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Information on EC 1.1.99.2 - L-2-hydroxyglutarate dehydrogenase
for references in articles please use BRENDA:EC1.1.99.2
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.99 With unknown physiological acceptors
1.1.99.2 L-2-hydroxyglutarate dehydrogenase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.1.99.2
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aciduria
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neurometabolic
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ataxia
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l-2-hga
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subcortical
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psychomotor
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oncometabolite
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neuroradiological
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terrier
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extrapyramidal
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macrocephaly
- d2hgdh
- leukoencephalopathy
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hyperintensity
- medicine
showSynonyms
l2hgdh, l-2-hydroxyglutarate dehydrogenase, 2-hydroxyglutarate dehydrogenase, l-2-hg dehydrogenase, l-2hg dehydrogenase, l-2-hgdh, l-2hgdh, l-2-hydroxyglutaric acid dehydrogenase, alpha-ketoglutarate reductase, alpha-hydroxyglutarate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxyglutarate dehydrogenase
alpha-hydroxyglutarate dehydrogenase
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alpha-hydroxyglutarate dehydrogenase (NAD+ specific)
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alpha-hydroxyglutarate oxidoreductase
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alpha-ketoglutarate reductase
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dehydrogenase, 2-hydroxyglutarate
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hydroxyglutaric dehydrogenase
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L-2-hydroxyglutarate dehydrogenase
L-2-hydroxyglutaric acid dehydrogenase
L-alpha-hydroxyglutarate dehydrogenase
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L-alpha-hydroxyglutarate:NAD+ 2-oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
(S)-2-hydroxyglutarate:acceptor 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9028-80-2
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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
(R)-2-hydroxyglutarate + 2,6-dichlorophenolindophenol
2-oxoglutarate + reduced 2,6-dichlorophenolindophenol
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Substrates: 3.7% activity compared to (S)-2-hydroxyglutarate
Products: -
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(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH
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Substrates: about 10% of the activity with (S)-2-hydroxyglutarate
Products: -
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(S)-2-hydroxyglutarate + 2,6-dichlorophenolindophenol
2-oxoglutarate + reduced 2,6-dichlorophenolindophenol
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Substrates: -
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(S)-2-hydroxyglutarate + iodonitrotetrazolium
2-oxoglutarate + ?
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Substrates: -
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2-hydroxy-n-hexanoate + NAD+
2-oxo-n-hexanoate + NADH + H+
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Substrates: at 12.4% of the activity with 2-oxoglutarate
Products: -
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?
2-hydroxy-n-pentanoate + NAD+
2-oxo-n-pentanoate + NADH + H+
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Substrates: at 10.7% of the activity with 2-oxoglutarate
Products: -
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?
2-hydroxybutanoate + NAD+
2-oxobutanoate + NADH
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Substrates: at 9.6% of the activity with 2-oxoglutarate
Products: -
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?
2-hydroxymalonate + NAD+
oxomalonate + NADH + H+
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Substrates: at 29.3% of the activity with 2-oxoglutarate
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L-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
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Substrates: -
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L-2-hydroxyglutarate + iodonitrotetrazolium chloride
2-oxoglutarate + reduced iodonitrotetrazolium chloride
Substrates: activity assay
Products: -
Products: -
?
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
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Substrates: -
Products: -
Products: -
?
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
Substrates: enzyme deficiency might be the cause of L-2-hydroxyglutaric aciduria
Products: -
Products: -
?
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
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Substrates: -
Products: -
Products: -
?
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
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Substrates: enzyme deficiency might be the cause of L-2-hydroxyglutaric aciduria
Products: -
Products: -
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(S)-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
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Substrates: -
Products: -
Products: -
?
(S)-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
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Substrates: enzyme deficiency might be the cause of L-2-hydroxyglutaric aciduria
Products: -
Products: -
?
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: in the reverse reaction almost 100% production of the S-isomer of 2-hydroxyglutarate
Products: -
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r
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: -
Products: -
Products: -
?
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: -
Products: -
Products: -
?
L-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: -
Products: -
Products: -
?
L-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: -
Products: -
Products: -
r
L-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: high levels of the enzyme is produced at the late stage of cultivation in the presence of citrate and with limited aeration
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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, as well as glycolate, D-lactate and L-lactate
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?
additional information
?
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Substrates: mutations (K81E, E176D, DELTA-exon9) found in patients with L-2-hydroxyglutaric aciduria supress L-2-hydroxyglutarate dehydrogenase activity. L-2-hydroxyglutartic aciduria is due to a deficiency in L-2-hydroxyglutarate dehydrogenase
Products: -
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additional information
?
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Substrates: no activity with 3-acetylpyridine adenine dinucleotide or NADP+
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?
additional information
?
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Substrates: no activity with D-2-hydroxyglutarate, L-malate, and L-lactate
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additional information
?
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Substrates: no activity with 3-acetylpyridine adenine dinucleotide or NADP+
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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
(S)-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
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Substrates: enzyme deficiency might be the cause of L-2-hydroxyglutaric aciduria
Products: -
Products: -
?
