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Information on EC 1.5.1.11 - D-octopine dehydrogenase
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EC Tree
1.5.1.11 D-octopine dehydrogenaseIUBMB Comments
In the reverse direction, acts also on L-ornithine, L-lysine and L-histidine.
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
octopine synthase, octopine dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-Octopine synthase
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Dehydrogenase, octopine
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N2-(D-1-carboxyethyl)-L-arginine:NAD+-oxidoreductase
OcDH
Octopine dehydrogenase
Octopine synthase
Octopine:NAD oxidoreductase
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ODH
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
Octopine dehydrogenase
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Octopine synthase
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ODH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
kinetic mechanism
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
NADH binds to the enzyme first followed by L-Arg and pyruvate, which bind randomly
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
bi-ter sequential mechanism where NAD+ binds first to the enzyme followed by D-octopine, and the products are released in the order L-Arg, pyruvate and NADH
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
partially random mechanism in which NADH is the obligatory first substrate, and Arg and pyruvate bind randomly to the enzyme-NADH complex. Ordered sequential addition of NAD+ and octopine in octopine oxidation
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
in the direction of octopine oxidation NAD binds to the enzyme before octopine in a rapid equilibrium fashion. The products L-Arg and pyruvate are released in a random fashion
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
partially ordered mechanism. NADPH binds first followed by the random order, rapid-equilibrium-binding of Arg and pyruvate. Orn probably binds before pyruvate
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
the enzyme removes the pro-S hydrogen atom of the dihydronicotinamide ring with transfer of label to the solvent and to the product octopine (N-2-(1-carboxyethyl)-L-arginine )
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
the enzyme removes the pro-S hydrogen atom of the dihydronicotinamide ring with transfer of label to the solvent and to the product octopine (N-2-(1-carboxyethyl)-L-arginine )
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
substrates bind in an ordered sequential manner. First NADH binds to OcDH followed by L-arginine. The binding of the guanidinium headgroup of L-arginine induces a conformational change, resulting in the formation of the pyruvate binding site. The reduction of pyruvate can only occur in the presence of L-arginine, which than forms octopine and prevents lactate formation
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase (L-arginine-forming)
In the reverse direction, acts also on L-ornithine, L-lysine and L-histidine.
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CAS REGISTRY NUMBER
COMMENTARY
37256-27-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
canavanine + pyruvate + NADH
? + NAD+ + H2O
24.74% activity with canavanine compared to L-Arg
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-
?
Canavanine + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-canavanine + NADP+ + H2O
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at 56% of the activity with L-Arg
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-
?
Homoarginine + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-homoarginine + NADP+ + H2O
-
at 62% of the activity with L-Arg
-
-
?
L-alanine + pyruvate + NADH
? + NAD+ + H2O
0.29% activity with L-alanine compared to L-Arg
-
-
?
L-Arg + 2-oxobutanoate + NADPH
N2-(D-2-Carboxypropyl)-L-Arg + NADP+ + H2O
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at 21% of the activity with pyruvate
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-
?
L-Arg + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
100% activity with L-Arg
-
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?
L-canavanine + pyruvate + NADPH + H+
N2-(D-1-carboxyethyl)-canavanine + NADP+ + H2O
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-
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r
L-Citrulline + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-citrulline + NADP+ + H2O
-
-
-
-
?
L-Cys + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Cys + NADP+ + H2O
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at 27% of the activity with L-Arg
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?
L-cysteine + pyruvate + NADH
? + NAD+ + H2O
1.18% activity with L-cysteine compared to L-Arg
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?
L-His + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-His + NADP+ + H2O
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at 78% of the activity with L-Arg
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?
L-serine + pyruvate + NADPH
N2-(D-1-carboxyethyl)-L-Ser + NADP+ + H2O
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at 25% of the activity with L-Arg
-
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?
norvaline + pyruvate + NADH
? + NAD+ + H2O
0.15% activity with norvaline compared to L-Arg
-
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?
Orn + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Orn + NADP+ + H2O
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at 30% of the activity with L-Arg
-
-
?
ornithine + pyruvate + NADH
? + NAD+ + H2O
0.26% activity with ornithine compared to L-Arg
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
L-canavanine, at 56% of the activity with L-Arg
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
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-
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
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57.6-92.6% of the activity with Arg, depending on enzyme variant
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
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-
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
L-canavanine, at 48% of the activity with L-Arg
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?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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-
-
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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-
-
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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at 13% of the activity with L-Arg
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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58.6-70.8% of activity with Arg, depending on enzyme variant
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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-
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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at 22% of the activity with L-Arg
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?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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-
-
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?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
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-
-
-
?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
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-
-
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?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
-
-
-
-
?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
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at 41% of the activity with L-Arg
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?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
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-
-
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?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
-
20.6-29.0% of activity with Arg
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?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
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-
-
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?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
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at 28% of the activity with pyruvate
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?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
-
-
-
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?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
r
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
r
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
2 enzyme forms. One catalyzes the reverse reaction with NAD+, the second with NADP+
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
r
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
Chlamys opercularis
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i.e. octopine
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
r
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-Arg + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Arg + NADP+ + H2O
-
-
-
-
?
