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Information on EC 1.5.99.B4 - flavin-containing opine dehydrogenase
for references in articles please use BRENDA:EC1.5.99.B4preliminary BRENDA-supplied EC number
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EC Tree
1.5.99.B4 flavin-containing opine dehydrogenaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
flavin-containing opine dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BjOpnDH
bll7190
flavin-containing opine dehydrogenase
Nox/Oox-like protein
OdhA
odhB
OpnDH
SoxB
flavin-containing opine dehydrogenase
Q89E96; Q89E94; Q89E97
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O = L-arginine + pyruvate + FADH2
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
N2-(D-1-carboxyethyl)-L-arginine:FAD+ oxidoreductase (L-arginine-forming)
-
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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
N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O
L-arginine + 2-oxoglutarate + FADH2
Q88EK6; Q88EK5
i.e. nopaline
-
-
?
N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O
L-arginine + 2-oxoglutarate + FADH2
Q88EK6; Q88EK5
i.e. nopaline
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q89E96; Q89E94; Q89E97
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
-
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q89E96; Q89E94; Q89E97
i.e. D-octopine, the electrons obtained through the oxidation of octopine are received by FMN via FAD in the beta-subunit, and finally transferred to an electron acceptor via the [2Fe-2S] cluster bound to [Fe-S]site 2, FAD in the alpha-subunit, and/or [4Fe-4S] cluster bound to [Fe-S]site 1. 2,6-Dichloroindophenol is used as final electron acceptor
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q89E96; Q89E94; Q89E97
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q89E96; Q89E94; Q89E97
i.e. D-octopine, the electrons obtained through the oxidation of octopine are received by FMN via FAD in the beta-subunit, and finally transferred to an electron acceptor via the [2Fe-2S] cluster bound to [Fe-S]site 2, FAD in the alpha-subunit, and/or [4Fe-4S] cluster bound to [Fe-S]site 1. 2,6-Dichloroindophenol is used as final electron acceptor
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q89E96; Q89E94; Q89E97
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q88EK6; Q88EK5
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q88EK6; Q88EK5
i.e. D-octopine
-
-
?
additional information
?
-
Q89E96; Q89E94; Q89E97
analysis of specificity of electron acceptors using 2,6-dichloroindophenol, 4-iodonitrotetrazolium violet (INT) or nitroblue tetrazolium (NBT) together with phenazine methosulfate (PMS) (electron-transfer intermediate), ferricyanide, horse heart cytochrome c, and NAD(P)+. Enzyme BjOdhAB2C and BjOdhAB1C both function as octopine-specific OpnDH, poor activity with nopaline
-
-
?
additional information
?
-
-
analysis of specificity of electron acceptors using 2,6-dichloroindophenol, 4-iodonitrotetrazolium violet (INT) or nitroblue tetrazolium (NBT) together with phenazine methosulfate (PMS) (electron-transfer intermediate), ferricyanide, horse heart cytochrome c, and NAD(P)+. Enzyme BjOdhAB2C and BjOdhAB1C both function as octopine-specific OpnDH, poor activity with nopaline
-
-
?
additional information
?
-
Q89E96; Q89E94; Q89E97
analysis of specificity of electron acceptors using 2,6-dichloroindophenol, 4-iodonitrotetrazolium violet (INT) or nitroblue tetrazolium (NBT) together with phenazine methosulfate (PMS) (electron-transfer intermediate), ferricyanide, horse heart cytochrome c, and NAD(P)+. Enzyme BjOdhAB2C and BjOdhAB1C both function as octopine-specific OpnDH, poor activity with nopaline
-
-
?
additional information
?
-
Q88EK6; Q88EK5
analysis of specificity of electron acceptors using 2,6-dichloroindophenol, 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
?
-
-
analysis of specificity of electron acceptors using 2,6-dichloroindophenol, 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
?
-
Q88EK6; Q88EK5
analysis of specificity of electron acceptors using 2,6-dichloroindophenol, 4-iodonitrotetrazolium violet (INT) or nitroblue tetrazolium (NBT) together with phenazine methosulfate (PMS) (electron-transfer intermediate), ferricyanide, horse heart cytochrome c, and NAD(P)+
-
-
?
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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
N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O
L-arginine + 2-oxoglutarate + FADH2
Q88EK6; Q88EK5
i.e. nopaline
-
-
?
