Information on EC 1.1.5.10 - D-2-hydroxyacid dehydrogenase (quinone)

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

EC NUMBER
COMMENTARY hide
1.1.5.10
-
RECOMMENDED NAME
GeneOntology No.
D-2-hydroxyacid dehydrogenase (quinone)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxyacid + a quinone = 2-oxoacid + a quinol
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxyacid:quinone oxidoreductase
The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-lactate + 2,6-dichlorophenol-indophenol
pyruvate + reduced 2,6-dichlorophenol-indophenol
show the reaction diagram
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ordered mechanism, first D-lactate and then 2,6-dichlorophenol-indophenol bind to the enzyme to form a ternary complex, from which pyruvate and reduced 2,6-dichlorophenol-indophenol dissociate in that oder
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?
D-lactate + oxidized 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
show the reaction diagram
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-
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?
D-lactate + ubiquinone
pyruvate + ubiquinol
show the reaction diagram
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the rate with 0.06 mM ubiquinone is 72% of the rate with 2,6-dichloroindophenol
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxalate
oxaloacetate
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95000
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combination of gel filtration data and the sedimentation coefficient
102000
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gel filtration
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
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20C, 30 min, stable above pH 10.5 or below pH 4.8
724205
5.5 - 10
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20C, 30 min, stable
724205
7.3
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unstable above 55C
724205
10.5
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20C, 30 min, stable above pH 10.5 or below pH 4.8
724205
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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pH 5.5-10, 30 min, stable
62
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pH 7.3, activity decreases by 79% in 10 min, in the presence of 1 mM oxalate the decrease is 5%
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 50 mM Tris-chloride buffer, pH 8-0, in the dark, stable for several weeks
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4C, as a precipitate in 32% (w/v) ammonium sulfate solution in 50 mM Tris-chloride buffer, pH 8.0, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli