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Information on EC 1.1.1.399 - 2-oxoglutarate reductase
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1.1.1.399 2-oxoglutarate reductaseIUBMB 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 .
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Word Map
- 1.1.1.399
- fusobacterium
- nucleatum
- butyrate
- sulci
- mortiferum
- varium
- prevotella
-
diaminopimelic
- peptidoglycan
The enzyme appears in viruses and cellular organisms
Synonyms
alpha-ketoglutarate reductase, alphaKG reductase, OGR, serA, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-ketoglutarate reductase
OGR
serA
serA
-
-
gene name
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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].
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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
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
-
r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
-
r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
-
r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
-
-
-
-
r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
-
-
-
-
r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
-
-
-
-
r
additional information
?
-
-
no activity with oxaloacetate, pyruvate, 2-oxobutyrate and glyoxylate
-
-
-
additional information
?
-
-
NADPH is oxidized in the presence of 2-oxoglutarate. The rate of this reaction is 3 to 4% of that observed with NADH
-
-
-
additional information
?
-
-
oxaloacetate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, and glyoxalate are not reduced by the enzyme
-
-
-
additional information
?
-
-
NADPH is oxidized in the presence of 2-oxoglutarate. The rate of this reaction is 3 to 4% of that observed with NADH
-
-
-
additional information
?
-
-
oxaloacetate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, and glyoxalate are not reduced by the enzyme
-
-
-
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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
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
-
r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
-
r
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
-
r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
-
-
-
-
r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
-
-
-
-
r
2-oxoglutarate + NADH + H+
(R)-2-hydroxyglutarate + NAD+
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
SER33_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
469
0
51188
Swiss-Prot
SERA_ECOL6
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
410
0
44176
Swiss-Prot
SERA_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
410
0
44665
Swiss-Prot
SERA_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
528
0
54554
Swiss-Prot
SERA_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
528
0
54554
Swiss-Prot
SERA_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
528
0
54554
Swiss-Prot
SERA_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
466
0
50883
Swiss-Prot
SERA_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
554
0
59222
Swiss-Prot
SERA_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
469
0
51193
Swiss-Prot
HGDH_ACIFV
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
331
0
36586
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
-
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
-
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, high protein concentrations (1 mg/ml or more), several months, no loss of activity
-
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
-
DEAE-cellulose column chromatography, hydroxyapatite column chromatography, and 5'-AMP-Sepharose affinity column chromatography
-
Sepharose-4B-(glutathione-2-pyridyl disulfide) column chromatography
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
brenda
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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