L-Arg + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Arg + NADP+ + H2O
-
2 enzyme forms. One catalyzes the reverse reaction with NAD+, the second with NADP+
-
-
?
L-Arg + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Arg + NADP+ + H2O
-
-
-
-
?
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
?
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
the reduction reaction is highly preferred
-
-
?
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
?
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
highest affinity for L-arginine
-
-
?
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
r
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
?
L-Gln + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Gln + NADP+ + H2O
-
at 18% of the activity with L-Arg
-
-
?
L-Gln + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Gln + NADP+ + H2O
-
-
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
at 1% of the activity with L-Arg
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
87.2-92.6% of activity with Arg, depending on enzyme variant
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
at 2% of the activity with L-Arg
-
-
?
L-Lys + pyruvate + NADPH
Lysopine + NADP+ + H2O
-
at 31% of the activity with L-Arg
-
-
?
L-Met + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Met + NADP+ + H2O
-
at 67% of the activity with L-Arg
-
-
?
L-Met + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Met + NADP+ + H2O
-
-
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
L-arginine + pyruvate + NADH + H+
-
-
-
r
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
L-arginine + pyruvate + NADH + H+
-
-
-
-
r
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
no activity
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
-
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
at 2% of the activity with L-Arg
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
-
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
at 4% of the activity with L-Arg
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
no activity
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
activity with brain enzyme, no activity with mantle enzyme
-
-
?
additional information
?
-
-
octopine [N2-(1-D-carboxyethyl)-L-arginine] is synthesized by a NAD(P)H-dependent soluble dehydrogenase that catalyzes the reductive condensation of pyruvate with L-arginine. Although the reaction may be reversible in vitro, the frequent use of the term synthase rather than dehydrogenase has emphasized the importance of biosynthesis, but not degradation, and distinguishes it from the mollusk octopine dehydrogenase
-
-
?
additional information
?
-
-
the enzyme OCS utilizes not only L-arginine, but also other amino acids, to yield the corresponding members of the octopine family. Analysis of specificity of electron acceptors using 4-iodonitrotetrazolium violet (INT) or nitroblue tetrazolium (NBT) together with phenazine methosulfate (PMS) (electron-transfer intermediate), ferricyanide, horse heart cytochrome c, and NAD(P)+
-
-
?
additional information
?
-
-
the enzyme may synthesize lysopine, octopinic acid, and the corresponding Nalpha-derivatives of glutamine
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
octopine is produced in the mantle via the reaction of the muscle isoenzyme and is subsequently flushed out into the blood and transported to other tissues such as the optic lobe for re-oxidation via the optic lobe isoenzyme
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
the enzyme shows no activity when taurine or beta-alanine is used as substrate
-
-
?
additional information
?
-
-
the major role of the brain enzyme may be the oxidation of octopine
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
mantle muscle enzyme appears geared for the rapid synthesis of octopine under conditions of muscular work
-
-
?
additional information
?
-
-
major physiological role in glycolytic energy poduction during burst swimming
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
?
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
?
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
r
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
L-arginine + pyruvate + NADH + H+
-
-
-
r
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
L-arginine + pyruvate + NADH + H+
-
-
-
-
r
additional information
?
-
-
octopine [N2-(1-D-carboxyethyl)-L-arginine] is synthesized by a NAD(P)H-dependent soluble dehydrogenase that catalyzes the reductive condensation of pyruvate with L-arginine. Although the reaction may be reversible in vitro, the frequent use of the term synthase rather than dehydrogenase has emphasized the importance of biosynthesis, but not degradation, and distinguishes it from the mollusk octopine dehydrogenase
-
-
?
additional information
?
-
-
the enzyme may synthesize lysopine, octopinic acid, and the corresponding Nalpha-derivatives of glutamine
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
octopine is produced in the mantle via the reaction of the muscle isoenzyme and is subsequently flushed out into the blood and transported to other tissues such as the optic lobe for re-oxidation via the optic lobe isoenzyme
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
the major role of the brain enzyme may be the oxidation of octopine
-
-
?
additional information
?
-
-
the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
-
-
?
additional information
?
-
-
mantle muscle enzyme appears geared for the rapid synthesis of octopine under conditions of muscular work
-
-
?
additional information
?
