Information on EC 1.1.99.2 - L-2-hydroxyglutarate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.99.2
-
RECOMMENDED NAME
GeneOntology No.
L-2-hydroxyglutarate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glutamate and glutamine metabolism
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Butanoate metabolism
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SYSTEMATIC NAME
IUBMB Comments
(S)-2-hydroxyglutarate:acceptor 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-80-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
canine, Staffordshire bull terriers
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH
show the reaction diagram
-
about 10% of the activity with (S)-2-hydroxyglutarate
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-
ir
(S)-2-hydroxyglutarate + acceptor
2-oxoglutarate + reduced acceptor
show the reaction diagram
(S)-2-hydroxyglutarate + FAD
2-oxoglutarate + FADH2
show the reaction diagram
(S)-2-hydroxyglutarate + iodonitrotetrazolium
2-oxoglutarate + ?
show the reaction diagram
-
-
-
-
?
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
2-hydroxy-n-hexanoate + NADH
2-oxo-n-hexanoate + NADH
show the reaction diagram
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at 12.4% of the activity with 2-oxoglutarate
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-
?
2-hydroxy-n-pentanoate + NADH
2-oxo-n-pentanoate + NADH
show the reaction diagram
-
at 10.7% of the activity with 2-oxoglutarate
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-
?
2-hydroxybutanoate + NAD+
2-oxobutanoate + NADH
show the reaction diagram
-
at 9.6% of the activity with 2-oxoglutarate
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-
?
2-hydroxymalonate + NADH
oxomalonate + NADH
show the reaction diagram
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at 29.3% of the activity with 2-oxoglutarate
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-
?
L-2-hydroxyglutarate + iodonitrotetrazolium chloride
2-oxoglutarate + reduced iodonitrotetrazolium chloride
show the reaction diagram
activity assay
-
-
?
L-2-hydroxyglutarate + oxidized o-phenylendiamine
alpha-ketoglutarate + reduced o-phenylendiamine
show the reaction diagram
-
experimental setup
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-
ir
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + FAD
2-oxoglutarate + FADH2
show the reaction diagram
-
enzyme deficiency might be the cause of L-2-hydroxyglutaric aciduria
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activation with FMN
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activity is not affected by 0.01 mM Co2+ or 0.01 mM Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-2-hydroxyglutarate
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-
additional information
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activity is not affected by 1 mM EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
(R)-2-hydroxyglutarate
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-
0.8 - 1.7
(S)-2-Hydroxyglutarate
0.12
2-oxoglutarate
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-
0.095
L-2-Hydroxyglutarate
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5.3
NAD+
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-
0.14
NADH
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-
additional information
L-2-Hydroxyglutarate
107 microM/l, lymphoblast; 112 microM/l, fibroblast
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
L-2-Hydroxyglutarate
Escherichia coli
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45
(R)-2-hydroxyglutarate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
activity assay
7.2
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reaction with alpha-oxoglutarate and NADH
7.3 - 9.3
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active over a wide pH range, without a clear optimum
11.5
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reaction with L-2-hydroxyglutarate and NAD+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
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active over a wide pH range, without a clear optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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low level
Manually annotated by BRENDA team
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high levels of the enzyme is produced at the late stage of cultivation in the presence of citrate and with limited aeration
Manually annotated by BRENDA team
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low level
Manually annotated by BRENDA team
additional information
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traces of activity in muscle and spleen
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47640
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theoretical value, verified by SDS-PAGE
48000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 42000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
concentrated by ultrafiltration and crystallized by vapor diffusion method
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very labile in purification processes
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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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using a Ni-charged nitrilotriacetic acid-Sepharose 6 fast-flow column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into the vector pET42b
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A140P
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the mutation is associated with L-2-hydroxyglutaric aciduria
A184V
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the mutation is associated with L-2-hydroxyglutaric aciduria
A406V
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the mutation is associated with L-2-hydroxyglutaric aciduria
A62D
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the mutation is associated with L-2-hydroxyglutaric aciduria
C179R
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the mutation is associated with L-2-hydroxyglutaric aciduria
DELTA-exon9
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mutated protein is inactive and abnormally processed
E176G
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the mutation is associated with L-2-hydroxyglutaric aciduria
E268X
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the mutation is associated with L-2-hydroxyglutaric aciduria
E336K
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the mutation is associated with L-2-hydroxyglutaric aciduria
G116D
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the mutation is associated with L-2-hydroxyglutaric aciduria
G128X
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the mutation is associated with L-2-hydroxyglutaric aciduria
G156V
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the mutation is associated with L-2-hydroxyglutaric aciduria
G211D
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the mutation is associated with L-2-hydroxyglutaric aciduria
G211V
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the mutation is associated with L-2-hydroxyglutaric aciduria
G260A
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the mutation is associated with L-2-hydroxyglutaric aciduria
G260V
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the mutation is associated with L-2-hydroxyglutaric aciduria
G55D
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the mutation is associated with L-2-hydroxyglutaric aciduria
G57R
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the mutation is associated with L-2-hydroxyglutaric aciduria
H434P
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the mutation is associated with L-2-hydroxyglutaric aciduria
H98R
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the mutation is associated with L-2-hydroxyglutaric aciduria
H98Y
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the mutation is associated with L-2-hydroxyglutaric aciduria
K246N
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the mutation is associated with L-2-hydroxyglutaric aciduria
P302L
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the mutation is associated with L-2-hydroxyglutaric aciduria
P441E
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the mutation is associated with L-2-hydroxyglutaric aciduria
Q197X
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the mutation is associated with L-2-hydroxyglutaric aciduria
Q204X
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the mutation is associated with L-2-hydroxyglutaric aciduria
R251X
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the mutation is associated with L-2-hydroxyglutaric aciduria
R277X
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the mutation is associated with L-2-hydroxyglutaric aciduria
R282Q
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the mutation is associated with L-2-hydroxyglutaric aciduria
R282W
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the mutation is associated with L-2-hydroxyglutaric aciduria
R335X
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the mutation is associated with L-2-hydroxyglutaric aciduria
R70X
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the mutation is associated with L-2-hydroxyglutaric aciduria
S263L
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the mutation is associated with L-2-hydroxyglutaric aciduria
S263X
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the mutation is associated with L-2-hydroxyglutaric aciduria
S440Y
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the mutation is associated with L-2-hydroxyglutaric aciduria
V296E
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the mutation is associated with L-2-hydroxyglutaric aciduria
Y153X
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the mutation is associated with L-2-hydroxyglutaric aciduria
Y195C
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the mutation is associated with L-2-hydroxyglutaric aciduria
Y301X
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the mutation is associated with L-2-hydroxyglutaric aciduria
Y367C
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the mutation is associated with L-2-hydroxyglutaric aciduria
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine