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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.11 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

EC Number Protein Variants Comment Organism
1.5.1.11 Q118A reduced activity Pecten maximus
1.5.1.11 Q118D reduced activity Pecten maximus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.11 0.0198
-
 NADH wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 0.104
-
 NADH mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 0.175
-
 NADH mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 0.5
-
 L-Arg wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 0.77
-
 pyruvate wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 5.8
-
 L-Arg mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 5.9
-
 2-oxobutyrate wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 27
-
 pyruvate mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 49.8
-
 2-oxovalerate wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 81
-
 L-Arg mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 162
-
 pyruvate mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.11 Pecten maximus Q9BHM6 great scallop
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.11 muscle
-
 Pecten maximus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.11 canavanine + pyruvate + NADH 24.74% activity with canavanine compared to L-Arg Pecten maximus ? + NAD+ + H2O
-
 ?
1.5.1.11 L-alanine + pyruvate + NADH 0.29% activity with L-alanine compared to L-Arg Pecten maximus ? + NAD+ + H2O
-
 ?
1.5.1.11 L-Arg + 2-oxobutyrate + NADH
-
 Pecten maximus ?
-
 ?
1.5.1.11 L-Arg + 2-oxovalerate + NADH
-
 Pecten maximus ?
-
 ?
1.5.1.11 L-Arg + NADH 100% activity with L-Arg Pecten maximus N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
 ?
1.5.1.11 L-cysteine + pyruvate + NADH 1.18% activity with L-cysteine compared to L-Arg Pecten maximus ? + NAD+ + H2O
-
 ?
1.5.1.11 norvaline + pyruvate + NADH 0.15% activity with norvaline compared to L-Arg Pecten maximus ? + NAD+ + H2O
-
 ?
1.5.1.11 ornithine + pyruvate + NADH 0.26% activity with ornithine compared to L-Arg Pecten maximus ? + NAD+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.11 N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase
-
 Pecten maximus
1.5.1.11 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
1.5.1.11 Octopine dehydrogenase
-
 Pecten maximus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.11 47
-
 NADH mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 73
-
 pyruvate mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 120
-
 L-Arg mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 122
-
 L-Arg mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 173
-
 NADH mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 272
-
 2-oxovalerate wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 283
-
 pyruvate mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 526
-
 2-oxobutanoate wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 640
-
 L-Arg wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 652
-
 NADH wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus
1.5.1.11 775
-
 pyruvate wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C Pecten maximus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.11 NADH
-
 Pecten maximus