-
-
major physiological role in glycolytic energy poduction during burst swimming
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
noncompetitive with respect to pyruvate, uncompetitive with respect to L-Arg
NEM
-
competitive with respect to NAD+; non-competitive with respect to octopine
octopine
-
substrate inhibition above 2 mM, 50% product inhibition at 1.2 mM
p-chloromercuriphenyl sulfonic acid
-
reversed by dithiothreitol, NADH prevents inactivation
pyruvate
-
significantly more sensitive to substrate inhibition than the foot muscle enzyme
pyruvate
-
brain enzyme shows strong substrate inhibition, mantle muscle enzyme only slight inhibition
additional information
ODH is not inhibited by 5 or 10 mM iodacetamide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme activity in adductor muscle increases following the marine-brackish gradient
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
Altered imino diacid synthesis and transcription in crown gall tumors with transposon Tn5 insertions in the 3' end of the octopine synthase gene.
Neoplasms
Clonal analysis of heterogeneous crown gall tumor tissues induced by wild-type and shooter mutant strains ofAgrobacterium tumefaciens-expression of T-DNA genes.
Neoplasms
Nucleotide sequence and transcript map of the Agrobacterium tumefaciens Ti plasmid-encoded octopine synthase gene.
Neoplasms
Octopine dehydrogenase from crown gall tumor and from Pecten maximus. Oxidation of (4R)- and (4S)-[4-3H]NADH.
Neoplasms
Silent T-DNA genes in plant lines transformed by Agrobacterium tumefaciens are activated by grafting and by 5-azacytidine treatment.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.9
2-oxobutyrate
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
49.8
2-oxovalerate
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
1.4 - 2.8
Arg
-
dependent on concentration of the cosubstrates NADH and pyruvate
0.5
L-Arg
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
0.5
L-Arg
wild type recombinant enzyme, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
1.6
L-Arg
mutant enzyme C148A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
1.7
L-Arg
mutant enzyme C148S, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
3.5
L-Arg
mutant enzyme H212A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
5.8
L-Arg
mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
9.8
L-Arg
mutant enzyme D329A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
81
L-Arg
mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
159
L-Arg
mutant enzyme R324A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
1.4
L-lysine
-
GST-tagged enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
1.8
L-lysine
-
crude extract enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
1.8
L-lysine
-
recombinant enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
0.0198
NADH
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
0.0198
NADH
wild type recombinant enzyme, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
0.0214
NADH
mutant enzyme D329A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
0.024
NADH
-
GST-tagged enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
0.026
NADH
-
crude extract enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
0.028
NADH
-
recombinant enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
0.0389
NADH
mutant enzyme C148S, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
0.04
NADH
mutant enzyme C148A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
0.0649
NADH
mutant enzyme H212A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
0.0904
NADH
mutant enzyme R324A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
0.104
NADH
mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
0.175
NADH
mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
0.25
pyruvate
-
crude extract enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
0.35
pyruvate
-
GST-tagged enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
0.35
pyruvate
-
recombinant enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
0.5 - 1.5
pyruvate
-
depending on concentration of the cosubstrates NADH and Arg
0.77
pyruvate
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
0.8
pyruvate
wild type recombinant enzyme, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
2.5
pyruvate
mutant enzyme C148A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
2.6
pyruvate
mutant enzyme C148S, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
27
pyruvate
mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
33
pyruvate
mutant enzyme D329A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
59
pyruvate
mutant enzyme H212A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
92
pyruvate
mutant enzyme R324A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
162
pyruvate
mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
additional information
additional information
-
dependence of the Km-values for Arg and pyruvate on the concentration of the other substrates
-
additional information
additional information
-
temperature-dependence of Km-values
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
526
2-oxobutanoate
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
272
2-oxovalerate
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
2 - 8
L-Arg
mutant enzyme D329A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
5.1
L-Arg
mutant enzyme H212A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
43
L-Arg
mutant enzyme R324A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
120
L-Arg
mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
122
L-Arg
mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
444
L-Arg
mutant enzyme C148A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
446
L-Arg
mutant enzyme C148S, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
640
L-Arg
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
640
L-Arg
wild type recombinant enzyme, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
7.3
NADH
mutant enzyme H212A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
9.3
NADH
mutant enzyme D329A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
25
NADH
mutant enzyme R324A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
47
NADH
mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
173
NADH
mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
410
NADH
