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Information on EC 1.1.99.2 - L-2-hydroxyglutarate dehydrogenase and Organism(s) Homo sapiens

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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
l2hgdh, l-2-hydroxyglutarate dehydrogenase, 2-hydroxyglutarate dehydrogenase, l-2-hg dehydrogenase, l-2hg dehydrogenase, l-2-hgdh, l-2hgdh, alpha-ketoglutarate reductase, l-2-hydroxyglutaric acid dehydrogenase, alpha-hydroxyglutarate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-hydroxyglutarate dehydrogenase
-
L2HGDH
alpha-hydroxyglutarate dehydrogenase
-
-
-
-
alpha-hydroxyglutarate dehydrogenase (NAD+ specific)
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-
-
-
alpha-hydroxyglutarate oxidoreductase
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-
-
-
alpha-ketoglutarate reductase
-
-
-
-
dehydrogenase, 2-hydroxyglutarate
-
-
-
-
hydroxyglutaric dehydrogenase
-
-
-
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L-2-HG dehydrogenase
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-
L-2-hydroxyglutarate dehydrogenase
L-2-hydroxyglutaric acid dehydrogenase
-
-
L-alpha-hydroxyglutarate dehydrogenase
-
-
-
-
L-alpha-hydroxyglutarate:NAD+ 2-oxidoreductase
-
-
-
-
L2HGDH
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(S)-2-hydroxyglutarate:acceptor 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-80-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
show the reaction diagram
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
-
-
-
-
?
L-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
show the reaction diagram
-
-
-
-
ir
L-2-hydroxyglutarate + iodonitrotetrazolium chloride
2-oxoglutarate + reduced iodonitrotetrazolium chloride
show the reaction diagram
activity assay
-
-
?
L-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
show the reaction diagram
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
-
-
-
-
?
L-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
show the reaction diagram
-
-
-
-
ir
L-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activity is not affected by 0.01 mM Co2+ or 0.01 mM Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
activity is not affected by 1 mM EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
(S)-2-hydroxyglutarate
-
-
4
L-2-hydroxyglutarate
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at pH 8.7 and 37°C
0.2
NAD+
-
at pH 8.7 and 37°C
additional information
L-2-hydroxyglutarate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.021
-
at pH 8.7 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9.3
-
the enzyme is active over a wide pH range (7.3-9.3) with no clear optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
no activity in heart, brain and skeletal muscle, cultured human skin fibroblasts and transformed lymphocyte
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
L-2-hydroxyglutaric aciduria is a rare inborn error of metabolism in the enzyme is defective
metabolism
L-2-hydroxyglutarate dehydrogenase might be regarded as an enzyme of metabolic repair
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
L2HDH_HUMAN
463
0
50316
Swiss-Prot
Mitochondrion (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A140P
-
the mutation is associated with L-2-hydroxyglutaric aciduria
A184V
-
the mutation is associated with L-2-hydroxyglutaric aciduria
A406V
-
the mutation is associated with L-2-hydroxyglutaric aciduria
A62D
-
the mutation is associated with L-2-hydroxyglutaric aciduria
C179R
-
the mutation is associated with L-2-hydroxyglutaric aciduria
DELTA-exon9
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mutated protein is inactive and abnormally processed
E176D
E176G
-
the mutation is associated with L-2-hydroxyglutaric aciduria
E268X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
E336K
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G116D
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G128X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G156V
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G211D
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G211V
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G260A
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G260V
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G55D
-
the mutation is associated with L-2-hydroxyglutaric aciduria
G57R
-
the mutation is associated with L-2-hydroxyglutaric aciduria
H434P
-
the mutation is associated with L-2-hydroxyglutaric aciduria
H98R
-
the mutation is associated with L-2-hydroxyglutaric aciduria
H98Y
-
the mutation is associated with L-2-hydroxyglutaric aciduria
K246N
-
the mutation is associated with L-2-hydroxyglutaric aciduria
P302L
-
the mutation is associated with L-2-hydroxyglutaric aciduria
P441E
-
the mutation is associated with L-2-hydroxyglutaric aciduria
Q197X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
Q204X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
R251X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
R277X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
R282Q
-
the mutation is associated with L-2-hydroxyglutaric aciduria
R282W
-
the mutation is associated with L-2-hydroxyglutaric aciduria
R335X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
R70X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
S263L
-
the mutation is associated with L-2-hydroxyglutaric aciduria
S263X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
S440Y
-
the mutation is associated with L-2-hydroxyglutaric aciduria
V296E
-
the mutation is associated with L-2-hydroxyglutaric aciduria
Y153X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
Y195C
-
the mutation is associated with L-2-hydroxyglutaric aciduria
Y301X
-
the mutation is associated with L-2-hydroxyglutaric aciduria
Y367C
-
the mutation is associated with L-2-hydroxyglutaric aciduria
additional information
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
6
E24
2017
Homo sapiens
Manually annotated by BRENDA team
Wanders, R.
L-2-hydroxyglutaric aciduria normal L-2-hydroxyglutarate dehydrogenase activity in liver from two new patients
J. Inherit. Metab. Dis.
20
725-726
1997
Homo sapiens
Manually annotated by BRENDA team