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beta-alanine + pyruvate + NADH + H+
?
-
-
-
-
?
canavanine + pyruvate + NADH
? + NAD+ + H2O
24.74% activity with canavanine compared to L-Arg
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
Canavanine + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-canavanine + NADP+ + H2O
-
at 56% of the activity with L-Arg
-
-
?
glycine + pyruvate + NADH + H+
?
-
-
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
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-alanine + pyruvate + NADH + H+
?
-
-
-
-
?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
L-Arg + 2-oxobutanoate + NADPH
N2-(D-2-Carboxypropyl)-L-Arg + NADP+ + H2O
-
at 21% of the activity with pyruvate
-
-
?
L-Arg + 2-oxobutyrate + NADH
?
-
-
-
?
L-Arg + 2-oxovalerate + NADH
?
-
-
-
?
L-Arg + glyoxylate + NADPH
?
-
at 5% of the activity with pyruvate
-
-
?
L-Arg + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
100% activity with L-Arg
-
-
?
L-Arg + oxaloacetate + NADH
?
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-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
L-canavanine + pyruvate + NADPH + H+
N2-(D-1-carboxyethyl)-canavanine + NADP+ + H2O
-
-
-
-
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
-
at 27% of the activity with L-Arg
-
-
?
L-cysteine + pyruvate + NADH
? + NAD+ + H2O
1.18% activity with L-cysteine compared to L-Arg
-
-
?
L-Gln + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Gln + NADP+ + H2O
L-His + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-His + NADP+ + H2O
-
at 78% of the activity with L-Arg
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
L-Lys + pyruvate + NADPH
Lysopine + NADP+ + H2O
L-lysine + pyruvate + NADH + H+
?
-
-
-
-
?
L-Met + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Met + NADP+ + H2O
L-serine + pyruvate + NADPH
N2-(D-1-carboxyethyl)-L-Ser + NADP+ + H2O
-
at 25% of the activity with L-Arg
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
L-arginine + pyruvate + NADH + H+
norvaline + pyruvate + NADH
? + NAD+ + H2O
0.15% activity with norvaline compared to L-Arg
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
Orn + pyruvate + NADPH
N2-(D-1-Carboxyethyl)-L-Orn + NADP+ + H2O
-
at 30% of the activity with L-Arg
-
-
?
ornithine + pyruvate + NADH
? + NAD+ + H2O
0.26% activity with ornithine compared to L-Arg
-
-
?
additional information
?
-
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
L-canavanine, at 56% of the activity with L-Arg
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
57.6-92.6% of the activity with Arg, depending on enzyme variant
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
L-canavanine, at 48% of the activity with L-Arg
-
-
?
Canavanine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-canavanine + NAD+ + H2O
-
-
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
-
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
-
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
-
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
at 13% of the activity with L-Arg
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
-
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
58.6-70.8% of activity with Arg, depending on enzyme variant
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
-
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
at 22% of the activity with L-Arg
-
-
?
Homoarginine + pyruvate + NADH
N2-(D-1-Carboxyethyl)-homoarginine + NAD+ + H2O
-
-
-
-
?
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
-
-
-
-
?
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
-
at 41% of the activity with L-Arg
-
-
?
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
-
20.6-29.0% of activity with Arg
-
-
?
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
-
at 28% of the activity with pyruvate
-
-
?
L-Arg + 2-oxobutanoate + NADH
N2-(D-2-Carboxypropyl)-L-Arg + NAD+ + H2O
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
at 6.8-14.4% of activity with L-Arg
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
L-Arg + oxaloacetate + NADH
?
-
-
-
-
?
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
-
-
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
-
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
-
-
-
?
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
-
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
-
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
Priapulus sp.
-
-
-
?
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
-
no activity
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
r
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
no activity
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
at 1% of the activity with L-Arg
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
-
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
r
-
-
?
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
-
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
r
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
at 2% of the activity with L-Arg
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
no activity
-
-
?
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
-
-
-
?
L-Lys + pyruvate + NADPH
Lysopine + NADP+ + H2O
-
at 31% of the activity with L-Arg
-
-
?
L-Lys + pyruvate + NADPH
Lysopine + NADP+ + H2O
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
?
-
-
no activity with 2-hydroxybutanoate
-
-
?
additional information
?
