BRENDA - Enzyme Database

The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase

Pruett, P.S.; Azzi, A.; Clark, S.A.; Yousef, M.S.; Gattis, J.L.; Somasundaram, T.; Ellington, W.R.; Chapman, M.S.; J. Biol. Chem. 278, 26952-26957 (2003)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
2.7.3.3
crystal structures of mutant enzymes E314D at 1.9 A and E225Q at 2.8 A resolution shows that the precise alignment of substrates is subtly distorted
Limulus polyphemus
Engineering
EC Number
Amino acid exchange
Commentary
Organism
2.7.3.3
E225A
turnover number is 0.03% of the wild-type value
Limulus polyphemus
2.7.3.3
E225D
KM-value for ADP is 2.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.14fold higher than wild-type value, turnover number is 0.24% of the wild-type value
Limulus polyphemus
2.7.3.3
E225Q
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.4fold higher than wild-type value, turnover number is 0.3% of the wild-type value
Limulus polyphemus
2.7.3.3
E225Q/E314Q
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 2.3fold higher than wild-type value, turnover number is 0.2% of the wild-type value
Limulus polyphemus
2.7.3.3
E314D
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.56fold higher than wild-type value, turnover number is 1.7% of the wild-type value
Limulus polyphemus
2.7.3.3
E314Q
KM-value for ADP is 1.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.1fold higher than wild-type value, turnover number is 0.3% of the wild-type value
Limulus polyphemus
2.7.3.3
R312G/E314V/H315D/E317A/E319V
KM-value for ADP is 1.5fold lower than the wild-type value, KM-value for N-phospho-L-arginine is 1.5fold higher than wild-type value, turnover number is 83% of the wild-type value
Limulus polyphemus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7.3.3
0.08
-
ADP
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
0.14
-
ADP
mutant enzyme E314Q
Limulus polyphemus
2.7.3.3
0.16
-
ADP
mutant enzyme E225Q; mutant enzyme E225Q/E314Q; mutant enzyme E314S
Limulus polyphemus
2.7.3.3
0.23
-
ADP
wild-type enzyme
Limulus polyphemus
2.7.3.3
0.26
-
ADP
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.63
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
wild-type enzyme
Limulus polyphemus
2.7.3.3
0.68
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314D
Limulus polyphemus
2.7.3.3
0.72
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.88
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q
Limulus polyphemus
2.7.3.3
0.92
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
0.98
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314S
Limulus polyphemus
2.7.3.3
1.45
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q/E314Q
Limulus polyphemus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.7.3.3
Limulus polyphemus
-
atlantic horseshoe crab
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.3.3
ADP + Nomega-phospho-L-arginine
-
662144
Limulus polyphemus
ATP + L-arginine
-
-
-
?
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.7.3.3
0.27
-
ADP
mutant enzyme E225Q/E314Q
Limulus polyphemus
2.7.3.3
0.27
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q/E314Q
Limulus polyphemus
2.7.3.3
0.34
-
ADP
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.34
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.37
-
ADP
mutant enzyme E314Q
Limulus polyphemus
2.7.3.3
0.37
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314D
Limulus polyphemus
2.7.3.3
0.45
-
ADP
mutant enzyme E225Q
Limulus polyphemus
2.7.3.3
0.45
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q
Limulus polyphemus
2.7.3.3
2.17
-
ADP
mutant enzyme E314D
Limulus polyphemus
2.7.3.3
2.17
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314S
Limulus polyphemus
2.7.3.3
116
-
ADP
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
116
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
140
-
ADP
wild-type enzyme
Limulus polyphemus
2.7.3.3
140
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
wild-type enzyme
Limulus polyphemus
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.7.3.3
crystal structures of mutant enzymes E314D at 1.9 A and E225Q at 2.8 A resolution shows that the precise alignment of substrates is subtly distorted
Limulus polyphemus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.7.3.3
E225A
turnover number is 0.03% of the wild-type value
Limulus polyphemus
2.7.3.3
E225D
KM-value for ADP is 2.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.14fold higher than wild-type value, turnover number is 0.24% of the wild-type value
Limulus polyphemus
2.7.3.3
E225Q
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.4fold higher than wild-type value, turnover number is 0.3% of the wild-type value
Limulus polyphemus
2.7.3.3
E225Q/E314Q
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 2.3fold higher than wild-type value, turnover number is 0.2% of the wild-type value
Limulus polyphemus
2.7.3.3
E314D
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.56fold higher than wild-type value, turnover number is 1.7% of the wild-type value
Limulus polyphemus
2.7.3.3
E314Q
KM-value for ADP is 1.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.1fold higher than wild-type value, turnover number is 0.3% of the wild-type value
Limulus polyphemus
2.7.3.3
R312G/E314V/H315D/E317A/E319V
KM-value for ADP is 1.5fold lower than the wild-type value, KM-value for N-phospho-L-arginine is 1.5fold higher than wild-type value, turnover number is 83% of the wild-type value
Limulus polyphemus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7.3.3
0.08
-
ADP
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
0.14
-
ADP
mutant enzyme E314Q
Limulus polyphemus
2.7.3.3
0.16
-
ADP
mutant enzyme E225Q; mutant enzyme E225Q/E314Q; mutant enzyme E314S
Limulus polyphemus
2.7.3.3
0.23
-
ADP
wild-type enzyme
Limulus polyphemus
2.7.3.3
0.26
-
ADP
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.63
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
wild-type enzyme
Limulus polyphemus
2.7.3.3
0.68
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314D
Limulus polyphemus
2.7.3.3
0.72
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.88
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q
Limulus polyphemus
2.7.3.3
0.92
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
0.98
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314S
Limulus polyphemus
2.7.3.3
1.45
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q/E314Q
Limulus polyphemus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.3.3
ADP + Nomega-phospho-L-arginine
-
662144
Limulus polyphemus
ATP + L-arginine
-
-
-
?
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.7.3.3
0.27
-
ADP
mutant enzyme E225Q/E314Q
Limulus polyphemus
2.7.3.3
0.27
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q/E314Q
Limulus polyphemus
2.7.3.3
0.34
-
ADP
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.34
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225D
Limulus polyphemus
2.7.3.3
0.37
-
ADP
mutant enzyme E314Q
Limulus polyphemus
2.7.3.3
0.37
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314D
Limulus polyphemus
2.7.3.3
0.45
-
ADP
mutant enzyme E225Q
Limulus polyphemus
2.7.3.3
0.45
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E225Q
Limulus polyphemus
2.7.3.3
2.17
-
ADP
mutant enzyme E314D
Limulus polyphemus
2.7.3.3
2.17
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme E314S
Limulus polyphemus
2.7.3.3
116
-
ADP
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
116
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
mutant enzyme R312G/E314V/H315D/E317A/E319V
Limulus polyphemus
2.7.3.3
140
-
ADP
wild-type enzyme
Limulus polyphemus
2.7.3.3
140
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
wild-type enzyme
Limulus polyphemus