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Information on EC 1.1.5.10 - D-2-hydroxyacid dehydrogenase (quinone)
for references in articles please use BRENDA:EC1.1.5.10
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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
1.1.5.10 D-2-hydroxyacid dehydrogenase (quinone)
IUBMB Comments
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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
fe-s d-ildh, nad-independent d-lactate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DLD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxyacid + a quinone = 2-oxoacid + a quinol
-
-
-
-
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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.
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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-hydroxybutyrate + ubiquinone-10
2-oxobutyrate + ubiquinol-10
Substrates: -
Products: -
Products: -
?
D-glycerate + ubiquinone-10
? + ubiquinol-10
Substrates: -
Products: -
Products: -
?
D-lactate + 2,6-dichlorophenol-indophenol
pyruvate + reduced 2,6-dichlorophenol-indophenol
-
Substrates: 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
Products: -
Products: -
?
D-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Substrates: -
Products: -
Products: -
?
D-lactate + oxidized 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
D-lactate + ubiquinone
pyruvate + ubiquinol
-
Substrates: the rate with 0.06 mM ubiquinone is 72% of the rate with 2,6-dichloroindophenol
Products: -
Products: -
?
D-lactate + ubiquinone-10
pyruvate + ubiquinol-10
Substrates: -
Products: -
Products: -
?
L-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Substrates: -
Products: -
Products: -
?
L-lactate + ubiquinone-10
pyruvate + ubiquinol-10
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme exhibits narrow substrate specificity. No activity with D-2-hydroxybutyrate, L-2-hydroxybutyrate, D-mandelate, L-mandelate, D-3-phenyllactate, D-glycerate, L-glycerate, DL-2-hydroxyisocaproate, and DL-2-hydroxyoctanoate, with 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as an electron acceptor
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
the enzyme contains an Fe-S oxidoreductase domain. The Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by the enzyme (Fe-S D-iLDH), and it helps the enzyme associate with the cell membrane
FAD
-
the purified enzyme has a spectrum typical of a flavoprotein. The change induced in the spectrum on addition of D-malate or D-lactate suggests the formation of a flavin semiquinone. Flavin can be removed by treatment with acid ammonium sulfate, and activity can be restored to the inactive apoenzyme by addition of FAD, but not of FMN or riboflavin
FAD
the enzyme contains a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain. Compared to the intact enzyme, the FAD-containing dehydrogenase domain shows increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely loses the ability to use coenzyme Q10. The FAD containing dehydrogenase domain is no longer associated with the cell membrane, and it can not support the utilization of D-lactate as a carbon source
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
antimycin A
inhibits electron transfer from quinone to cytochrome c
NaN3
inhibits electron transfer from cytochrome c to molecular oxygen
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.048
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pH 7.4, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
128
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pH 7.4, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2700
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pH 7.4, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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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
physiological function
physiological function
inactivation results in loss of the ability to grow with D-lactate. Heterologous expression in Corynebacterium efficiens enables this species to grow with D-lactate as sole carbon source
physiological function
-
inactivation results in loss of the ability to grow with D-lactate. Heterologous expression in Corynebacterium efficiens enables this species to grow with D-lactate as sole carbon source
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q88DT2_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
936
0
102629
TrEMBL
-
DLD_CORGL
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
571
0
63723
Swiss-Prot
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
95000
-
combination of gel filtration data and the sedimentation coefficient
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62
-
pH 7.3, activity decreases by 79% in 10 min, in the presence of 1 mM oxalate the decrease is 5%
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-chloride buffer, pH 8-0, in the dark, stable for several weeks
-
4°C, 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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologously expressed in Escherichia coli C43(DE3) as a His-tagged protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cammack, R.
Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase
Biochem. J.
115
55-64
1969
Oryctolagus cuniculus
brenda
Cammack, R.
Mammalian D-2-hydroxy acid dehydrogenase. Effect of inhibitors and reaction sequence
Biochem. J.
118
405-408
1970
Oryctolagus cuniculus
brenda
Kato, O.; Youn, J.; Stansen, K.; Matsui, D.; Oikawa, T.; Wendisch, V.
Quinone-dependent D-lactate dehydrogenase Dld (Cg1027) is essential for growth of Corynebacterium glutamicum on D-lactate
BMC Microbiol.
10
321
2010
Corynebacterium glutamicum (Q8NRY8), Corynebacterium glutamicum DSM 20300 (Q8NRY8)
brenda
Jiang, T.; Guo, X.; Yan, J.; Zhang, Y.; Wang, Y.; Zhang, M.; Sheng, B.; Ma, C.; Xu, P.; Gao, C.
A bacterial multidomain NAD-independent D-lactate dehydrogenase utilizes flavin adenine dinucleotide and Fe-S clusters as cofactors and quinone as an electron acceptor for D-lactate oxidization
J. Bacteriol.
199
e00342
2017
Pseudomonas putida (Q88DT2)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.5.10)
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