N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O
L-arginine + 2-oxoglutarate + FADH2
Q88EK6; Q88EK5
i.e. nopaline
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q89E96; Q89E94; Q89E97
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
-
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q89E96; Q89E94; Q89E97
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q88EK6; Q88EK5
i.e. D-octopine
-
-
?
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
Q88EK6; Q88EK5
i.e. D-octopine
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
Q89E96; Q89E94; Q89E97
1 FMN between the alpha- and beta-subunits
FMN
Q88EK6; Q88EK5
required for activity, the gamma-subunit has no effect on the binding of FMN
[2Fe-2S]-center
Q89E96; Q89E94; Q89E97
importance of the [2Fe-2S] cluster for catalytic activity, the [Fe-S]site 2 of BjOpnDH binds to the [2Fe-2S] clusters. The gamma-subunit by itself is necessary for the adequate binding of [2Fe-2S]. The [2Fe-2S] cluster is important for structural folding and enzyme catalysis
[2Fe-2S]-center
Q88EK6; Q88EK5
[4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the gamma- and alpha-subunits, respectively. Cysteine residues C380, C382, C415, and C420 coordinate with the [Fe-S] clusters. The [2Fe-2S] cluster is important for structural folding and enzyme catalysis
[2Fe-2S]-center
Q89E96; Q89E94; Q89E97
[4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the gamma- and alpha-subunits, respectively. The [2Fe-2S] cluster is important for structural folding and enzyme catalysis
[4Fe-4S]-center
Q89E96; Q89E94; Q89E97
the [Fe-S]site 1 of BjOpnDH binds to the [4Fe-4S] clusters
[4Fe-4S]-center
Q89E96; Q89E94; Q89E97
[4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the gamma- and alpha-subunits, respectively
[4Fe-4S]-center
Q88EK6; Q88EK5
[4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the gamma- and alpha-subunits, respectively. Cysteine residues C56, C61, C64, and C77 coordinate with the [Fe-S] clusters
additional information
Q89E96; Q89E94; Q89E97
cysteine residues in the [Fe-S] binding site natively form disulfide bond(s)
-
additional information
-
cysteine residues in the [Fe-S] binding site natively form disulfide bond(s)
-
additional information
Q89E96; Q89E94; Q89E97
electron acceptor specificities of BjOdhAB2C and BjOdhAB1C, overview
-
additional information
-
electron acceptor specificities of BjOdhAB2C and BjOdhAB1C, overview
-
additional information
Q89E96; Q89E94; Q89E97
[4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the gamma- and alpha-subunits, respectively. Site [Fe-S]site 1 consists of Cys56-X4-Cys61-X2-Cys64-X11~12-Cys77 near the C-terminus, while site [Fe-S]site 2 consists of Cys380-X-Cys382-X15~20-Cys415-X4-Cys420
-
additional information
-
[4Fe-4S] and [2Fe-2S] clusters bind to two different types of [Fe-S] binding sites in the gamma- and alpha-subunits, respectively. Site [Fe-S]site 1 consists of Cys56-X4-Cys61-X2-Cys64-X11~12-Cys77 near the C-terminus, while site [Fe-S]site 2 consists of Cys380-X-Cys382-X15~20-Cys415-X4-Cys420
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
Q89E96; Q89E94; Q89E97
electron paramagnetic resonance analysis
Fe2+
Q89E96; Q89E94; Q89E97
in iron-sufur clusters, [4Fe-4S] and [2Fe-2S], overview
Fe2+
Q88EK6; Q88EK5
in iron-sufur clusters, [4Fe-4S] and [2Fe-2S], overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.077
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with nitroblue tetrazolium (NBT) together with phenazine methosulfate, recombinant His6-tagged enzyme
0.127
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 4-iodonitrotetrazolium violet (INT) together with phenazine methosulfate, recombinant His6-tagged enzyme
0.379
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with cytochrome c, recombinant His6-tagged enzyme
0.379
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with ferricyanide, recombinant His6-tagged enzyme
0.476
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
0.0078
N2-(D-1-carboxyethyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
1.29
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with nitroblue tetrazolium (NBT) together with phenazine methosulfate, recombinant His6-tagged enzyme
3.54
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with cytochrome c, recombinant His6-tagged enzyme
4.81
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
6.52
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with ferricyanide, recombinant His6-tagged enzyme
12.9
