Any feedback?
No. of entries
Information on EC 1.1.5.12 - D-lactate dehydrogenase (quinone)
for references in articles please use BRENDA:EC1.1.5.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
1.1.5.12 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.
The enzyme appears in viruses and cellular organisms
showSynonyms
quinone-dependent d-lactate dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cg1027
DLD
-
-
-
-
quinone-dependent D-lactate dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-lactate + a quinone = pyruvate + a quinol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
2-chloroacrylate degradation I, D-lactate to cytochrome bo oxidase electron transfer, methylglyoxal degradation I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-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: -
?
(R)-lactate + coenzyme Q10
pyruvate + reduced coenzyme Q10
Substrates: -
Products: -
Products: -
?
(R)-lactate + cytochrome c
pyruvate + reduced cytochrome c
Substrates: -
Products: -
Products: -
?
(R)-lactate + phenazine methosulfate
pyruvate + reduced phenazine methosulfate
-
Substrates: -
Products: -
Products: -
?
(R,S)-2-hydroxybutanoate + a quinone
2-oxobutanoate + a quinol
-
Substrates: 12% of the activity with (R)-lactate
Products: -
Products: -
?
(S)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Substrates: poor substrate
Products: -
Products: -
?
(S)-lactate + oxidized dichlorophenolindophenol
pyruvate + reduced dichlorophenolindophenol
-
Substrates: 14% of the activity with (R)-lactate
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: poor substrate
Products: -
Products: -
?
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
(R)-lactate + oxidized phenazine methosulfate
pyruvate + reduced phenazine methosulfate
-
Substrates: -
Products: -
Products: -
?
(R)-lactate + oxidized phenazine methosulfate
pyruvate + reduced phenazine methosulfate
-
Substrates: -
Products: -
Products: -
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
D-lactate + ferricyanide
pyruvate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
D-lactate + ferricyanide
pyruvate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
D-lactate + ubiquinone 1
pyruvate + reduced ubiquinone 1
-
Substrates: -
Products: -
Products: -
?
D-lactate + ubiquinone 1
pyruvate + reduced ubiquinone 1
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxybutanoate + 2,6-dichloroindophenol
2-oxobutanoate + reduced 2,6-dichloroindophenol
-
Substrates: about 5% of the activity with D-lactate
Products: -
Products: -
?
DL-2-hydroxybutanoate + 2,6-dichloroindophenol
2-oxobutanoate + reduced 2,6-dichloroindophenol
-
Substrates: about 5% of the activity with D-lactate
Products: -
Products: -
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: about 5% of the activity with D-lactate
Products: -
Products: -
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: about 5% of the activity with D-lactate
Products: -
Products: -
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no significant reaction with D-malate, L-malate, D-tartrate and L-tartrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no significant reaction with D-malate, L-malate, D-tartrate and L-tartrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
protein is predicted to bind three [4Fe-4S] clusters and a [3Fe-4S] cluster overall
FAD
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
-
not inhibited by 4-chloromercuribenzoate, N-ethylmaleimide, or 5,5'-dithiobis(2-nitrobenzoic acid)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
-
stimulates D-lactate dehydrogenase activity at neutral pH, though it inhibits the activity at alkaline pH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.094
(R)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
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
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
1.67
D-glycerate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
(R)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
1.5
(S)-lactate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
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
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
0.78
D-glycerate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.84
(S)-lactate
isolated FAD-containing dehydrogenase domain, 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
0.47
D-glycerate
isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
-
Show AA Sequence and Transmembrane Helices (2558 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fluorine-19 nuclear magnetic resonance spectroscopy of 5-fluorotryptophan-labeled enzyme. The membrane-bound D-lactate dehydrogenase may have the two-domain structure of many cytoplasmic dehydrogenases but with the addition of a membrane-binding domain between the catalytic and cofactor-binding domains
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
1 h, 35% loss of activity, more readily inactivated in presence of Triton X-100
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from sonicated cell extracts, purifiaction in the presence of 1% Triton X-100 and 0.1% sodium dodecyl sulfate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Corynebacterium glutamicum ATCC 13032
brenda
Futai, M.
Membrane D-lactate dehydrogenase from Escherichia coli. Purification and properties
Biochemistry
12
2468-2474
1973
Escherichia coli
brenda
Pratt, E.; Fung, L.; Flower, J.; Ho, C.
Membrane-bound D-lactate dehydrogenase from Escherichia coli: Purification and properties
Biochemistry
18
312-316
1979
Escherichia coli, Escherichia coli W3110trpA33
brenda
Matsushita, K., Kaback, H.R.
D-Lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome O oxidase
Biochemistry
25
2321-2327
1986
Escherichia coli, Escherichia coli GR19N
brenda
Peersen, O.; Pratt, E.; Truong, H.; Ho, C.; Rule, G.
Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: A19F nuclear magnetic resonance study
Biochemistry
29
3256-3262
1990
Escherichia coli
brenda
Kohn, L.; Kaback, H.
Mechanisms of active transport in isolated bacterial membrane vesicles
J. Biol. Chem.
248
7012-7017
1973
Escherichia coli, Escherichia coli ML 308-225
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 KT2440 (Q88DT2)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.5.12)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
