Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
kinetic mechanism
-
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
-
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
-
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
-
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 )
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
canavanine + pyruvate + NADH
? + NAD+ + H2O
24.74% activity with canavanine compared to L-Arg
-
-
?
L-alanine + pyruvate + NADH
? + NAD+ + H2O
0.29% activity with L-alanine compared to L-Arg
-
-
?
L-Arg + 2-oxobutyrate + NADH
?
-
-
-
?
L-Arg + 2-oxovalerate + NADH
?
-
-
-
?
L-Arg + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
100% activity with L-Arg
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
-
-
?
L-cysteine + pyruvate + NADH
? + NAD+ + H2O
1.18% activity with L-cysteine compared to L-Arg
-
-
?
norvaline + pyruvate + NADH
? + NAD+ + H2O
0.15% activity with norvaline compared to L-Arg
-
-
?
ornithine + pyruvate + NADH
? + NAD+ + H2O
0.26% activity with ornithine compared to L-Arg
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
-
-
-
r
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
-
no activity
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
-
no activity
-
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
additional information
-
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
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
0.0389
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
0.77
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
1.5
D-octopine
-
-
1.5
D-octopine
-
pyruvate
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, Mytilus edulis, Pecten maximus, Phorcus lineatus
brenda
Schrimsher, J.L.; Taylor, K.B.
Octopine dehydrogenase from Pecten maximus: steady-state mechanism
Biochemistry
23
1348-1353
1984
Pecten maximus
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
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
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
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
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
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
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