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with 4-iodonitrotetrazolium violet (INT) together with phenazine methosulfate, recombinant His6-tagged enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.33
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with ferricyanide, recombinant His6-tagged enzyme
23.17
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with nitroblue tetrazolium (NBT) together with phenazine methosulfate, recombinant His6-tagged enzyme
91.5
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 4-iodonitrotetrazolium violet (INT) together with phenazine methosulfate, recombinant His6-tagged enzyme
298.67
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with cytochrome c, recombinant His6-tagged enzyme
315
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
0.093
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with nitroblue tetrazolium (NBT) together with phenazine methosulfate, recombinant His6-tagged enzyme
0.098
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
0.173
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with cytochrome c, recombinant His6-tagged enzyme
0.21
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with 4-iodonitrotetrazolium violet (INT) together with phenazine methosulfate, recombinant His6-tagged enzyme
0.252
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with ferricyanide, recombinant His6-tagged enzyme
2.3
N2-(D-1-carboxyethyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
45.73
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with ferricyanide, recombinant His6-tagged enzyme
300.9
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with nitroblue tetrazolium (NBT) together with phenazine methosulfate, recombinant His6-tagged enzyme
661.77
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
720.47
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 4-iodonitrotetrazolium violet (INT) together with phenazine methosulfate, recombinant His6-tagged enzyme
788.05
N2-(D-1,3-dicarboxypropyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with cytochrome c, recombinant His6-tagged enzyme
0.0163
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with 4-iodonitrotetrazolium violet (INT) together with phenazine methosulfate, recombinant His6-tagged enzyme
0.0203
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
0.0387
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with ferricyanide, recombinant His6-tagged enzyme
0.0489
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with cytochrome c, recombinant His6-tagged enzyme
0.0721
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
pH 9.0, 30°C, with nitroblue tetrazolium (NBT) together with phenazine methosulfate, recombinant His6-tagged enzyme
1.97
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
mutant alphaC382Sbetagamma, pH 9.0, 30°C
3.73
N2-(D-1-carboxyethyl)-L-arginine
Q89E96; Q89E94; Q89E97
recombinant wild-type enzyme, pH 9.0, 30°C
294.87
N2-(D-1-carboxyethyl)-L-arginine
Q88EK6; Q88EK5
pH 9.0, 30°C, with 2,6-dichloroindophenol, recombinant His6-tagged enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.257
Q89E96; Q89E94; Q89E97
purified recombinant enzyme mutant alphaC382Sbetagamma, pH 9.0, 30°C
0.504
Q89E96; Q89E94; Q89E97
purified recombinant wild-type enzyme, pH 9.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Q89E96; Q89E94; Q89E97
pH optimum of BjOdhAB2C and BjOdhAB1C, overview
additional information
-
pH optimum of BjOdhAB2C and BjOdhAB1C, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunits BjOdhA (bll7191 or ooxA), BjOdhB1 (bll7193), and BjOdhB2 (bll7190 or soxB)
Q89E96; Q89E94; Q89E97
UniProt
brenda
subunits BjOdhA (bll7191 or ooxA), BjOdhB1 (bll7193), and BjOdhB2 (bll7190 or soxB)
Q89E96; Q89E94; Q89E97
UniProt
brenda
subunits alpha and beta; isolated from soil
Q88EK6; Q88EK5
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
Q89E96; Q89E94; Q89E97
opine dehydrogenase (OpnDH) belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s). This enzyme is phylogenetically related to hydrogen cyanide synthase, EC 1.4.99.5, from bacteria, D-hydroxyproline dehydrogenase from bacteria, and L-proline dehydrogenase, EC 1.5.5.2, from archaea. In contrast to Agrobacterium species, PpOpnDH and BjOpnDH genes are located on the chromosome. Flavin-containing OpnDH (the beta-subunit) belongs to the D-amino acid oxidase (DAD) superfamily (pfam01266). An ancestor of this protein family may inherently possess FMN between the alpha- and beta-subunits, and OpnDHtype-1 and OpnDHtype-2 may have acquired the same substrate specificity independently, convergent evolution of OpnDH