-
-
-
-
-
?
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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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
3.9
L-canavanine
-
with pyruvate and NADPH as cosubstrates
5.4
L-Cys
-
with pyruvate and NADPH as cosubstrate
2.7
L-Gln
-
with pyruvate and NADPH as cosubstrates
23
L-His
-
with pyruvate and NADPH as cosubstrate
additional information
additional information
-
6.2
2-oxobutanoate
-
-
7.8
2-oxobutanoate
-
mantle enzyme
0.3
Arg
-
digestive gland enzyme
0.3
Arg
-
pyruvate, mantle muscle enzyme
0.9
Arg
-
D-octopine, mantle enzyme
1.1
Arg
-
Arg, foot muscle enzyme
1.2
Arg
-
pyruvate, gill enzyme
1.22
Arg
-
digestive gland enzyme
1.35
Arg
-
foot muscle enzyme
1.4 - 2.8
Arg
-
dependent on concentration of the cosubstrates NADH and pyruvate
2.5
Arg
-
L-Arg, with oxaloacetate as cosubstrate
2.5
Arg
-
L-Lys, brain enzyme
3.2
D-lysopine
-
-
3.2
D-lysopine
-
L-Arg, mantle muscle enzyme
0.1
D-octopine
-
brain enzyme
0.1
D-octopine
-
NAD+, foot muscle enzyme
1.5
D-octopine
-
pyruvate
2
D-octopine
-
L-Arg, with pyruvate as cosubstrate, brain enzyme
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
1.4
L-Arg
-
octopine, foot muscle enzyme
1.4
L-Arg
-
pyruvate, mantle enzyme
1.4
L-Arg
-
with pyruvate as cosubstrate
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
2.2
L-Arg
-
with 2-ketobutanoate as cosubstrate
3
L-Arg
-
with pyruvate as cosubstrate
3.5
L-Arg
mutant enzyme H212A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
3.7
L-Arg
-
with 2-ketobutanoate as cosubstrate
3.8
L-Arg
-
with 2-ketobutanoate as cosubstrate
4
L-Arg
-
with oxaloacetate as cosubstrate
5
L-Arg
-
with oxaloacetate as cosubstrate
5.1
L-Arg
-
with pyruvate and NADPH as cosubstrate
5.3
L-Arg
-
with 2-ketobutanoate as cosubstrate, brain enzyme
5.5
L-Arg
-
with pyruvate as cosubstrate, mantle enzyme
5.8
L-Arg
mutant enzyme Q118A, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
6.2
L-Arg
-
with 2-oxobutanoate as cosubstrate, mantle enzyme
8
L-Arg
-
2-ketobutanoate
8
L-Arg
-
with oxaloacetate as cosubstrate, mantle enzyme
9.8
L-Arg
mutant enzyme D329A, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
12
L-Arg
-
with oxaloacetate as cosubstrate, brain enzyme
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
22
L-citrulline
-
with pyruvate and NADPH as cosubstrates
22
L-citrulline
-
L-Met, with pyruvate and NADPH as cosubstrate
3.3
L-Lys
-
-
6.1
L-Lys
-
mantle enzyme
6.1
L-Lys
-
2-ketobutanoate, brain enzyme
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
0.7
L-Orn
-
with pyruvate and NADPH as cosubstrates
1.8
Lys
-
-
1.8
Lys
-
L-Arg, with pyruvate as cosubstrate
0.014
NAD+
-
-
0.022
NAD+
-
NADH, adductor muscle enzyme
0.022
NAD+
-
adductor muscle enzyme
0.023
NAD+
-
digestive gland enzyme
0.036
NAD+
-
foot muscle enzyme
0.01
NADH
-
foot muscle enzyme
0.011
NADH
-
digestive gland enzyme
0.019
NADH
-
digestive gland enzyme
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
0.021
NADH
-
foot muscle enzyme
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
0.03
NADH
-
mantle muscle enzyme
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
0.08
NADH
-
NAD+, digestive gland enzyme
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
0.09
octopine
-
brain enzyme
0.18
octopine
-
digestive gland enzyme
0.22
octopine
-
NADH, gill enzyme
0.27
octopine
-
foot muscle enzyme
0.85
octopine
-
gill enzyme
0.85
octopine
-
octopine, mantle muscle enzyme
1.3
octopine
-
adductor muscle enzyme
1.3
octopine
-
pyruvate, adductor muscle enzyme
1.7
octopine
-
digestive gland enzyme
1
oxaloacetate
-
-
1
oxaloacetate
-
pyruvate
1
oxaloacetate
-
L-Lys, with pyruvate and NADPH as cosubstrates
1.6
oxaloacetate
-
brain enzyme
1.6
oxaloacetate
-
pyruvate, foot muscle enzyme
2.6
oxaloacetate
-
D-lysopine, brain enzyme
2.6
oxaloacetate
-
mantle enzyme
0.25
pyruvate
-
brain enzyme
0.25
pyruvate
-
NAD+, mantle muscle enzyme
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
0.4
pyruvate
-
digestive gland enzyme
0.4
pyruvate
-
Arg, brain enzyme
0.5 - 1.5
pyruvate
-
depending on concentration of the cosubstrates NADH and Arg
0.6
pyruvate
-
brain enzyme
0.6
pyruvate
-
oxaloacetate
0.77
pyruvate
wild type enzyme, in 50 mM triethanolamine buffer, pH 7.0, at 25°C
0.8
pyruvate
-
pyruvate, foot muscle enzyme
0.8
pyruvate
wild type recombinant enzyme, in 50 mM triethanolamine hydrochloride buffer pH 7.0, at 25°C
1.56
pyruvate
-
digestive gland enzyme
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
3.1
pyruvate
-
D-octopine
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