mutant enzyme C148S, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
422
NADH
mutant enzyme C148A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
652
NADH
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
652
NADH
wild type recombinant enzyme, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
13
pyruvate
mutant enzyme H212A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
15.4
pyruvate
mutant enzyme D329A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
22.5
pyruvate
mutant enzyme R324A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
73
pyruvate
mutant enzyme Q118D, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
283
pyruvate
mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
499
pyruvate
mutant enzyme C148A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
511
pyruvate
mutant enzyme C148S, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
775
pyruvate
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
775
pyruvate
wild type recombinant enzyme, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.45
-
crude extract enzyme, using beta-alanine as substrate, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
1.5
-
crude extract enzyme, using L-alanine as substrate, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
1.7
-
crude extract enzyme, using glycine as substrate, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
10.1
-
recombinant enzyme, using glycine as substrate, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
10.4
-
crude extract enzyme, using L-arginine as substrate, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
324.8
-
recombinant enzyme, using L-arginine as substrate, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
33.3
-
recombinant enzyme, using L-alanine as substrate, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication
additional information
additional information
in terms of activity, the three constructs (tagless OcDH, His5-tagged OcDH and His6-tagged OcDH) are indistinguishable
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 allozymic forms are distributed in a highly population-specific manner, enzyme variants: ss, ff, and sf
-
-
brenda
crown-gall tumor-tissue induced by Agrobacterium tumefaciens
-
-
brenda
collected in the straits of Messina area (central Mediterranean) between May and June of 2011, from two nearby marine and brackish-water sites, two populations
-
-
brenda
collected at Capitol Lake, Olympia, Washington, USA, during winter and spring seasons with environmental temperature 5°C and 10°C, respectively
-
-
brenda
2 isoenzymes: a polymorphic anodal form and a hepatopancreas-specific cathodally migrating form
-
-
brenda
crown-gall tumor-tissue induced by Agrobacterium tumefaciens. 2 enzyme form one dependent on NAD+, the second on NADP+
-
-
brenda
the structural gene for octopine synthase is located in a central portion of the T-DNA Agrobacterium tumefaciens Ti plasmid
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ODH is the major opine dehydrogenase in the adductor muscle
brenda
additional information
-
enzyme tissue distribution and expression analysis
brenda
-
the structural gene for octopine synthase is located in a central portion of the T-DNA of Agrobacterium tumefaciens Ti plasmid
brenda
-
hepatopancreas-specific cathodally migrating form
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
-
bivalves have evolved diverse and highly specialised strategies for surviving in hypoxic episodes including pathways that are efficient both in terms of ATP production, and in minimising H+ and toxic end product accumulation. Under these circumstances, glycogen is metabolized to pyruvate and the cytosolic NADH/NAD+ redox ratio is balanced by the reduction of pyruvate to lactate. Alternatively, NAD+ can be recycled more efficiently by coupling an amino acid to pyruvate, with formation of opines such as alanopine, tauropine, octopine, and strombine. Specimens utilizing the octopine rather than the alanopine pathway will increase energy flow rapidly, developing a major ability to counteract environmental variations. The high ratio between malate dehydrogenase/lactate dehydrogenase is due to the ability of Pinna nobilis to turn on anaerobic metabolism as a consequence of environmental or anthropogenic stresses. Anaerobic pathways are not all equivalent in terms of energy production based upon maximum rates for ATP output (lactate > octopine > alanopine = strombine). The ODH pathway is probably able to realize a higher rate of energy production than either the SDH or ADH pathways
metabolism
in mollusks, anaerobic conditions, in addition to the lactate dehydrogenase (LDH) activity, have been shown to produce energy by the arginine phosphate/arginine kinase system in which octopine dehydrogenase (ODH) is involved. ODH maintains a lower cytosolic redox ratio (NADH/NAD+) than LDH during anoxia, where the glycolytic pathway is prevalent. Activity of key enzymes of intermediary metabolism in Octopus vulgaris palarvae at hatching and after 12 and 28 days of feeding with control diet (Artemia enriched with phytoplankton) or LC60 diet (Artemia enriched with marine lecithin), overview
physiological function
analysis of the metabolic organization of octopus paralarvae throughout an ontogenic period of 12 days post-hatching, as well as assessment of the effect of diet enrichment with live prey containing abundant marine phospholipids. Throughout the ontogenic period studied, an increase in anaerobic metabolism takes place largely due to an increased dependence of paralarvae on exogenous food. This activity is supported by octopine dehydrogenase activity, with a less significant contribution of lactate dehydrogenase activity. Regarding aerobic metabolism, the use of amino acids is maintained for the duration of the experiment, and a significant increase in the rate of oxidation of fatty acids from 6 days after-hatching is observed. Capacity for de novo synthesis of glucose from amino acids and glycerol is also observed. Feeding larvae with phospholipid-enriched Artemia improves animal viability and welfare, significantly increasing the rate of survival and growth of paralarvae
physiological function
-