evolution
Q88EK6; Q88EK5
opine dehydrogenase (OpnDH) belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s). This enzyme is phylogenetically related to hydrogen cyanide synthase, EC 1.4.99.5, from bacteria, D-hydroxyproline dehydrogenase from bacteria, and L-proline dehydrogenase, EC 1.5.5.2, from archaea. In contrast to Agrobacterium species, PpOpnDH and BjOpnDH, genes are located on the chromosome. Pseudomonas putida strain KT2440 very recently acquired this ability by horizontal gene transfer (not plasmid transfer). Convergent evolution of OpnDH
evolution
Q89E96; Q89E94; Q89E97
two types of ProDHs, alphabetagammadelta, and alpha4beta4 complexes, have been identified from hyperthermophilic archaea, and their alpha-subunits commonly correspond to the gamma-subunit of OpnDH. OpnDH belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s)
evolution
-
two types of ProDHs, alphabetagammadelta, and alpha4beta4 complexes, have been identified from hyperthermophilic archaea, and their alpha-subunits commonly correspond to the gamma-subunit of OpnDH. OpnDH belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s)
-
evolution
-
opine dehydrogenase (OpnDH) belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s). This enzyme is phylogenetically related to hydrogen cyanide synthase, EC 1.4.99.5, from bacteria, D-hydroxyproline dehydrogenase from bacteria, and L-proline dehydrogenase, EC 1.5.5.2, from archaea. In contrast to Agrobacterium species, PpOpnDH and BjOpnDH genes are located on the chromosome. Flavin-containing OpnDH (the beta-subunit) belongs to the D-amino acid oxidase (DAD) superfamily (pfam01266). An ancestor of this protein family may inherently possess FMN between the alpha- and beta-subunits, and OpnDHtype-1 and OpnDHtype-2 may have acquired the same substrate specificity independently, convergent evolution of OpnDH
-
evolution
-
opine dehydrogenase (OpnDH) belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s). This enzyme is phylogenetically related to hydrogen cyanide synthase, EC 1.4.99.5, from bacteria, D-hydroxyproline dehydrogenase from bacteria, and L-proline dehydrogenase, EC 1.5.5.2, from archaea. In contrast to Agrobacterium species, PpOpnDH and BjOpnDH, genes are located on the chromosome. Pseudomonas putida strain KT2440 very recently acquired this ability by horizontal gene transfer (not plasmid transfer). Convergent evolution of OpnDH
-
malfunction
Q89E96; Q89E94; Q89E97
loss of the [4Fe-4S] cluster and/or gamma-subunit by itself has no effect on the binding of FAD and FMN. A marked decrease in the activity of the alphabeta mutant appears to be due to the (partial) degradation of the [2Fe-2S] cluster
malfunction
-
loss of the [4Fe-4S] cluster and/or gamma-subunit by itself has no effect on the binding of FAD and FMN. A marked decrease in the activity of the alphabeta mutant appears to be due to the (partial) degradation of the [2Fe-2S] cluster
-
physiological function
Q89E96; Q89E94; Q89E97
a potential physiological role in opine catabolism may be limited to (active) BjOpnDH2 because the OdhA and OdhC proteins preferentially associate with OdhB2 over OdhB1
physiological function
-
a potential physiological role in opine catabolism may be limited to (active) BjOpnDH2 because the OdhA and OdhC proteins preferentially associate with OdhB2 over OdhB1
-
additional information
Q89E96; Q89E94; Q89E97
a poor phylogenetic relationship exists between OdhB1 and OdhB2 in spite of them both functioning as octopine dehydrogenases, which provided clear evidence for the acquisition of novel functions by subunit exchange
additional information
-
a poor phylogenetic relationship exists between OdhB1 and OdhB2 in spite of them both functioning as octopine dehydrogenases, which provided clear evidence for the acquisition of novel functions by subunit exchange
additional information
Q88EK6; Q88EK5
the beta-subunit functions as a catalytic subunit by itself
additional information
-
the beta-subunit functions as a catalytic subunit by itself
additional information
Q89E96; Q89E94; Q89E97
the gamma-subunit by itself is necessary for the adequate binding of FMN and [2Fe-2S], particularly the latter. The removal of the [4Fe-4S] cluster may result in the easier formation of a disulfide bond between the remaining three cysteine residues in [Fe-S]site 1 of the alphabetagammaC61S mutant than in alphabetagamma-wild-type for structural stabilization
additional information
-
