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EC Tree
IUBMB Comments The enzyme, characterized from the bacterium Escherichia coli, contains an FAD cofactor that is not covalently attached. It is bound to the cytoplasmic membrane and is coupled to the membrane quinone pool.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
L-2-HG dehydrogenase, L-2-hydroxyglutarate dehydrogenase, L-2-hydroxyglutarate oxygenase, L-2HG dehydrogenase, L-2HGDH, L2HG dehydrogenase, L2HG:quinone oxidoreductase, L2HGDH,
lhgO ,
YgaF ,
more
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L-2-hydroxyglutarate dehydrogenase
L-2-hydroxyglutarate oxygenase
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L2HG:quinone oxidoreductase
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L-2-hydroxyglutarate dehydrogenase
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ambiguous
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L-2-hydroxyglutarate dehydrogenase
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L-2-hydroxyglutarate dehydrogenase
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L-2-hydroxyglutarate dehydrogenase
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lhgO
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YgaF
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(S)-2-hydroxyglutarate + a quinone = 2-oxoglutarate + a quinol
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(S)-2-hydroxyglutarate:quinone oxidoreductase
The enzyme, characterized from the bacterium Escherichia coli, contains an FAD cofactor that is not covalently attached. It is bound to the cytoplasmic membrane and is coupled to the membrane quinone pool.
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D-2-hydroxyglutarate + 2,6-dichlorophenolindophenol
2-oxoglutarate + reduced 2,6-dichlorophenolindophenol
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3.7% activity compared to L-2-hydroxyglutarate
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L-2-hydroxyglutarate + 2,6-dichlorophenolindophenol
2-oxoglutarate + reduced 2,6-dichlorophenolindophenol
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
L-2-hydroxyglutarate + iodonitrotetrazolium
2-oxoglutarate + reduced iodonitrotetrazolium
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L-2-hydroxyglutarate + menaquinone-4
2-oxoglutarate + menaquinol-4
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L-2-hydroxyglutarate + O2
2-oxoglutarate + H2O2
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L-2-hydroxyglutarate + oxidized o-phenylendiamine
alpha-ketoglutarate + reduced o-phenylendiamine
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experimental setup
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ir
L-2-hydroxyglutarate + ubiquinone-1
2-oxoglutarate + ubiquinol-1
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additional information
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
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additional information
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the enzyme is not active in the presence of NAD+, NADP+, cytochrome c or O2. No activity with glycolate, L-lactate or D-lactate
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additional information
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no activity with dimethylglycine, sarcosine, butyraldehyde or 3-hydroxybutyric acid. Most 2-hydroxy acids are ineffective as substrates, including L-malic acid, DL-malic acid, DL-lactic acid, L-mandelic acid, D-mandelic acid, and 2-hydroxycaproic acid
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
L-2-hydroxyglutarate + O2
2-oxoglutarate + H2O2
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
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FAD
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dependent on
FAD
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the enzyme contains a noncovalently bound FAD
FAD
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the enzyme contains FAD. The addition of 2.5 mM FAD results in 31% increase of activity as measured without FAD
additional information
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not affected by NAD+ or NADP+
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additional information
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not stimulated by FMN
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additional information
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the enzyme is not stimulated by FMN
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additional information
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the activity is not affected by 0.01 mM Co2+, 0.01 mM Zn2+, or 1 mM EDTA
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0.15
iodonitrotetrazolium
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at pH 7.1 and 30°C
0.095 - 0.8
L-2-hydroxyglutarate
0.095
L-2-hydroxyglutarate
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0.095
L-2-hydroxyglutarate
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at pH 7.0 and 25°C
0.24
L-2-hydroxyglutarate
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at pH 7.4 and 30°C
0.8
L-2-hydroxyglutarate
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in the absence of FAD, pH and temperature not specified in the publication
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0.08 - 613
L-2-hydroxyglutarate
0.08
L-2-hydroxyglutarate
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0.08
L-2-hydroxyglutarate
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at pH 7.0 and 25°C
613
L-2-hydroxyglutarate