standard metabolic rate and enzymatic activities (malate dehydrogenase, lactate dehydrogexadnase, alanopine dehydrogenase) in snails after a 10-day acclimation period at high salinity. Opine dehydrogenase is measured for anaerobic respiration. Significantly higher mortalities are observed at higher salinities, the strongest effects occur on snails collected at the end of winter, and exposed to 30 psu and 20°C (100% mortality in 3 days). When snails are collected during the spring, 100% mortality is observed after 40 days at 30 psu and 20°C. Standard metabolic rates are significantly lower when snails are exposed to salinities of 25 and 30 psu, even after 10 days of acclimation. Analysis of effects of high salinity, osmotic and thermal shock, determination of enzyme activity and mortality rates of the New Zealand mudsnail under different conditions, overview
additional information
-
chronic nighttime hypoxia does not affect the ODH enzyme activity in corals
additional information
-
comparisons of opine dehydrogenases activities (octopine dehydrogenase, alanopine dehydrogenase, strombine dehydrogenase, and tauropine dehydrogenase) in the adductor muscle, overview. The ODH activity in adductor muscle increases following the marine-brackish gradient, while the one of ADH, SDH and TDH decreases following the same gradient
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DHLO_AGRT4
358
0
38797
Swiss-Prot
-
DHLO_AGRT9
358
0
38797
Swiss-Prot
-
OCDH_MIZYE
400
0
43417
Swiss-Prot
other Location (Reliability: 5)
OCDH_PECMA
399
0
43320
Swiss-Prot
other Location (Reliability: 5)
A0A484RDS0_9ZZZZ
171
0
17870
TrEMBL
other Location (Reliability: 2)
A0A484SGP1_9ZZZZ
62
0
6734
TrEMBL
other Location (Reliability: 2)
A0A484QND8_9ZZZZ
320
0
35230
TrEMBL
other Location (Reliability: 3)
A0A484REB1_9ZZZZ
190
0
21234
TrEMBL
other Location (Reliability: 4)
Q9GNX6_DOROP
408
0
45583
TrEMBL
other Location (Reliability: 3)
Q6W0Z7_SINFN
Sinorhizobium fredii (strain NBRC 101917 / NGR234)
375
1
40241
TrEMBL
-
A0A484T7T1_9ZZZZ
320
0
35229
TrEMBL
other Location (Reliability: 3)
A0A286MYQ0_ARGIR
399
0
43352
TrEMBL
other Location (Reliability: 5)
Q9BHU3_LOLVU
409
0
45792
TrEMBL
other Location (Reliability: 2)
B3RAH1_CUPTR
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1)
459
0
48323
TrEMBL
-
M1FK93_MYTGA
401
0
44275
TrEMBL
other Location (Reliability: 3)
A0A160TTP6_9ZZZZ
369
0
38796
TrEMBL
Secretory Pathway (Reliability: 3)
M1FBU6_MYTTR
392
0
43444
TrEMBL
Mitochondrion (Reliability: 5)
A0A484P9Z0_9ZZZZ
150
0
15703
TrEMBL
other Location (Reliability: 2)
A0A484Y037_9ZZZZ
371
0
40325
TrEMBL
other Location (Reliability: 2)
A0A822VCA5_RHIRD
358
0
38797
TrEMBL
-
M1FHV2_MYTED
401
0
44340
TrEMBL
other Location (Reliability: 5)
B3RAG9_CUPTR
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1)
378
1
40288
TrEMBL
-
Q9BHK4_SEPOF
409
0
45857
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
39000
43000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tag-induced crystallization of OcDH is found to be dependent on the length of the His tag. OcDH-tagless and His6-tagged OcDH do not yield crystals. The purified His5-tagged OcDH yields small crystals. Together with the coenzyme NADH the crystals obtained are single and diffract to 2.1 A resolution. Two distinct domains can be found in OcDH: an NADH-dependent glycerol-3-phosphate dehydrogenase-like domain (domain I) and an octopine dehydrogenase specific domain (domain II; Interpro database). Each domain comprises approximately half of the protein, with domain I containing the classic Rossman fold of dinucleotide-binding proteins
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C148S
the mutant shows reduced activity and is only slightly inhibited by 5,5'-dithiobis(2-nitrobenzoic acid) and p-chloromercuribenzoate
D329A
the mutation results in strong increases in Km and decreases in kcat values for pyruvate and L-arginine, but has little effect on the Km and kcat values for NADH
H212A
the mutation results in strong increases in Km and decreases in kcat values for pyruvate and L-arginine, but has little effect on the Km and kcat values for NADH
R324A
the mutation results in strong increases in Km and decreases in kcat values for pyruvate and L-arginine, but has little effect on the Km and kcat values for NADH
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
4°C, stable. Loses most of its activity after 24 h at lower or higher pH-values
13323
additional information
-
enzyme form B is more sensitive to alkaline treatments than enzyme form A
13314
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, buffer containing glycerol, NADPH and 2-mercaptoethanol, stable for many weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Ni2+-NTA column chromatography, and Sephadex G-100 gel filtration
crown-gall tumor-tissue induced by Agrobacterium tumefaciens
His5-tagged OcDH and His6-tagged OcDH are purified by Ni-NTA chromatography, yielding almost 20 mg homogenous enzyme per litre of cell culture (purity greater than 98%). The purification of OcDH-tagless requires several chromatographic steps and yields 3-5 mg per litre of cell culture, with a purity of more than 98%
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, dialysis, and gel filtration
-
the biospecific chromatographic affinity purification is not applicable to the purification of the enzyme from Monodonta lineate
-
the biospecific chromatographic affinity purification is not applicable to the purification of the enzyme from Mytilus edulis
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ocs, DNA and amino acid sequence determination, analysis, and comparisons, genetic structure, phylogenetic analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
OcDH is cloned and expressed tagless (OcDH-tagless), as a His5-tagged OcDH (OcDH-His5) and as a His6-tagged OcDH variant (OcDHLEHis6) in Escherichia coli. The His tag is always placed at the C-terminus
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
kinetic of renaturation. A fast process involves the formation of a structured intermediate
-
refolding kinetics. Upon reactivation after short denaturation of less than 8 s, about 25% of the activity is recovered in a fast initial phase of 20 s. The slow phase of reactivation, which predominates after long-term denaturation, is determined by a single-first-order reaction
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
His-tag-induced crystallization of OcDH is found to be dependent on the length of the His tag
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mulcahy, P.; Griffin, T.; O'Carra, P.
Biospecific affinity chromatographic purification of octopine dehydrogenase from molluscs
Protein Expr. Purif.
9
109-114
1997
Chlamys opercularis, Loligo vulgaris, Phorcus lineatus, Mytilus edulis, Pecten maximus
brenda
Sheikh, S.; Katiyar, S.S.
Involvement of different cysteines in the inactivation of octopine dehydrogenase by p-chloromercuriphenyl sulfonic acid and o-phthalaldehyde
Biochem. Mol. Biol. Int.
29
719-727
1993
Pecten jacobaeus
brenda
Carvajal, N.; Vega, E.; Erices, A.; Bustos, D.; Torres, C.
Lactate dehydrogenase, alanopine dehydrogenase and octopine dehydrogenase from heart of Concholepas concholepas (gastropoda: muricidae)
Comp. Biochem. Physiol. B
108
543-550
1994
Concholepas concholepas
-
brenda
Hammen, C.S.; Fileding, C.
Opine oxidoreductases in marine worms of five phyla
Comp. Biochem. Physiol. B
106
989-992
1993
Cerebratulus sp., Lineus sp., no activity in Amphitrite sp., no activity in Chaetopterus variopedatus, no activity in Clymenella torquata, no activity in Glycera sp., no activity in Hydroides sp., no activity in Lepidonotus sp., no activity in Nereis sp., no activity in Phascolopsis sp., no activity in Phascolosoma sp., no activity in Themiste sp., no activity in Urechis sp., Priapulus sp.
-
brenda
Sato, M.; Takeuchi, M.; Kanno, N.; Nagahisa, E.; Sato, Y.
Distribution of opine dehydrogenases and lactate dehydrogenase activities in marine animals
Comp. Biochem. Physiol. B
106
955-960
1993
Anthopleura nigrescens, Buccinum isaotakii, Azumapecten farreri nipponensis, Fusitriton oregonensis, Haliotis discus hannai, Littorina brevicula, Heterololigo bleekeri, Meretrix lusoria, Mytilus edulis, Neptunea arthritica, Amphioctopus membranaceus, Octopus vulgaris, Mizuhopecten yessoensis, Perinereis nuntia, Reishia clavigera, Ruditapes philippinarum, Anadara broughtonii, Todarodes pacificus, Scelidotoma gigas, Pseudocardium sachalinense
-
brenda
Santulli, A.; Wilkins, N.P.; D'Amelio, V.
Two tissue-specific loci for octopine dehydrogenase in Tapes decussatus (bivalvia, veneridae)
Comp. Biochem. Physiol. B
102
409-411
1992
Ruditapes decussatus
-
brenda
Coughlan, M.; O'Carra, P.
The lysopine and octopine dehydrogenase activities of Mytilus edulis are catalyzed by a single enzyme
Biochem. Soc. Trans.
24
128S
1996
Mytilus edulis
brenda
Gde, G.; Carlsson, K.H.
Purification and characterisation of octopine dehydrogenase from marine nemertean Cerebratulus lactus (anopla: heteronemerta): comparison with scallop octopine dehydrogenase
Mar. Biol.
79
39-45
1984
Cerebratulus lacteus, Pecten jacobaeus
-
brenda
Carvajal, N.; Kessi, E.
Kinetic mechanism of octopine dehydrogenase from the muscle of the sea mollusc, Concholepas concholepas
Biochim. Biophys. Acta
953
14-19
1988
Concholepas concholepas
-
brenda
Teschner, W.; Rudolph, R.; Garel, J.R.
Intermediates on the folding pathway of octopine dehydrogenase from Pecten jacobaeus
Biochemistry
26
2791-2796
1987
Pecten jacobaeus
-
brenda
Schrimsher, J.L.; Taylor, K.B.
Octopine dehydrogenase from Pecten maximus: steady-state mechanism
Biochemistry
23
1348-1353
1984
Pecten maximus
brenda
Zettlmeissl, G.; Teschner, W.; Rudolph, R.; Jaenicke, R.; Gde, G.
Isolation, physicochemical properties, and folding of octopine dehydrogenase from Pecten jacobeus
Eur. J. Biochem.
143
401-407
1984
Pecten jacobaeus
brenda
Hammen, C.S.; Bullock, R.C.
