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Information on EC 1.1.1.399 - 2-oxoglutarate reductase for references in articles please use BRENDA:EC1.1.1.399
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EC Tree
IUBMB Comments 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 .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-ketoglutarate reductase, alphaKG reductase, OGR,
serA ,
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alpha-ketoglutarate reductase
alpha-ketoglutarate reductase
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alpha-ketoglutarate reductase
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OGR
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serA
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(R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
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(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].
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(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
additional information
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(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
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no activity with oxaloacetate, pyruvate, 2-oxobutyrate and glyoxylate
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NADPH is oxidized in the presence of 2-oxoglutarate. The rate of this reaction is 3 to 4% of that observed with NADH
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oxaloacetate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, and glyoxalate are not reduced by the enzyme
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additional information
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NADPH is oxidized in the presence of 2-oxoglutarate. The rate of this reaction is 3 to 4% of that observed with NADH
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additional information
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oxaloacetate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, and glyoxalate are not reduced by the enzyme
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(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
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r
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NADH
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the enzyme is almost entirely specific towards NADH
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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
L-serine
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noncompetitive inhibition
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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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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
0.000064
2-oxoglutarate
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at pH 7.5 and 25°C
0.088
2-oxoglutarate
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at pH 7.5 and 37°C
0.12
2-oxoglutarate
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at pH 6.5 and 25°C
0.000004
NADH
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at pH 7.5 and 25°C
0.3
NADH
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at pH 6.5 and 25°C
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33.3
2-oxoglutarate
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at pH 7.5 and 37°C
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380
2-oxoglutarate
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at pH 7.5 and 37°C
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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
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0.0076
L-serine
Escherichia coli
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at pH 7.5 and 37°C
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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
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brenda
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brenda
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brenda
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brenda
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46000
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x * 46000, SDS-PAGE
68000
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x * 68000, SDS-PAGE
74000 - 78000
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gel filtration
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x * 46000, SDS-PAGE
homodimer
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2 * 36000-40000, SDS-PAGE
homodimer
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2 * 36000-40000, SDS-PAGE
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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
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-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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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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expressed in Escherichia coli JM105 cells
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Zhao, G.; Winkler, M.E.
A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12, and its possible implications for human 2-hydroxyglutaric aciduria
J. Bacteriol.
178
232-239
1996
Escherichia coli
brenda
Gharbia, S.; Shah, H.
Isolation, purification and characterisation of 2-oxoglutarate reductase from Fusobacterium nucleatum
FEMS Microbiol. Lett.
80
283-288
1991
Fusobacterium nucleatum
brenda
Gharbia, S.; Shah, H.
Glutamate dehydrogenase and 2-oxoglutarate reductase electrophoretic patterns and deoxyribonucleic acid-deoxyribonucleic acid hybridization among human oral isolates of Fusobacterium nucleatum
Int. J. Syst. Bacteriol.
39
467-470
1989
Fusobacterium nucleatum
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brenda
Lerud, R.; Whiteley, H.
Purification and properties of alpha-ketoglutarate reductase from Micrococcus aerogenes
J. Bacteriol.
106
571-577
1971
Micrococcus aerogenes 228, Micrococcus aerogenes
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Gharbia, S.E.; Shah, H.N.
Identification of Fusobacterium species by the electrophoretic migration of glutamate dehydrogenase and 2-oxoglutarate reductase in relation to their DNA base composition and peptidoglycan dibasic amino acids
J. Med. Microbiol.
33
183-188
1990
Eubacterium sulci, Filifactor alocis, Fusobacterium gonidiaformans, Fusobacterium mortiferum, Fusobacterium naviforme, Fusobacterium necrogenes, Fusobacterium necrophorum, Fusobacterium nucleatum, Fusobacterium periodonticum, Fusobacterium russii, Fusobacterium simiae, Fusobacterium ulcerans, Fusobacterium varium
brenda
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Enzyme Nomenclature
1.1.1.399 2-oxoglutarate reductase
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