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Literature summary extracted from

  • Wu, Q.Y.; Li, F.; Wang, X.Y.; Chen, Z.J.
    Impact of inter-subunit interactions on the dimeric arginine kinase activity and structural stability (2011), Arch. Biochem. Biophys., 512, 61-68.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.3 expressed in Escherichia coli BL21(DE3) Codon Plus cells Apostichopus japonicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.3.3 D57A the mutation causes pronounced loss of activity and substrate synergism, and distinct conformational changes Apostichopus japonicus
2.7.3.3 D57E most of the kinetic parameters are similar to those of wild type enzyme. A small decrease in Kd/Km and kcat/Km (L-Arg) values indicate a slight loss of substrate synergism and catalytic efficiency Apostichopus japonicus
2.7.3.3 Q53A the mutation causes pronounced loss of activity and substrate synergism, and distinct conformational changes Apostichopus japonicus
2.7.3.3 Q53A/D57A the changes in kinetic parameters as well as the loss of substrate synergism of the double mutant are more severe than that of Q53A and D57A single mutant enzymes. In addition, the double mutant has the lowest affinity for ATP Apostichopus japonicus
2.7.3.3 Q53E most of the kinetic parameters are similar to those of wild type enzyme. A small decrease in Kd/Km and kcat/Km (L-Arg) values indicate a slight loss of substrate synergism and catalytic efficiency Apostichopus japonicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.3.3 0.413
-
 L-Arg native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 0.421
-
 L-Arg recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 0.578
-
 L-Arg mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 0.744
-
 L-Arg mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 0.814
-
 ATP native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 0.823
-
 ATP recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 0.988
-
 ATP mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 1.036
-
 L-Arg mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 1.132
-
 ATP mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 1.321
-
 ATP mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 1.571
-
 L-Arg mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 1.631
-
 ATP mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 2.726
-
 L-Arg mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 3.092
-
 ATP mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C 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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.3.3 muscle
-
 Apostichopus japonicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.3 ATP + L-Arg
-
 Apostichopus japonicus ADP + Nomega-phospho-L-Arg
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.3.3 dimer
-
 Apostichopus japonicus

Synonyms

EC Number Synonyms Comment Organism
2.7.3.3 ATP: L-arginine phosphotransferase
-
 Apostichopus japonicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.3.3 46 60 the activity of wild type enzyme changes a little after heat treatment for 10 min at temperatures below 45°C. A steep decrease of activity is observed after 10 min between 45 and 60°C, and a complete loss of activity occurs above 65°C. The midpoint of thermal inactivation of wild type enzyme is at about 52°C Apostichopus japonicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.3.3 4.38
-
 L-Arg mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 10.26
-
 L-Arg mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 13.09
-
 L-Arg mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 15.95
-
 L-Arg mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 23.33
-
 L-Arg mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 25.7
-
 L-Arg native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus
2.7.3.3 29.93
-
 L-Arg recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Apostichopus japonicus