the gamma-subunit by itself is necessary for the adequate binding of FMN and [2Fe-2S], particularly the latter. The removal of the [4Fe-4S] cluster may result in the easier formation of a disulfide bond between the remaining three cysteine residues in [Fe-S]site 1 of the alphabetagammaC61S mutant than in alphabetagamma-wild-type for structural stabilization
additional information
-
the gamma-subunit by itself is necessary for the adequate binding of FMN and [2Fe-2S], particularly the latter. The removal of the [4Fe-4S] cluster may result in the easier formation of a disulfide bond between the remaining three cysteine residues in [Fe-S]site 1 of the alphabetagammaC61S mutant than in alphabetagamma-wild-type for structural stabilization
-
additional information
-
a poor phylogenetic relationship exists between OdhB1 and OdhB2 in spite of them both functioning as octopine dehydrogenases, which provided clear evidence for the acquisition of novel functions by subunit exchange
-
additional information
-
the beta-subunit functions as a catalytic subunit by itself
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterododecamer
additional information
heterododecamer
Q88EK6; Q88EK5
alpha4beta4gamma4, 4 * 42000, beta-subunit, + 4 * 9000, gamma-subunit, + 4 * 45000, alpha-subunit, SDS-PAGE
heterododecamer
-
alpha4beta4gamma4, 4 * 42000, beta-subunit, + 4 * 9000, gamma-subunit, + 4 * 45000, alpha-subunit, SDS-PAGE
-
additional information
Q89E96; Q89E94; Q89E97
BjOdhB1 and BjOdhB2 both assemble with common alpha- and gamma-subunits, and function as the same octopine dehydrogenase. Most of the purified BjOdhAB2C exists as alpha4beta4gamma4 as determined by gel-filtration, while BjOdhB1 is clearly dominant in purified BjOdhAB1C, thereby confirming that the molar ratio of FAD:FMN of the former (1.8:1.0) is similar to that of PpOdhABC. The gene cluster from Bradyrhizobium japonicum consists of genes OdhB1-C-A-B2, from which two proteins, OdhAB1C and OdhAB2C, appear through the assembly of each beta-subunit together with common alpha- and gamma-subunits, overview. A poor phylogenetic relationship exists between OdhB1 and OdhB2 in spite of them both functioning as octopine dehydrogenases, which provided clear evidence for the acquisition of novel functions by subunit exchange
additional information
-
BjOdhB1 and BjOdhB2 both assemble with common alpha- and gamma-subunits, and function as the same octopine dehydrogenase. Most of the purified BjOdhAB2C exists as alpha4beta4gamma4 as determined by gel-filtration, while BjOdhB1 is clearly dominant in purified BjOdhAB1C, thereby confirming that the molar ratio of FAD:FMN of the former (1.8:1.0) is similar to that of PpOdhABC. The gene cluster from Bradyrhizobium japonicum consists of genes OdhB1-C-A-B2, from which two proteins, OdhAB1C and OdhAB2C, appear through the assembly of each beta-subunit together with common alpha- and gamma-subunits, overview. A poor phylogenetic relationship exists between OdhB1 and OdhB2 in spite of them both functioning as octopine dehydrogenases, which provided clear evidence for the acquisition of novel functions by subunit exchange
additional information
-
BjOdhB1 and BjOdhB2 both assemble with common alpha- and gamma-subunits, and function as the same octopine dehydrogenase. Most of the purified BjOdhAB2C exists as alpha4beta4gamma4 as determined by gel-filtration, while BjOdhB1 is clearly dominant in purified BjOdhAB1C, thereby confirming that the molar ratio of FAD:FMN of the former (1.8:1.0) is similar to that of PpOdhABC. The gene cluster from Bradyrhizobium japonicum consists of genes OdhB1-C-A-B2, from which two proteins, OdhAB1C and OdhAB2C, appear through the assembly of each beta-subunit together with common alpha- and gamma-subunits, overview. A poor phylogenetic relationship exists between OdhB1 and OdhB2 in spite of them both functioning as octopine dehydrogenases, which provided clear evidence for the acquisition of novel functions by subunit exchange
-
additional information
Q88EK6; Q88EK5
PpOpnDH (alpha4beta4gamma4) contained 2 FAD (alpha- and beta-subunits), 1 FMN (between the alpha- and beta-subunits), and 1 [2Fe-2S] iron-sulfur cluster (gamma-subunit) within the structural unit of alphabetagamma. The beta- and alpha-subunit are both necessary for substrate binding, but the beta-subunit functions as a catalytic subunit by itself
additional information
-
