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Literature summary for 1.5.1.11 extracted from

  • Smits, S.H.; Mueller, A.; Schmitt, L.; Grieshaber, M.K.
    A structural basis for substrate selectivity and stereoselectivity in octopine dehydrogenase from Pecten maximus (2008), J. Mol. Biol., 381, 200-211.
    View publication on PubMed
Search for more literature for 1.5.1.11

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli ER2566 cells Pecten maximus

Crystallization (Commentary)

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

Protein Variants Comment Organism
Q118A reduced activity Pecten maximus
Q118D reduced activity Pecten maximus

KM Value [mM]

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

Organism UniProt Comment Textmining
Pecten maximus Q9BHM6 great scallop
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Ni2+-NTA column chromatography, and Sephadex G-100 gel filtration Pecten maximus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Pecten maximus
-

Substrates and Products (Substrate)

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

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 [1/s]

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

Cofactor Comment Organism Structure
NADH
-
 Pecten maximus