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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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
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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
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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
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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
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1984
Pecten jacobaeus
brenda
Hammen, C.S.; Bullock, R.C.
Opine oxidoreductases in brachiopods, bryozoans, phoronids and molluscs
Biochem. Syst. Ecol.
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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
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brenda
Storey, K.B.; Dando, P.R.
Substrate specificities of octopine dehydrogenases from marine invertebrates
Comp. Biochem. Physiol. B
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521-528
1982
Arctica islandica, Calliactis parasitica, Cerastoderma edule, Glycymeris glycymeris, Mytilus edulis, Pecten maximus, Sepia officinalis
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Gde, G.
A comparative study of octopine dehydrogenase isoenzymes in gastropod, bivalve and cephalopod molluscs
Comp. Biochem. Physiol. B
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575-582
1980
Buccinum undatum, Acanthocardia tuberculata, Loligo vulgaris, Mytilus edulis, Pecten jacobaeus
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Monneuse-Doublet, M.O.; Olomucki, A.
A proposed kinetic mechanism for octopine dehydrogenase from Pecten maximus L.
Biochem. Soc. Trans.
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300-302
1981
Pecten maximus
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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
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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
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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
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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
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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
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brenda
Mueller, A.; Janssen, F.; Grieshaber, M.K.
Putative reaction mechanism of heterologously expressed octopine dehydrogenase from the great scallop, Pecten maximus (L)
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2007
Pecten maximus (Q9BHM6), Pecten maximus
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Smits, S.H.; Mueller, A.; Schmitt, L.; Grieshaber, M.K.
A structural basis for substrate selectivity and stereoselectivity in octopine dehydrogenase from Pecten maximus
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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
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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
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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
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2012
Pecten maximus
brenda
Lagana, G.; Barreca, D.; Giacobbe, S.; Bellocco, E.
Anaerobiosis and metabolic plasticity of Pinna nobilis biochemical and ecological features
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2014
Pinna nobilis
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brenda
Murphy, J.W.; Richmond, R.H.
Changes to coral health and metabolic activity under oxygen deprivation
PeerJ
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e1956
2016
Montipora capitata
brenda
Watanabe, S.; Sueda, R.; Fukumori, F.; Watanabe, Y.
Characterization of flavin-containing opine dehydrogenase from bacteria
PLoS ONE
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2015
Agrobacterium tumefaciens
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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
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427
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Octopus vulgaris (H2B4T3), Octopus vulgaris
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Paolucci, E.; Thuesen, E.
Effects of osmotic and thermal shock on the invasive aquatic mudsnail Potamopyrgus antipodarum mortality and physiology under stressful conditions
NeoBiota
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2020
Potamopyrgus antipodarum
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