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: -
Products: -
Products: -
?
L-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
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Substrates: -
Products: -
Products: -
ir
L-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
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Substrates: -
Products: -
Products: -
r
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
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Substrates: -
Products: -
Products: -
?
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
Substrates: enzyme deficiency might be the cause of L-2-hydroxyglutaric aciduria
Products: -
Products: -
?
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
-
Substrates: enzyme deficiency might be the cause of L-2-hydroxyglutaric aciduria
Products: -
Products: -
?
additional information
?
-
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Substrates: high levels of the enzyme is produced at the late stage of cultivation in the presence of citrate and with limited aeration
Products: -
Products: -
?
additional information
?
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Substrates: mutations (K81E, E176D, DELTA-exon9) found in patients with L-2-hydroxyglutaric aciduria supress L-2-hydroxyglutarate dehydrogenase activity. L-2-hydroxyglutartic aciduria is due to a deficiency in L-2-hydroxyglutarate dehydrogenase
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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activity is not affected by 0.01 mM Co2+ or 0.01 mM Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Diseases
A novel compound heterozygous mutation in a Chinese boy with L-2-hydroxyglutaric aciduria: a case study.
Brain Neoplasms
L-2-hydroxyglutaric aciduria and brain tumors in children with mutations in the L2HGDH gene: neuroimaging findings.
Brain Neoplasms
Mutational analysis of D2HGDH and L2HGDH in brain tumours without IDH1 or IDH2 mutations.
Carcinoma
Biochemical and Epigenetic Insights into L-2-Hydroxyglutarate, a Potential Therapeutic Target in Renal Cancer.
Carcinoma
Epigenetic dysregulation by aberrant metabolism in renal cell carcinoma can be reversed with Ascorbic acid.
Carcinoma, Renal Cell
Biochemical and Epigenetic Insights into L-2-Hydroxyglutarate, a Potential Therapeutic Target in Renal Cancer.
Carcinoma, Renal Cell
Epigenetic dysregulation by aberrant metabolism in renal cell carcinoma can be reversed with Ascorbic acid.
Drug Resistant Epilepsy
White matter abnormalities in an adult patient with l-2-hydroxyglutaric aciduria.
Intellectual Disability
White matter abnormalities in an adult patient with l-2-hydroxyglutaric aciduria.
l-2-hydroxyglutarate dehydrogenase deficiency
Adult manifestation of L-2-hydroxyglutarate dehydrogenase deficiency by a novel mutation.
l-2-hydroxyglutarate dehydrogenase deficiency
Familial hyperlysinaemia due to L-lysine alpha-ketoglutarate reductase deficiency: results of attempted treatment.
l-2-hydroxyglutarate dehydrogenase deficiency
L2hgdh Deficiency Accumulates l-2-Hydroxyglutarate with Progressive Leukoencephalopathy and Neurodegeneration.
Leukoencephalopathies
L2hgdh Deficiency Accumulates l-2-Hydroxyglutarate with Progressive Leukoencephalopathy and Neurodegeneration.
Leukoencephalopathies
Metabolite proofreading, a neglected aspect of intermediary metabolism.
Neoplasms
Another small molecule in the oncometabolite mix: L-2-Hydroxyglutarate in kidney cancer.
Neoplasms
Biochemical and Epigenetic Insights into L-2-Hydroxyglutarate, a Potential Therapeutic Target in Renal Cancer.
Neoplasms
L-2-Hydroxyglutarate: an epigenetic modifier and putative oncometabolite in renal cancer.
Neuroinflammatory Diseases
L2hgdh Deficiency Accumulates l-2-Hydroxyglutarate with Progressive Leukoencephalopathy and Neurodegeneration.
Starvation
An L-2-hydroxyglutarate biosensor based on specific transcriptional regulator LhgR.
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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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Ki 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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
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pH 5.0: about 45% of maximal activity, pH 8.5: 60% of maximal activity, reaction with alpha-oxoglutarate and NADH
7.3 - 9.3
7.3 - 9.3
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the enzyme is active over a wide pH range (7.3-9.3) with no clear optimum
7.3 - 9.3
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the enzyme is active over a wide pH range (7.3-9.3) with no clear optimum
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TEMPERATURE OPTIMUM
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
-
high levels of the enzyme is produced at the late stage of cultivation in the presence of citrate and with limited aeration
brenda
additional information
additional information
-
no activity in heart, brain and skeletal muscle, cultured human skin fibroblasts and transformed lymphocyte
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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L-2-hydroxyglutaric aciduria is a rare inborn error of metabolism in the enzyme is defective
metabolism
metabolism
L-2-hydroxyglutarate dehydrogenase might be regarded as an enzyme of metabolic repair
metabolism
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2-hydroxyglutarate dehydrogenase is involved exclusively in lysine degradation. 2-hydroxyglutarate dehydrogenase act as electron donors to the ubiquinol pool via an electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase-mediated route
Show AA Sequence and Transmembrane Helices (139 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E176D
K81E
additional information
additional information
A320G, G607T, naturally occurring mutations found in L-2-hydroxyglutaric aciduria affected patients
additional information
-
A320G, G607T, naturally occurring mutations found in L-2-hydroxyglutaric aciduria affected patients
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme separated from D-2-hydroxyglutarate dehydrogenase by chromatography on DEAE-sepharose
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partially purified from liver, further purification not possible due to the instability of the enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transfection of HEK cells with cDNA encoding the product of the human gene leads to more than 15fold increase in L-2-hydroxyglutarate dehydrogenase activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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L-2-hydroxyglutaric aciduria is a neurometabolic disorder that produces a variety of clinical neurological deficits, mutations within the gene L2HGDH encoding L-2-hydroxyglutaric acid dehydrogenase causes the disease, the canine model shares many of the clinical features of the disease in humans and represents a valuable resource as a spontaneous model of L-2-hydroxyglutaric aciduria
medicine
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L-2-hydroxyglutaric aciduria is a rare autosomal recessive neurometabolic organic aciduria, case report, mutation analysis and measurement of L-2-hydroxyglutaric acid in the amniotic fluid is used for prenatal diagnosis of the disease
medicine
an enzyme assay for the determination of L-2-hydroxyglutarate dehydrogenase activity in cells derived from L-2-hydroxyglutaric aciduria patients is developed and implemented
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suzuki, T.; Uozomi, T.; Beppu, T.
