Information on EC 1.1.1.399 - 2-oxoglutarate reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.399
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RECOMMENDED NAME
GeneOntology No.
2-oxoglutarate reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-glutamate degradation V (via hydroxyglutarate)
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxyglutarate,NAD+ 2-oxidireductase
The enzyme catalyses a reversible reaction. The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate [1,2]. The SerA enzyme from the bacterium Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyses the activity of EC 1.1.1.95, phosphoglycerate dehydrogenase [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl disulfide
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2-oxoglutarate
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inhibitor of the reverse reaction
3-phosphoglycerate
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noncompetitive inhibition
D-2-hydroxyglutaric acid
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competitive inhibition
glycine
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L-serine
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noncompetitive inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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sodium acetate, acetyl phosphate, acetyl coenzyme A, glutamate, histidine, adenosine mono-, di-, and triphosphates, dithiothreitol, N-ethylmaleimide or iodoacetate at a concentration of 0.01-1 mM have no effect on the rate of the reaction
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
(R)-2-hydroxyglutarate
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at pH 8.5 and 25°C
0.000064 - 0.12
2-oxoglutarate
1
NAD+
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at pH 8.5 and 25°C
0.000004 - 0.3
NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33.3
2-oxoglutarate
Escherichia coli
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at pH 7.5 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
380
2-oxoglutarate
Escherichia coli
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at pH 7.5 and 37°C
34
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.7
3-phosphoglycerate
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at pH 7.5 and 37°C
0.37
D-2-hydroxyglutaric acid
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at pH 7.5 and 37°C
0.0054
L-serine
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at pH 7.5 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0076
L-serine
Escherichia coli
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at pH 7.5 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.27
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crude extract, at pH 7.5 and 37°C
9.7
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after 3fold purification, at pH 7.5 and 37°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000 - 78000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
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the enzyme remains stable after 3 min incubation between 0 and 40°C, while 3 min at 45, 50 and 60°C leads to about 40, 70, and 100% loss of activity
45 - 60
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the enzyme is stable at 45°C for 10 min, 70% of its activity is lost at 50°C, 5% of the original activity is retained at 55°C, while incubation at 60°C abolishes all activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, high protein concentrations (1 mg/ml or more), several months, no loss of activity
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0°C, high protein concentrations (1 mg/ml or more), several weeks, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and hydroxylapatite column chromatography
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DEAE-cellulose column chromatography, hydroxyapatite column chromatography, and 5'-AMP-Sepharose affinity column chromatography
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Sepharose-4B-(glutathione-2-pyridyl disulfide) column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM105 cells
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