PpOpnDH (alpha4beta4gamma4) contained 2 FAD (alpha- and beta-subunits), 1 FMN (between the alpha- and beta-subunits), and 1 [2Fe-2S] iron-sulfur cluster (gamma-subunit) within the structural unit of alphabetagamma. The beta- and alpha-subunit are both necessary for substrate binding, but the beta-subunit functions as a catalytic subunit by itself
additional information
-
PpOpnDH (alpha4beta4gamma4) contained 2 FAD (alpha- and beta-subunits), 1 FMN (between the alpha- and beta-subunits), and 1 [2Fe-2S] iron-sulfur cluster (gamma-subunit) within the structural unit of alphabetagamma. The beta- and alpha-subunit are both necessary for substrate binding, but the beta-subunit functions as a catalytic subunit by itself
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C382S
Q89E96; Q89E94; Q89E97
site-directed mutagenesis, FAD and FMN are detected at very low level in the extract of the alphaC382Sbetagamma mutant. The recombinant expression level of the alphaC382Sbetagamma mutant is approximately 6fold lower than that of alphabetagamma-wild-type
C61S
Q89E96; Q89E94; Q89E97
site-directed mutagenesis, the alphabetagammaC61S mutant is more resistant to the thermal treatment than the wild-type
C382S
-
site-directed mutagenesis, FAD and FMN are detected at very low level in the extract of the alphaC382Sbetagamma mutant. The recombinant expression level of the alphaC382Sbetagamma mutant is approximately 6fold lower than that of alphabetagamma-wild-type
-
C61S
-
site-directed mutagenesis, the alphabetagammaC61S mutant is more resistant to the thermal treatment than the wild-type
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
Q89E96; Q89E94; Q89E97
after incubation for 10 min at 45°C, pH 8.0, the activities of mutant alphabetagammaC61S and alphabetagamma-wild-type maintain 49% and 30% of initial activity, respectively
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His- and S-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity chromatography as holoenzymes. The expression level of the alphaC382Sbetagamma mutant is approximately 6fold lower than that of alphabetagamma-wild-type
Q89E96; Q89E94; Q89E97
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, dialysis, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, dialysis, and gel filtration
Q88EK6; Q88EK5
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, dialysis, and gel filtration
Q89E96; Q89E94; Q89E97
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes bll7191, bll7190, and bll7192, sequence comparisons and phylogenetic analysis, recombinant expression from vectors pETDuet-1, pACYCDuet-1, and pCOLADuet-1 with the (His)6-tag attached to the N-terminus of the bll7190 gene, whereas the S-tag is attached to the C-termini of the bll7191 and bll7192 genes, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Q89E96; Q89E94; Q89E97
PpOdhB, PpOdhC, and PpOdhA genes in the PpOdhABC gene cluster, the genes encoding the beta-, gamma-, and alpha-subunits are arranged in tandem on the bacterial genome, genetic structure overview, and amino acid sequence determination, analysis, and comparisons, genetic structure, phylogenetic analysis, recombinant expression as N-terminally His6-tagged proteins in Escherichia coli strain BL21(DE3), recombinant expression of the PpOdhABC gene cluster in Pseudomonas putida
Q88EK6; Q88EK5
the gene cluster from Bradyrhizobium japonicum consists of genes OdhB1-C-A-B2, from which two proteins, OdhAB1C and OdhAB2C, appear through the assembly of each beta-subunit together with common alpha- and gamma-subunits, and amino acid sequence determination, analysis, and comparisons, genetic structure, phylogenetic analysis, recombinant expression as N-terminally His6-tagged proteins in Escherichia coli strain BL21(DE3), recombinant expression of the PpOdhABC gene cluster in Pseudomonas putida
Q89E96; Q89E94; Q89E97
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Watanabe, S.; Tajima, K.; Matsui, K.; Watanabe, Y.
Characterization of iron-sulfur clusters in flavin-containing opine dehydrogenase
Biosci. Biotechnol. Biochem.
80
2371-2375
2016
Bradyrhizobium japonicum (Q89E96 AND Q89E94 AND Q89E97), Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA110 (Q89E96 AND Q89E94 AND Q89E97)
brenda
Watanabe, S.; Sueda, R.; Fukumori, F.; Watanabe, Y.
Characterization of flavin-containing opine dehydrogenase from bacteria
PLoS ONE
10
e0138434
2015
Pseudomonas putida (Q88EK6 AND Q88EK5), Pseudomonas putida, Bradyrhizobium japonicum (Q89E96 AND Q89E94 AND Q89E97), Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA110 (Q89E96 AND Q89E94 AND Q89E97), Pseudomonas putida KT 2240 (Q88EK6 AND Q88EK5)
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