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Information on EC 1.1.5.13 - (S)-2-hydroxyglutarate dehydrogenase
for references in articles please use BRENDA:EC1.1.5.13
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.5 With a quinone or similar compound as acceptor
1.1.5.13 (S)-2-hydroxyglutarate dehydrogenase
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
showSynonyms
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-2-hydroxyglutarate dehydrogenase
lhgO
YgaF
L-2-hydroxyglutarate dehydrogenase
-
-
ambiguous
-
lhgO
-
-
-
-
YgaF
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-2-hydroxyglutarate + a quinone = 2-oxoglutarate + a quinol
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
L-lysine degradation I
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SYSTEMATIC NAME
IUBMB Comments
(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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-2-hydroxyglutarate + 2,6-dichlorophenolindophenol
2-oxoglutarate + reduced 2,6-dichlorophenolindophenol
-
Substrates: 3.7% activity compared to L-2-hydroxyglutarate
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L-2-hydroxyglutarate + 2,6-dichlorophenolindophenol
2-oxoglutarate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
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L-2-hydroxyglutarate + iodonitrotetrazolium
2-oxoglutarate + reduced iodonitrotetrazolium
-
Substrates: -
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L-2-hydroxyglutarate + menaquinone-4
2-oxoglutarate + menaquinol-4
-
Substrates: -
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L-2-hydroxyglutarate + O2
2-oxoglutarate + H2O2
-
Substrates: -
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L-2-hydroxyglutarate + ubiquinone-1
2-oxoglutarate + ubiquinol-1
-
Substrates: -
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
-
Substrates: -
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
-
Substrates: -
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
-
Substrates: -
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additional information
?
-
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Substrates: 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
?
-
-
Substrates: 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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-2-hydroxyglutarate + O2
2-oxoglutarate + H2O2
-
Substrates: -
Products: -
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L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
-
Substrates: -
Products: -
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?
L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
-
Substrates: -
Products: -
Products: -
?
L-2-hydroxyglutarate + a quinone
2-oxoglutarate + a quinol
-
Substrates: -
Products: -
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the enzyme contains FAD. The addition of 2.5 mM FAD results in 31% increase of activity as measured without FAD
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the activity is not affected by 0.01 mM Co2+, 0.01 mM Zn2+, or 1 mM EDTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
L-2-hydroxyglutarate
-
in the absence of FAD, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme suppresses both in vitro cell migration and in vivo tumor growth in renal cell carcinoma
Show AA Sequence and Transmembrane Helices (889 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA-exon9
E176D
K81E
-
the mutation leads to severely reduced enzyme activity and is associated with L-2-hydroxyglutaric aciduria
DELTA-exon9
-
the mutation leads to severely reduced enzyme activity and is associated with L-2-hydroxyglutaric aciduria
E176D
-
the mutation leads to severely reduced enzyme activity and is associated with L-2-hydroxyglutaric aciduria
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
lower enzyme expression is associated with tumor progression and/or worsened prognosis in patients with renal cell carcinoma
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rzem, R.; Veiga-da-Cunha, M.; Noel, G.; Goffette, S.; Nassogne, M.C.; Tabarki, B.; Scholler, 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
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
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
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
EXTERNAL LINKS (specific for EC-Number 1.1.5.13)
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