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Literature summary for 2.7.3.3 extracted from

  • Wu, Q.Y.; Guo, H.Y.; Geng, H.L.; Ru, B.M.; Cao, J.; Chen, C.; Zeng, L.Y.; Wang, X.Y.; Li, F.; Xu, K.L.
    T273 plays an important role in the activity and structural stability of arginine kinase (2014), Int. J. Biol. Macromol., 63, 21-28.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Locusta migratoria manilensis

Protein Variants

Protein Variants Comment Organism
additional information effects of the enzyme mutations on the enzyme's thermal inactivation andaggregation, the mutant enzymes show reduced thermal stability compared to the wild-type enzyme, overview Locusta migratoria manilensis
T273A site-directed mutagenesis, the mutation leads to significant loss of activity, obviously decreased substrate synergism and structural stability compared to the wild-type enzyme, the enzyme structure is impaired and the enzyme protein in a partially unfolded state Locusta migratoria manilensis
T273D site-directed mutagenesis, the mutation does not significantly affect the enzyme activity and structure Locusta migratoria manilensis
T273G site-directed mutagenesis, the mutation leads to significant loss of activity, obviously decreased substrate synergism and structural stability compared to the wild-type enzyme, the enzyme structure is impaired and the enzyme protein in a partially unfolded state Locusta migratoria manilensis
T273S site-directed mutagenesis, the mutation does not significantly affect the enzyme activity and structure Locusta migratoria manilensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information dissociation consants of wild-type and mutant enzymes, overview Locusta migratoria manilensis
0.94
-
L-arginine pH 8.0, 30°C, wild-type enzyme Locusta migratoria manilensis
0.95
-
L-arginine pH 8.0, 30°C, recombinant wild-type enzyme Locusta migratoria manilensis
0.98
-
L-arginine pH 8.0, 30°C, recombinant mutant T273S Locusta migratoria manilensis
1.04
-
L-arginine pH 8.0, 30°C, recombinant mutant T273D Locusta migratoria manilensis
1.27
-
ATP pH 8.0, 30°C, recombinant wild-type enzyme Locusta migratoria manilensis
1.28
-
ATP pH 8.0, 30°C, recombinant mutant T273S Locusta migratoria manilensis
1.29
-
ATP pH 8.0, 30°C, wild-type enzyme Locusta migratoria manilensis
1.32
-
ATP pH 8.0, 30°C, recombinant mutant T273D Locusta migratoria manilensis
1.64
-
ATP pH 8.0, 30°C, recombinant mutant T273A Locusta migratoria manilensis
1.7
-
ATP pH 8.0, 30°C, recombinant mutant T273G Locusta migratoria manilensis
3.05
-
L-arginine pH 8.0, 30°C, recombinant mutant T273A Locusta migratoria manilensis
3.18
-
L-arginine pH 8.0, 30°C, recombinant mutant T273G Locusta migratoria manilensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Locusta migratoria manilensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-arginine Locusta migratoria manilensis
-
ADP + Nomega-phospho-L-arginine
-
r

Organism

Organism UniProt Comment Textmining
Locusta migratoria manilensis A6M9J4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) Locusta migratoria manilensis

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Locusta migratoria manilensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
54.16
-
ATP pH 8.0, 30°C, recombinant mutant T273G Locusta migratoria manilensis
54.16
-
L-arginine pH 8.0, 30°C, recombinant mutant T273G Locusta migratoria manilensis
60.97
-
ATP pH 8.0, 30°C, recombinant mutant T273A Locusta migratoria manilensis
60.97
-
L-arginine pH 8.0, 30°C, recombinant mutant T273A Locusta migratoria manilensis
143.2
-
ATP pH 8.0, 30°C, recombinant mutant T273D Locusta migratoria manilensis
143.2
-
L-arginine pH 8.0, 30°C, recombinant mutant T273D Locusta migratoria manilensis
151.3
-
ATP pH 8.0, 30°C, recombinant mutant T273S Locusta migratoria manilensis
151.3
-
L-arginine pH 8.0, 30°C, recombinant mutant T273S Locusta migratoria manilensis
159.4
-
ATP pH 8.0, 30°C, recombinant wild-type enzyme Locusta migratoria manilensis
159.4
-
L-arginine pH 8.0, 30°C, recombinant wild-type enzyme Locusta migratoria manilensis
163
-
ATP pH 8.0, 30°C, wild-type enzyme Locusta migratoria manilensis
163
-
L-arginine pH 8.0, 30°C, wild-type enzyme Locusta migratoria manilensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Locusta migratoria manilensis

Cofactor

Cofactor Comment Organism Structure
ADP
-
Locusta migratoria manilensis
ATP
-
Locusta migratoria manilensis

General Information

General Information Comment Organism
additional information enzyme structure homology modelling, overview Locusta migratoria manilensis
additional information residue C271 is involved in the enzyme activity and constraining the orientation of the substrate arginine. Residue T273 interacts with C271 and plays a vital role in the enzyme activity, substrate synergism, and structural stability Locusta migratoria manilensis
physiological function arginine kinase is a key enzyme for cellular energy metabolism, catalyzing the reversible phosphoyl transfer from phosphoarginine to ADP in invertebrates Locusta migratoria manilensis