Opine oxidoreductases in brachiopods, bryozoans, phoronids and molluscs
Biochem. Syst. Ecol.
19
263-269
1991
Lunarca ovalis, Antalis pilsbryi, Haliotis rufescens, no activity in Bugula neritina, no activity in Chaetopleura apiculata, no activity in Crepidula fornicata, no activity in Diodora cayenensis, no activity in Glottidia pyramidata, no activity in Laqueus californianus, no activity in Littorina littorea, no activity in Lyonsia hyalina, no activity in Membranipora tenuis, no activity in Mopalia muscosa, no activity in Mya arenaria, no activity in Phoronis architecta, no activity in Phoronis vancouverensis, no activity in Schizoporella floridana, no activity in Tectura testudinalis, no activity in Tegula funebralis, no activity in Terebratalia transversa, no activity in Turbo castanea, no activity in Urosalpinx cinerea, Nucella lapillus, Nucula proxima, Solemya velum, Spisula solidissima
-
brenda
Storey, K.B.; Dando, P.R.
Substrate specificities of octopine dehydrogenases from marine invertebrates
Comp. Biochem. Physiol. B
73
521-528
1982
Arctica islandica, Calliactis parasitica, Cerastoderma edule, Glycymeris glycymeris, Mytilus edulis, Pecten maximus, Sepia officinalis
-
brenda
Gde, G.
A comparative study of octopine dehydrogenase isoenzymes in gastropod, bivalve and cephalopod molluscs
Comp. Biochem. Physiol. B
67
575-582
1980
Buccinum undatum, Acanthocardia tuberculata, Loligo vulgaris, Mytilus edulis, Pecten jacobaeus
-
brenda
Monneuse-Doublet, M.O.; Olomucki, A.
A proposed kinetic mechanism for octopine dehydrogenase from Pecten maximus L.
Biochem. Soc. Trans.
9
300-302
1981
Pecten maximus
-
brenda
Olomucki, A.
Structure and function of octopine dehydrogenase of Pecten maximus (great scallop)
Biochem. Soc. Trans.
9
278-279
1981
Pecten maximus
brenda
Barrett, J.; Krting, W.
Octopine dehydrogenase in gastropods from different environments
Experientia
37
958-959
1981
Buccinum undatum, Steromphala umbilicaris, Phorcus lineatus, Nucella lapillus, Patella aspera, Patella vulgata
-
brenda
Gde, G.; Head, E.J.H.
A rapid method for the purification of octopine dehydrogenase for determination of cell metabolites
Experientia
35
304-305
1979
Pecten maximus
-
brenda
Huc, C.; Olomucki, A.; Le-Thi-Lan; Pho, D.B.; van Thoai, N.
Essential histidyl residues of octopine dehydrogenase
Eur. J. Biochem.
21
161-169
1971
Pecten maximus
brenda
Thome-Beau, F.; Olomucki, A.
Presence of a single essential histidyl residue in octopine dehydrogenase as shown by photooxidation
Eur. J. Biochem.
39
557-562
1973
Pecten maximus
brenda
Huc, C.; Olomucki, A.; Thome-Beau, F.
Modification of the essential carboxyl group in octopine dehydrogenase
FEBS Lett.
60
414-418
1975
Pecten maximus
brenda
Luisi, P.L.; Baici, A.; Olomucki, A.; Doublet, M.O.
Temperature-determined enzymatic functions in octopine dehydrogenase
Eur. J. Biochem.
50
511-516
1975
Pecten maximus
brenda
Doublet, M.O.; Olomucki, A.
Investigations on the kinetic mechanism of octopine dehydrogenase
Eur. J. Biochem.
59
175-183
1975
Pecten maximus
brenda
Storey, K.B.; Storey, J.M.
Kinetic characterization of tissue-specific isozymes of octopine dehydrogenase from mantle muscle and brain of Sepia officinalis
Eur. J. Biochem.
93
545-552
1979
Sepia officinalis
brenda
Van Thoai, N.; Huc, C.; Pho, D.B.; Olomucki, A.
Octopine deshydrogenase. Purification et proprietes catalytiques
Biochim. Biophys. Acta
191
46-57
1969
Pecten maximus
brenda
Monneuse-Doublet, M.O.; Lefebure, F.; Olomucki, A.
Isolation and characterization of two molecular forms of octopine dehydrogenase from Pecten maximus L.
Eur. J. Biochem.
108
261-269
1980
Pecten maximus
brenda
Seikh, S.; Katiyar, S.S.
Chemical medification of octopine dehydrogenase by thiol-specific reagents: evidence for the presence of an essential cysteine at the catalytic site
Biochim. Biophys. Acta
1202
251-257
1993
Pecten maximus
brenda
Olomucki, A.; Huc, C.; Lefebure, F.; van Thoai, N.
Octopine dehydrogenase. Evidence for a single-chain structure
Eur. J. Biochem.
