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Literature summary for 2.7.3.3 extracted from

  • Fujimoto, N.; Tanaka, K.; Suzuki, T.
    Amino acid residues 62 and 193 play the key role in regulating the synergism of substrate binding in oyster arginine kinase (2005), FEBS Lett., 579, 1688-1692.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K193G turnover number is 68% of the wild-type value, KM-value for L-arginine is 4.1fold higher than wild-type value, Km-value for ATP is 2.2fold higher than wild-type value Crassostrea sp.
K194R turnover number is 85% of the wild-type value, KM-value for L-arginine is 4.5fold higher than wild-type value, Km-value for ATP is 1.3fold higher than wild-type value Crassostrea sp.
N62D turnover number is 88% of the wild-type value, KM-value for L-arginine is 1.1fold lower than wild-type value, Km-value for ATP is 1.2fold higher than wild-type value Crassostrea sp.
N62D/K193R turnover number is 89% of the wild-type value, KM-value for L-arginine is 2.3fold higher than wild-type value, Km-value for ATP is 1.6fold higher than wild-type value Crassostrea sp.
N62G turnover number is 53% of the wild-type value, KM-value for L-arginine is identical to wild-type value, Km-value for ATP is 1.2fold lower than wild-type value Crassostrea sp.
N62G/K193G turnover number is 51% of the wild-type value, KM-value for L-arginine is 4.1fold higher than wild-type value, Km-value for ATP is 3.9fold higher than wild-type value Crassostrea sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.31
-
L-arginine pH 7.9, 25°C, mutant enzyme N62D Crassostrea sp.
0.35
-
L-arginine pH 7.9, 25°C, mutant enzyme N62G Crassostrea sp.
0.35
-
L-arginine pH 7.9, 25°C, wild-type enzyme Crassostrea sp.
0.81
-
L-arginine pH 7.9, 25°C, mutant enzyme N62D/K193R Crassostrea sp.
0.82
-
ATP pH 7.9, 25°C, mutant enzyme N62G Crassostrea sp.
0.97
-
ATP pH 7.9, 25°C, wild-type enzyme Crassostrea sp.
1.17
-
ATP pH 7.9, 25°C, mutant enzyme N62D Crassostrea sp.
1.25
-
ATP pH 7.9, 25°C, mutant enzyme K193R Crassostrea sp.
1.44
-
L-arginine pH 7.9, 25°C, mutant enzyme N62G/K193G Crassostrea sp.
1.45
-
L-arginine pH 7.9, 25°C, mutant enzyme K193G Crassostrea sp.
1.57
-
L-arginine pH 7.9, 25°C, mutant enzyme K193R Crassostrea sp.
2.17
-
ATP pH 7.9, 25°C, mutant enzyme K193G Crassostrea sp.
2.54
-
ATP pH 7.9, 25°C, mutant enzyme N62D/K193R Crassostrea sp.
3.7 5 ATP pH 7.9, 25°C, mutant enzyme N62G/K193G Crassostrea sp.

Organism

Organism UniProt Comment Textmining
Crassostrea sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine key enzyme in invertebrate energy metabolism Crassostrea sp. ADP + Nomega-phosphono-L-arginine
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
24.4
-
ATP pH 7.9, 25°C, mutant enzyme N62G/K193G Crassostrea sp.
24.4
-
L-arginine pH 7.9, 25°C, mutant enzyme N62G/K193G Crassostrea sp.
25.3
-
ATP pH 7.9, 25°C, mutant enzyme N62G Crassostrea sp.
25.3
-
L-arginine pH 7.9, 25°C, mutant enzyme N62G Crassostrea sp.
32.4
-
ATP pH 7.9, 25°C, mutant enzyme K193G Crassostrea sp.
32.4
-
L-arginine pH 7.9, 25°C, mutant enzyme K193G Crassostrea sp.
40.8
-
ATP pH 7.9, 25°C, mutant enzyme K193R Crassostrea sp.
40.8
-
L-arginine pH 7.9, 25°C, mutant enzyme K193R Crassostrea sp.
41.9
-
ATP pH 7.9, 25°C, mutant enzyme N62D Crassostrea sp.
41.9
-
L-arginine pH 7.9, 25°C, mutant enzyme N62D Crassostrea sp.
42.1
-
ATP pH 7.9, 25°C, mutant enzyme N62D/K193R Crassostrea sp.
42.1
-
L-arginine pH 7.9, 25°C, mutant enzyme N62D/K193R Crassostrea sp.
47.5
-
ATP pH 7.9, 25°C, wild-type enzyme Crassostrea sp.
47.5
-
L-arginine pH 7.9, 25°C, wild-type enzyme Crassostrea sp.