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Information on EC 1.1.5.12 - D-lactate dehydrogenase (quinone)
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1.1.5.12 D-lactate dehydrogenase (quinone)IUBMB Comments
The enzyme is an FAD-dependent peripheral membrane dehydrogenase that participates in respiration. Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool.
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The enzyme appears in viruses and cellular organisms
Synonyms
quinone-dependent d-lactate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cg1027
DLD
-
-
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-
pp4737
quinone-dependent D-lactate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-lactate + a quinone = pyruvate + a quinol
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SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:quinone 2-oxidoreductase
The enzyme is an FAD-dependent peripheral membrane dehydrogenase that participates in respiration. Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c
quinone is the preferred electron acceptor of the enzyme
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-
?
(R)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + ?
quinone is the preferred electron acceptor of the enzyme
-
-
?
(R)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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-
-
?
(R)-lactate + cytochrome c
pyruvate + reduced cytochrome c
-
-
-
?
(R)-lactate + phenazine methosulfate
pyruvate + reduced phenazine methosulfate
-
-
-
-
?
(R,S)-2-hydroxybutanoate + a quinone
2-oxobutanoate + a quinol
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12% of the activity with (R)-lactate
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-
?
(S)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + ?
quinone is the preferred electron acceptor of the enzyme
-
-
?
(S)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
poor substrate
-
-
?
(S)-lactate + oxidized dichlorophenolindophenol
pyruvate + reduced dichlorophenolindophenol
-
14% of the activity with (R)-lactate
-
-
?
D-2-hydroxybutanoate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
2-oxobutanoate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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-
-
?
D-2-hydroxybutyrate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
2-oxobutanoate + ?
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-
-
?
D-2-hydroxybutyrate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
? + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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-
-
?
D-glycerate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
?
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-
-
?
D-glycerate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
? + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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-
-
?
D-glycerate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
D-glyceraldehyde + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
poor substrate
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-
?
D-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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-
-
?
D-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
DL-2-hydroxybutanoate + 2,6-dichloroindophenol
2-oxobutanoate + reduced 2,6-dichloroindophenol
L-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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-
-
?
(R)-lactate + coenzyme Q10
pyruvate + reduced coenzyme Q10
quinone is the preferred electron acceptor of the enzyme
-
-
?
(R)-lactate + coenzyme Q10
pyruvate + reduced coenzyme Q10
-
-
-
?
(R)-lactate + oxidized phenazine methosulfate
pyruvate + reduced phenazine methosulfate
-
-
-
-
?
(R)-lactate + oxidized phenazine methosulfate
pyruvate + reduced phenazine methosulfate
-
-
-
-
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
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-
-
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?
D-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
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-
-
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?
D-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
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-
-
-
?
DL-2-hydroxybutanoate + 2,6-dichloroindophenol
2-oxobutanoate + reduced 2,6-dichloroindophenol
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about 5% of the activity with D-lactate
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-
?
DL-2-hydroxybutanoate + 2,6-dichloroindophenol
2-oxobutanoate + reduced 2,6-dichloroindophenol
-
about 5% of the activity with D-lactate
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-
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
about 5% of the activity with D-lactate
-
-
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
about 5% of the activity with D-lactate
-
-
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
-
-
-
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
-
-
-
?
additional information
?
-
-
no significant reaction with D-malate, L-malate, D-tartrate and L-tartrate
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-
?
additional information
?
-
-
no significant reaction with D-malate, L-malate, D-tartrate and L-tartrate
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?
additional information
?
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not active with D-glycerate, L-glycerate, succinate, malate, D-tartrate, L-tartrate, meso-tartrate, 1-propanol, or isopropanol as substrates and oxidized diphosphopyridine nucleotide has no effect on the catalytic conversion of D-lactate to pyruvate
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?
additional information
?
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not active with D-glycerate, L-glycerate, succinate, malate, D-tartrate, L-tartrate, meso-tartrate, 1-propanol, or isopropanol as substrates and oxidized diphosphopyridine nucleotide has no effect on the catalytic conversion of D-lactate to pyruvate
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-
?
additional information
?
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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
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-
additional information
?
