D.; Wang, J.S.; Shi, Y.L.; Zhang, X.C.; Pan, J.C.; Zou, G.L.
    Mutation of residue arginine 330 of arginine kinase results in the generation of the oxidized form more susceptible (2013), Int. J. Biol. Macromol., 54, 238-243.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta cells Limulus polyphemus

Protein Variants

Protein Variants Comment Organism
R330K the mutant enzyme is more susceptible to oxidation than the wild type enzyme and shows 20% of wild type activity Limulus polyphemus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, bound to ATP Limulus polyphemus

Organism

Organism UniProt Comment Textmining
Limulus polyphemus P51541
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
53.78
-
mutant enzyme R330K, pH and temperature not specified in the publication Limulus polyphemus
268.6
-
recombinant wild type enzyme, pH and temperature not specified in the publication Limulus polyphemus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
Limulus polyphemus ADP + Nomega-phospho-L-Arg
-
r

Synonyms

Synonyms Comment Organism
ATP: L-arginine phosphotransferase
-
Limulus polyphemus