Information on EC 1.5.99.B4 - flavin-containing opine dehydrogenase

for references in articles please use BRENDA:EC1.5.99.B4
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.99.B4
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
flavin-containing opine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O = L-arginine + pyruvate + FADH2
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
N2-(D-1-carboxyethyl)-L-arginine:FAD+ oxidoreductase (L-arginine-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunits BjOdhA (bll7191 or ooxA), BjOdhB1 (bll7193), and BjOdhB2 (bll7190 or soxB)
Q89E96 AND Q89E94 AND Q89E97 AND
UniProt
Manually annotated by BRENDA team
subunits BjOdhA (bll7191 or ooxA), BjOdhB1 (bll7193), and BjOdhB2 (bll7190 or soxB)
Q89E96 AND Q89E94 AND Q89E97 AND
UniProt
Manually annotated by BRENDA team
subunits alpha and beta; isolated from soil
Q88EK6 AND Q88EK5
UniProt
Manually annotated by BRENDA team
subunits alpha and beta; isolated from soil
Q88EK6 AND Q88EK5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O
L-arginine + 2-oxoglutarate + FADH2
show the reaction diagram
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O
L-arginine + 2-oxoglutarate + FADH2
show the reaction diagram
N2-(D-1-carboxyethyl)-L-arginine + FAD + H2O
L-arginine + pyruvate + FADH2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[2Fe-2S]-center
[4Fe-4S]-center
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-arginine
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substrate inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.077 - 0.476
N2-(D-1,3-dicarboxypropyl)-L-arginine
0.0078 - 12.9
N2-(D-1-carboxyethyl)-L-arginine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.33 - 315
N2-(D-1,3-dicarboxypropyl)-L-arginine
0.093 - 2.3
N2-(D-1-carboxyethyl)-L-arginine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45.73 - 788.05
N2-(D-1,3-dicarboxypropyl)-L-arginine
0.0163 - 294.87
N2-(D-1-carboxyethyl)-L-arginine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.257
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purified recombinant enzyme mutant alphaC382Sbetagamma, pH 9.0, 30C
0.504
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purified recombinant wild-type enzyme, pH 9.0, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH optimum of BjOdhAB2C and BjOdhAB1C, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterododecamer
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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after incubation for 10 min at 45C, pH 8.0, the activities of mutant alphabetagammaC61S and alphabetagamma-wild-type maintain 49% and 30% of initial activity, respectively
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
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recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, dialysis, and gel filtration
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)
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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 AND 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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C382S
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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
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site-directed mutagenesis, the alphabetagammaC61S mutant is more resistant to the thermal treatment than the wild-type
C382S
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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
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C61S
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site-directed mutagenesis, the alphabetagammaC61S mutant is more resistant to the thermal treatment than the wild-type
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