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Literature summary for 2.7.3.3 extracted from

  • Li, F.; Wu, Q.Y.; Wang, X.Y.
    The amino acid residue L113 is involved in arginine kinase activity and structural stability (2013), Int. J. Biol. Macromol., 52, 198-205.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) Codon Plus cells Locusta migratoria manilensis

Protein Variants

Protein Variants Comment Organism
L113D the mutant shows strongly decreased activity compared to the wild type enzyme Locusta migratoria manilensis
L113G the mutant shows decreased activity compared to the wild type enzyme Locusta migratoria manilensis
L113I the mutant shows about wild type Km and kcat values Locusta migratoria manilensis
L113K the mutant shows strongly decreased activity (10.3% catalytic efficiency) compared to the wild type enzyme Locusta migratoria manilensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.94
-
L-Arg native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
0.951
-
L-Arg recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
0.99
-
L-Arg mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
1.27
-
ATP recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
1.29
-
ATP native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
1.42
-
ATP mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
1.81
-
L-Arg mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
2.42
-
ATP mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
2.98
-
L-Arg mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
3.25
-
L-Arg mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
3.68
-
ATP mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
4.15
-
ATP mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis

Organism

Organism UniProt Comment Textmining
Locusta migratoria manilensis A6M9J4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
Locusta migratoria manilensis ADP + Nomega-phospho-L-Arg
-
?

Synonyms

Synonyms Comment Organism
ATP: L-arginine phosphotransferase
-
Locusta migratoria manilensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 65 the wild type enzyme retains its activity well at temperatures lower than 48°C, and then its activity shows a steep decrease from 45 to 60°C and completely loses its activity at temperatures above 65°C Locusta migratoria manilensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
56.21
-
L-Arg mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
64.43
-
L-Arg mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
105.6
-
L-Arg mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
152.2
-
L-Arg mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
159.4
-
L-Arg recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis
163
-
L-Arg native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C Locusta migratoria manilensis