Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli ER2566 cells | Pecten maximus |
Crystallization (Comment) | Organism |
---|---|
in complex with NADH, hanging drop vapour diffusion method, using 100 mM MES, pH 7.0, and Na-citrate ranging from 1.0 to 1.2 M in a 1:1 ratio, at 12°C | Pecten maximus |
Protein Variants | Comment | Organism |
---|---|---|
Q118A | reduced activity | Pecten maximus |
Q118D | reduced activity | Pecten maximus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0198 | - |
NADH | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
0.104 | - |
NADH | mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
0.175 | - |
NADH | mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
0.5 | - |
L-Arg | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
0.77 | - |
pyruvate | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
5.8 | - |
L-Arg | mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
5.9 | - |
2-oxobutyrate | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
27 | - |
pyruvate | mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
49.8 | - |
2-oxovalerate | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
81 | - |
L-Arg | mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
162 | - |
pyruvate | mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pecten maximus | Q9BHM6 | great scallop | - |
Purification (Comment) | Organism |
---|---|
ammonium sulfate precipitation, Ni2+-NTA column chromatography, and Sephadex G-100 gel filtration | Pecten maximus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Pecten maximus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
canavanine + pyruvate + NADH | 24.74% activity with canavanine compared to L-Arg | Pecten maximus | ? + NAD+ + H2O | - |
? | |
L-alanine + pyruvate + NADH | 0.29% activity with L-alanine compared to L-Arg | Pecten maximus | ? + NAD+ + H2O | - |
? | |
L-Arg + 2-oxobutyrate + NADH | - |
Pecten maximus | ? | - |
? | |
L-Arg + 2-oxovalerate + NADH | - |
Pecten maximus | ? | - |
? | |
L-Arg + NADH | 100% activity with L-Arg | Pecten maximus | N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O | - |
? | |
L-cysteine + pyruvate + NADH | 1.18% activity with L-cysteine compared to L-Arg | Pecten maximus | ? + NAD+ + H2O | - |
? | |
norvaline + pyruvate + NADH | 0.15% activity with norvaline compared to L-Arg | Pecten maximus | ? + NAD+ + H2O | - |
? | |
ornithine + pyruvate + NADH | 0.26% activity with ornithine compared to L-Arg | Pecten maximus | ? + NAD+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase | - |
Pecten maximus |
OcDH | catalyzes the reductive condensation of L-arginine and pyruvate to octopine during escape swimming in great scallop, oxidizes glycolytically born NADH to NAD+, thus sustaining anaerobic ATP provision during short periods of strenuous muscular activity | Pecten maximus |
Octopine dehydrogenase | - |
Pecten maximus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
47 | - |
NADH | mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
73 | - |
pyruvate | mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
120 | - |
L-Arg | mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
122 | - |
L-Arg | mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
173 | - |
NADH | mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
272 | - |
2-oxovalerate | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
283 | - |
pyruvate | mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
526 | - |
2-oxobutanoate | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
640 | - |
L-Arg | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
652 | - |
NADH | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus | |
775 | - |
pyruvate | wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C | Pecten maximus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Pecten maximus |