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at pH 7.4 and 30°C
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6.5 - 8.5
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more than 50% activity between pH 6.5 and 8.5
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ecotype Columbia-0
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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high expression
brenda
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highest expression
brenda
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brenda
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brenda
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brenda
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brenda
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lowest expression
brenda
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brenda
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mutation A241G in A498 cells
brenda
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brenda
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brenda
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brenda
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malfunction
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enzyme mutations cause L-2-hydroxyglutaric aciduria
physiological function
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the enzyme suppresses both in vitro cell migration and in vivo tumor growth in renal cell carcinoma
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47640
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theoretical value, verified by SDS-PAGE
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x * 46000, SDS-PAGE
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x * 47640, His-tagged protein, calculated from amino acid sequence
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K71E
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the mutation is associated with L-2-hydroxyglutaric aciduria
K81E
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the mutation leads to severely reduced enzyme activity and is associated with L-2-hydroxyglutaric aciduria
DELTA-exon9
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the mutation is associated with L-2-hydroxyglutaric aciduria
DELTA-exon9
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the mutation leads to severely reduced enzyme activity and is associated with L-2-hydroxyglutaric aciduria
E176D
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the mutation is associated with L-2-hydroxyglutaric aciduria
E176D
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the mutation leads to severely reduced enzyme activity and is associated with L-2-hydroxyglutaric aciduria
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DEAE Sepharose column chromatography and Q-Sepharose column chromatography
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Ni-NTA agarose column chromatography
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Ni-NTA column chromatography
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Ni-NTA-Sepharose 6 column chromatography
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using a Ni-charged nitrilotriacetic acid-Sepharose 6 fast-flow column
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli C41(DE3) cells
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expressed in HEK-293T cells
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medicine
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lower enzyme expression is associated with tumor progression and/or worsened prognosis in patients with renal cell carcinoma
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Kalliri, E.; Mulrooney, S.B.; Hausinger, R.P.
Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase
J. Bacteriol.
190
3793-3798
2008
Escherichia coli
brenda
Rzem, R.; Van Schaftingen, E.; Veiga-da-Cunha, M.
The gene mutated in L-2-hydroxyglutaric aciduria encodes L-2-hydroxyglutarate dehydrogenase
Biochimie
88
113-116
2006
Homo sapiens
brenda
Shelar, S.; Shim, E.H.; Brinkley, G.J.; Kundu, A.; Carobbio, F.; Poston, T.; Tan, J.; Parekh, V.; Benson, D.; Crossman, D.K.; Buckhaults, P.J.; Rakheja, D.; Kirkman, R.; Sato, Y.; Ogawa, S.; Dutta, S.; Velu, S.E.; Emberley, E.; Pan, A.; Chen, J.; Huang, T.; Absher, D.; Becker, A.; Kunick, C.; Sudarshan, S.
Biochemical and epigenetic insights into L-2-hydroxyglutarate, a potential therapeutic target in renal cancer
Clin. Cancer Res.
24
6433-6446
2018
Homo sapiens
brenda
Kalliri, E.; Mulrooney, S.; Hausinger, R.
Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase
J. Bacteriol.
190
3793-3798
2008
Escherichia coli
brenda
Knorr, S.; Sinn, M.; Galetskiy, D.; Williams, R.; Wang, C.; Mueller, N.; Mayans, O.; Schleheck, D.; Hartig, J.
Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate
Nat. Commun.
9
5071
2018
Escherichia coli
brenda
Huedig, M.; Maier, A.; Scherrers, I.; Seidel, L.; Jansen, E.E.; Mettler-Altmann, T.; Engqvist, M.K.; Maurino, V.G.
Plants possess a cyclic mitochondrial metabolic pathway similar to the mammalian metabolic repair mechanism involving malate dehydrogenase and L-2-hydroxyglutarate dehydrogenase
Plant Cell Physiol.
56
1820-1830
2015
Arabidopsis thaliana
brenda
Rzem, R.; Veiga-da-Cunha, M.; Noel, G.; Goffette, S.; Nassogne, M.C.; Tabarki, B.; Schoeller, C.; Marquardt, T.; Vikkula, M.; Van Schaftingen, E.
A gene encoding a putative FAD-dependent L-2-hydroxyglutarate dehydrogenase is mutated in L-2-hydroxyglutaric aciduria
Proc. Natl. Acad. Sci. USA
101
16849-16854
2004
Homo sapiens
brenda
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