Purification and characterization of a-hydroxyglutarate dehydrogenase from Alcaligenes sp.
Agric. Biol. Chem.
49
2939-2947
1985
Alcaligenes sp.
-
brenda
Jansen, G.A.; Wanders, R.J.A.
L-2-Hydroxyglutarate dehydrogenase: identification of a novel enzyme activity in rat and human liver. Implications for L-2-hydroxyglutaric acidemia
Biochim. Biophys. Acta
1225
53-56
1993
Homo sapiens, Rattus norvegicus
brenda
Achouri, Y.; Noel, G.; Vertommen, D.; Rider, M.H.; Veiga-da-Cunha, M.; van Schaftingen, E.
Identification of a dehydrogenase acting on D-2-hydroxyglutarate
Biochem. J.
381
35-42
2004
Rattus norvegicus
brenda
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 (Q9H9P8), Homo sapiens, Rattus norvegicus
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
Penderis, J.; Calvin, J.; Abramson, C.; Jakobs, C.; Pettitt, L.; Binns, M.M.; Verhoeven, N.M.; ODriscoll, E.; Platt, S.R.; Mellersh, C.S.
L-2-hydroxyglutaric aciduria: characterisation of the molecular defect in a spontaneous canine model
J. Med. Genet.
44
334-340
2007
Canis lupus familiaris
brenda
Augoustides-Savvopoulou, P.; Salomons, G.S.; Dotis, J.; Roilides, E.; Leontsini, M.; Jakobs, C.; Panteliadis, C.
Mutation analysis a prerequisite for prenatal diagnosis of L-2-hydroxyglutaric aciduria?
Mol. Genet. Metab.
91
399-401
2007
Homo sapiens
brenda
Kranendijk, M.; Salomons, G.S.; Gibson, K.M.; Aktuglu-Zeybek, C.; Bekri, S.; Christensen, E.; Clarke, J.; Hahn, A.; Korman, S.H.; Mejaski-Bosnjak, V.; Superti-Furga, A.; Vianey-Saban, C.; van der Knaap, M.S.; Jakobs, C.; Struys, E.A.
Development and implementation of a novel assay for L-2-hydroxyglutarate dehydrogenase (L-2-HGDH) in cell lysates: L-2-HGDH deficiency in 15 patients with L-2-hydroxyglutaric aciduria
J. Inherit. Metab. Dis.
32
713-719
2009
Homo sapiens (Q9H9P8)
brenda
Steenweg, M.E.; Jakobs, C.; Errami, A.; van Dooren, S.J.; Adeva Bartolome, M.T.; Aerssens, P.; Augoustides-Savvapoulou, P.; Baric, I.; Baumann, M.; Bonafe, L.; Chabrol, B.; Clarke, J.T.; Clayton, P.; Coker, M.; Cooper, S.; Falik-Zaccai, T.; Gorman, M.; Hahn, A.; Hasanoglu, A.; King, M.D.; de Klerk, H.
An overview of L-2-hydroxyglutarate dehydrogenase gene (L2HGDH) variants: a genotype-phenotype study
Hum. Mutat.
31
380-390
2010
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
Jansen, G.A.; Wanders, R.J.
L-2-hydroxyglutarate dehydrogenase identification of a novel enzyme activity in rat and human liver. Implications for L-2-hydroxyglutaric acidemia
Biochim. Biophys. Acta
1225
53-56
1993
Homo sapiens, Rattus norvegicus
brenda
Hariharan, V.A.; Denton, T.T.; Paraszcszak, S.; McEvoy, K.; Jeitner, T.M.; Krasnikov, B.F.; Cooper, A.J.
The enzymology of 2-hydroxyglutarate, 2-hydroxyglutaramate and 2-hydroxysuccinamate and their relationship to oncometabolites
Biology