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quinone is the preferred electron acceptor of the enzyme. No substrates: glycolate, L-2-hydroxybutyrate, D-mandelate, L-mandelate, D-3-phenyllactate, L-glycerate, DL-2-hydroxyisocaproate, and DL-2-hydroxyoctanoate
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S cluster
the enzyme contains an Fe-S oxidoreductase domain that functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor. It helps the enzyme to associate with the cell membrane
FAD
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visible absorption spectrum of the purified enzyme shows a broad peak at around 450 nm and a shoulder at around 480 nm
FAD
the ratio of Fe-S D-iLDH to FAD is 0.92. Compared to the intact enzyme, the FAD-containing dehydrogenase domain shows increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely lost the ability to use coenzyme Q10. The isolated 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
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
Fe-S center
protein is predicted to bind three [4Fe-4S] clusters and a [3Fe-4S] cluster overall
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
antimycin A
inhibits electron transfer from quinone to cytochrome c
Ba2+
5 mM, partial inhibition; 5 mM, partial inhibition of activity
Ca2+
5 mM, partial inhibition; 5 mM, partial inhibition of activity
cyanide
-
stimulates D-lactate dehydrogenase activity at neutral pH, though it inhibits the activity at alkaline pH. At 1.5 mM, 50% inhibition at pH 9.3
Mg2+
5 mM, partial inhibition; 5 mM, partial inhibition of activity
NaN3
inhibits electron transfer from cytochrome c to molecular oxygen
Ni2+
5 mM, partial inhibition; 5 mM, partial inhibition of activity
additional information
-
not inhibited by 4-chloromercuribenzoate, N-ethylmaleimide, or 5,5'-dithiobis(2-nitrobenzoic acid)
-
Cd2+
5 mM, complete inhibition; 5 mM, complete inhibition of activity
Co2+
5 mM, complete inhibition; 5 mM, complete inhibition of activity
Cu2+
5 mM, complete inhibition; 5 mM, complete inhibition of activity
EDTA
5 mM, partial inhibition; 5 mM, partial inhibition of activity
Fe2+
5 mM, complete inhibition; 5 mM, complete inhibition of activity
Mn2+
5 mM, complete inhibition; 5 mM, complete inhibition of activity
Zn2+
5 mM, complete inhibition; 5 mM, complete inhibition of activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
-
stimulates D-lactate dehydrogenase activity at neutral pH, though it inhibits the activity at alkaline pH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
(R)-lactate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
0.094
(R)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
1.04
(S)-lactate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
1.78
(S)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
0.031
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C
0.048
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pH 7.4, 30°C
0.048
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
cosubstrate (R)-lactate, pH 7.4, 30°C
0.0095
cytochrome c
cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C
0.17
D-2-hydroxybutanoate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
0.1
D-2-hydroxybutyrate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
1.38
D-glycerate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
1.67
D-glycerate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
(R)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
120
(R)-lactate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
1.5
(S)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
9.5
(S)-lactate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
5.3
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C
128
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pH 7.4, 30°C
128
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
cosubstrate (R)-lactate, pH 7.4, 30°C
2
cytochrome c
cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C
13
D-2-hydroxybutanoate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
66
D-2-hydroxybutyrate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
0.78
D-glycerate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
8
D-glycerate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
176
(R)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
2100
(R)-lactate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
0.84
(S)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
9
(S)-lactate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
2.7
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pH 7.4, 30°C
170
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C
2700
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
cosubstrate (R)-lactate, pH 7.4, 30°C
210
cytochrome c
cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C
78
D-2-hydroxybutanoate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
660
D-2-hydroxybutyrate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
0.47
D-glycerate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
6
D-glycerate
pH 7.4, 30°C, acceptor: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the isolated FAD-containing dehydrogenase domain retains 2-hydroxyacid-oxidizing activity, although it decreased compared to the full Fe-S D-iLDH. Compared to the intact enzyme, the FAD-containing dehydrogenase domain shows increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely lost the ability to use coenzyme Q10. The Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by Fe-S D-iLDH, and it helps the enzyme associate with the cell membrane
physiological function
physiological function
-
D-lactate/ubiquinone 1 or D-lactate/ferricyanide oxidoreductase activity does not generate a membranepotential, suggesting that electron flow from D-lactate dehydrogenase to ubiquinone is not electrogenic. Proteoliposomes reconstituted with purified D-lactate dehydrogenase, ubiquinone 8, and purified cytochrome o catalyze D-lactate and ubiquinol 1 oxidation and generate a H+ electrochemical gradient similar to that observed in membrane vesicles. The only component between D-lactate dehydrogenase or ubiquinol and oxygen in the membranes that is directly involved in the generation of the H+ electrochemical gradient is cytochrome 0
physiological function
-
inactivation of Dld results in the 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 of Dld results in the 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
-
D-lactate/ubiquinone 1 or D-lactate/ferricyanide oxidoreductase activity does not generate a membranepotential, suggesting that electron flow from D-lactate dehydrogenase to ubiquinone is not electrogenic. Proteoliposomes reconstituted with purified D-lactate dehydrogenase, ubiquinone 8, and purified cytochrome o catalyze D-lactate and ubiquinol 1 oxidation and generate a H+ electrochemical gradient similar to that observed in membrane vesicles. The only component between D-lactate dehydrogenase or ubiquinol and oxygen in the membranes that is directly involved in the generation of the H+ electrochemical gradient is cytochrome 0
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
118000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer