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Literature summary for 2.7.3.3 extracted from

  • Pruett, P.S.; Azzi, A.; Clark, S.A.; Yousef, M.S.; Gattis, J.L.; Somasundaram, T.; Ellington, W.R.; Chapman, M.S.
    The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase (2003), J. Biol. Chem., 278, 26952-26957.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
E225A turnover number is 0.03% of the wild-type value Limulus polyphemus
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
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
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
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
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.08
-
ADP mutant enzyme R312G/E314V/H315D/E317A/E319V Limulus polyphemus
0.14
-
ADP mutant enzyme E314Q Limulus polyphemus
0.16
-
ADP mutant enzyme E225Q Limulus polyphemus
0.16
-
ADP mutant enzyme E225Q/E314Q Limulus polyphemus
0.16
-
ADP mutant enzyme E314S Limulus polyphemus
0.23
-
ADP wild-type enzyme Limulus polyphemus
0.26
-
ADP mutant enzyme E225D Limulus polyphemus
0.63
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine wild-type enzyme Limulus polyphemus
0.68
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E314D Limulus polyphemus
0.72
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E225D Limulus polyphemus
0.88
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E225Q Limulus polyphemus
0.92
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme R312G/E314V/H315D/E317A/E319V Limulus polyphemus
0.98
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E314S Limulus polyphemus
1.45
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E225Q/E314Q Limulus polyphemus

Organism

Organism UniProt Comment Textmining
Limulus polyphemus
-
atlantic horseshoe crab
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + Nomega-phospho-L-arginine
-
Limulus polyphemus ATP + L-arginine
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.27
-
ADP mutant enzyme E225Q/E314Q Limulus polyphemus
0.27
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E225Q/E314Q Limulus polyphemus
0.34
-
ADP mutant enzyme E225D Limulus polyphemus
0.34
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E225D Limulus polyphemus
0.37
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E314D Limulus polyphemus
0.37
-
ADP mutant enzyme E314Q Limulus polyphemus
0.45
-
ADP mutant enzyme E225Q Limulus polyphemus
0.45
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E225Q Limulus polyphemus
2.17
-
ADP mutant enzyme E314D Limulus polyphemus
2.17
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme E314S Limulus polyphemus
116
-
ADP mutant enzyme R312G/E314V/H315D/E317A/E319V Limulus polyphemus
116
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine mutant enzyme R312G/E314V/H315D/E317A/E319V Limulus polyphemus
140
-
ADP wild-type enzyme Limulus polyphemus
140
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine wild-type enzyme Limulus polyphemus