28
261-268
1972
Pecten maximus
brenda
Walsh, P.J.
Purification and characterization of two allozymic forms of octopine dehydrogenase from california populations of Metridium senile
J. Comp. Physiol.
143
213-222
1981
Metridium senile
-
brenda
Gde, G.
Octopine dehydrogenase in the cockle Cardium edule
Biochem. Soc. Trans.
4
433-436
1976
Cerastoderma edule
brenda
Hack, E.; Kemp, J.D.
Purification and characterization of the crown gall-specific enzyme, octopine synthase
Plant Physiol.
65
949-955
1980
Helianthus annuus
brenda
Birnberg, P.R.; Lippincott, B.B.; Lippincott, J.A.
Two octopine dehydrogenases in crown-gall tumor tissue
Phytochemistry
16
647-650
1977
Catharanthus roseus, Nicotiana tabacum, Phaseolus vulgaris
-
brenda
Schrimsher, J.L.; Taylor, K.B.
Octopine dehydrogenase from crown gall tumor and from Pecten maximus. Oxidation of (4R)- and (4S)-[4-3H]NADH
J. Biol. Chem.
257
8953-8956
1982
Nicotiana tabacum, Pecten maximus
brenda
Murai, N.; Kemp, J.D.
Octopine synthase mRNA isolated from sunflower crown gall callus is homologous to the Ti plasmid of Agrobacterium tumefaciens
Proc. Natl. Acad. Sci. USA
79
86-90
1982
Helianthus annuus
brenda
Birnberg, P.R.; Rao, S.S.; Lippincott, J.A.
Octopine dehydrogenase of a Vinca rosea crown gall-tumor
Phytochemistry
22
1345-1355
1983
Catharanthus roseus
-
brenda
Mueller, A.; Janssen, F.; Grieshaber, M.K.
Putative reaction mechanism of heterologously expressed octopine dehydrogenase from the great scallop, Pecten maximus (L)
FEBS J.
274
6329-6339
2007
Pecten maximus (Q9BHM6), Pecten maximus
brenda
Smits, S.H.; Mueller, A.; Schmitt, L.; Grieshaber, M.K.
A structural basis for substrate selectivity and stereoselectivity in octopine dehydrogenase from Pecten maximus
J. Mol. Biol.
381
200-211
2008
Pecten maximus (Q9BHM6), Pecten maximus
brenda
Smits, S.H.; Mueller, A.; Grieshaber, M.K.; Schmitt, L.
Coenzyme- and His-tag-induced crystallization of octopine dehydrogenase
Acta Crystallogr. Sect. F
64
836-839
2008
Pecten maximus (Q9BHM6)
brenda
Smits, S.H.; Meyer, T.; Mueller, A.; van Os, N.; Stoldt, M.; Willbold, D.; Schmitt, L.; Grieshaber, M.K.
Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography
PLoS ONE
5
e12312
2010
Pecten maximus (Q9BHM6), Pecten maximus
brenda
Vazquez-Dorado, S.; Sanjuan, A.; Comesana, A.S.; de Carlos, A.
Identification of octopine dehydrogenase from Mytilus galloprovincialis
Comp. Biochem. Physiol. B
160
94-103
2011
Mytilus galloprovincialis
brenda
van Os, N.; Smits, S.H.; Schmitt, L.; Grieshaber, M.K.
Control of D-octopine formation in scallop adductor muscle as revealed through thermodynamic studies of octopine dehydrogenase
J. Exp. Biol.
215
1515-1522
2012
Pecten maximus
brenda
Lagana, G.; Barreca, D.; Giacobbe, S.; Bellocco, E.
Anaerobiosis and metabolic plasticity of Pinna nobilis biochemical and ecological features
Biochem. Syst. Ecol.
56
138-143
2014
Pinna nobilis
-
brenda
Murphy, J.W.; Richmond, R.H.
Changes to coral health and metabolic activity under oxygen deprivation
PeerJ
4
e1956
2016
Montipora capitata
brenda
Watanabe, S.; Sueda, R.; Fukumori, F.; Watanabe, Y.
Characterization of flavin-containing opine dehydrogenase from bacteria
PLoS ONE
10
e0138434
2015
Agrobacterium tumefaciens
brenda
Morales, A.E.; Cardenete, G.; Hidalgo, M.C.; Garrido, D.; Martin, M.V.; Almansa, E.
Time course of metabolic capacities in paralarvae of the common octopus, Octopus vulgaris, in the first stages of life. Searching biomarkers of nutritional imbalance
Front. Physiol.
8
427
2017
Octopus vulgaris (H2B4T3), Octopus vulgaris
brenda
Paolucci, E.; Thuesen, E.
Effects of osmotic and thermal shock on the invasive aquatic mudsnail Potamopyrgus antipodarum mortality and physiology under stressful conditions
NeoBiota
54
1-22
2020
Potamopyrgus antipodarum
-
brenda
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