Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.5.1.11 - D-octopine dehydrogenase and Organism(s) Pecten maximus and UniProt Accession Q9BHM6

for references in articles please use BRENDA:EC1.5.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
In the reverse direction, acts also on L-ornithine, L-lysine and L-histidine.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pecten maximus
UNIPROT: Q9BHM6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Pecten maximus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
octopine synthase, octopine dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase
-
N2-(D-1-carboxyethyl)-L-arginine:NAD+-oxidoreductase
-
Octopine dehydrogenase
-
D-Octopine synthase
-
-
-
-
Dehydrogenase, octopine
-
-
-
-
N2-(D-1-carboxyethyl)-L-arginine:NAD+-oxidoreductase
-
-
Octopine dehydrogenase
-
-
-
-
Octopine synthase
-
-
-
-
Octopine:NAD oxidoreductase
-
-
-
-
ODH
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+
show the reaction diagram
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+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-27-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
canavanine + pyruvate + NADH
? + NAD+ + H2O
show the reaction diagram
24.74% activity with canavanine compared to L-Arg
-
-
?
L-alanine + pyruvate + NADH
? + NAD+ + H2O
show the reaction diagram
0.29% activity with L-alanine compared to L-Arg
-
-
?
L-Arg + 2-oxobutyrate + NADH
?
show the reaction diagram
-
-
-
?
L-Arg + 2-oxovalerate + NADH
?
show the reaction diagram
-
-
-
?
L-Arg + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
show the reaction diagram
100% activity with L-Arg
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
show the reaction diagram
-
-
-
?
L-cysteine + pyruvate + NADH
? + NAD+ + H2O
show the reaction diagram
1.18% activity with L-cysteine compared to L-Arg
-
-
?
norvaline + pyruvate + NADH
? + NAD+ + H2O
show the reaction diagram
0.15% activity with norvaline compared to L-Arg
-
-
?
ornithine + pyruvate + NADH
? + NAD+ + H2O
show the reaction diagram
0.26% activity with ornithine compared to L-Arg
-
-
?
L-Arg + pyruvate + NADH
N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
show the reaction diagram
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
L-Lys + pyruvate + NADH
Lysopine + NAD+ + H2O
show the reaction diagram
-
no activity
-
-
?
Orn + pyruvate + NADH
N2-(D-1-Carboxyethyl)-L-Orn + NAD+ + H2O
show the reaction diagram
-
no activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
p-chloromercuribenzoate
-
1,10-phenanthroline
-
-
1-Ethyl-3(3-dimethylaminopropyl)carbodiimide hydrochloride
-
-
2,2'-dipyridyl
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-Guanidinopentanoate
-
-
diethyldicarbonate
-
reversal of the inhibition by hydroxylamine
diethyldithiocarbamate
-
-
Guanidinobutane
-
-
L-Arg
NAD+
-
noncompetitive with respect to pyruvate, uncompetitive with respect to L-Arg
p-chloromercuriphenyl sulfonic acid
-
-
propanoate
-
-
pyruvate
-
substrate inhibition
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
0.5 - 159
L-Arg
0.0198 - 0.175
NADH
0.77 - 162
pyruvate
1.5
D-octopine
0.026
NADH
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 640
L-Arg
7.3 - 652
NADH
13 - 775
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
464
His-tagged recombinant enzyme, after purification, at 18°C
63
crude extract, at 18°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
enzyme form A and B, octopine formation
9.7
-
enzyme form A and B, octopine oxidation
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.35
theoretical value
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OCDH_PECMA
399
0
43320
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
His-tagged recombinant enzyme, SDS-PAGE
43300
calculated from sequence of cDNA
35800
-
1 * 35800, equilibrium sedimentation with guanidine hydrochloride
38000
-
equilibrium sedimentation
43000
-
1 * 43000, enzyme form A and B, SDS-PAGE
46000
-
1 * 46000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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 and agmatine, to 2.8 A resolution
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C148A
the mutant shows reduced activity
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
Q118A
reduced activity
Q118D
reduced activity
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme form B is more sensitive to alkaline treatments than enzyme form A
13314
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
-
half-denaturation time: 40 min, enzyme forms A and B
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
irreversible inactivation by photooxidation in presence of rose bengal
-
13308
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Ni2+-NTA column chromatography, and Sephadex G-100 gel filtration
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%
Ni-NTA affinity chromatography and Sephadex G-100 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli ER2566 cells
expressed in Escherichia coli with a C-terminal penta His-tag
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
expressed in Escherichia coli strain ER2566
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
His-tag-induced crystallization of OcDH is found to be dependent on the length of the His tag
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, Mytilus edulis, Pecten maximus, Phorcus lineatus
Manually annotated by BRENDA team
Schrimsher, J.L.; Taylor, K.B.
Octopine dehydrogenase from Pecten maximus: steady-state mechanism
Biochemistry
23
1348-1353
1984
Pecten maximus
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Olomucki, A.
Structure and function of octopine dehydrogenase of Pecten maximus (great scallop)
Biochem. Soc. Trans.
9
278-279
1981
Pecten maximus
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Huc, C.; Olomucki, A.; Thome-Beau, F.
Modification of the essential carboxyl group in octopine dehydrogenase
FEBS Lett.
60
414-418
1975
Pecten maximus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Doublet, M.O.; Olomucki, A.
Investigations on the kinetic mechanism of octopine dehydrogenase
Eur. J. Biochem.
59
175-183
1975
Pecten maximus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team