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Information on EC 1.1.99.6 - D-lactate dehydrogenase (acceptor)
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1.1.99.6 D-lactate dehydrogenase (acceptor)IUBMB Comments
The zinc flavoprotein (FAD) from the archaeon Archaeoglobus fulgidus cannot utilize NAD+, cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.
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Word Map
- 1.1.99.6
-
l-2-hydroxy
- dl-methionine
- archaeon
-
hyperthermophilic
-
archaeoglobus
-
dl-met
- fulgidus
- fad
- tokodaii
- subterraneum
-
candidatus
- flavin
-
tracer
-
sulfolobus
-
aeropyrum
- pernix
- dihydrolipoamide
-
l-isomer
- analysis
- diagnostics
- synthesis
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
dye-dldh, dye-linked d-lactate dehydrogenase, d-2-hydroxy acid dehydrogenase, dld enzyme, af0394, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
APE_0487
D-2-hydroxy acid dehydrogenase
-
-
-
-
dehydrogenase, D-2-hydroxy acid
-
-
-
-
dye-DLDH
dye-linked D-lactate dehydrogenase
ST0649
TTX_0794
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-lactate + acceptor = pyruvate + reduced acceptor
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:acceptor 2-oxidoreductase
The zinc flavoprotein (FAD) from the archaeon Archaeoglobus fulgidus cannot utilize NAD+, cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.
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CAS REGISTRY NUMBER
COMMENTARY
9028-83-5
-
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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)-2-hydroxybutanoate + 2,6-dichlorophenolindophenol
2-oxobutanoate + reduced 2,6-dichlorophenolindophenol
preferred substrate
-
-
?
(R)-2-hydroxybutyrate + oxidized 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
(R)-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
preferred substrate
-
-
?
(R)-lactate + ferricyanide
pyruvate + ferrocyanide + H+
-
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
-
-
-
?
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
2(R)-hydroxybutanoate + acceptor
2-oxobutanoate + reduced acceptor
-
-
-
?
2(R)-hydroxyheptanoate + acceptor
2-oxoheptanoate + reduced acceptor
-
-
-
?
2(R)-hydroxyhexanoate + acceptor
2-oxohexanoate + reduced acceptor
-
-
-
?
2(R)-hydroxyoctanoate + acceptor
2-oxooctanoate + reduced acceptor
-
-
-
?
2(R)-hydroxypentanoate + acceptor
2-oxopentanoate + reduced acceptor
-
-
-
?
D-glycerate + acceptor
hydroxypyruvate + reduced acceptor
-
-
-
?
D-lactate + 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
D-lactate + phenazine methosulfate p-iodonitrotetrazolium
pyruvate + reduced phenazine methosulfate p-iodonitrotetrazolium
-
-
-
?
D-tartrate + acceptor
2-oxo-3-hydroxybutanoate + reduced acceptor
-
poor substrate
-
?
meso-tartrate + acceptor
2-oxo-3-hydroxybutanoate + reduced acceptor
-
good substrate
-
?
phenylpyruvate + reduced acceptor
phenyl-(R)-lactate + acceptor
-
-
-
r
(R)-2-hydroxybutyrate + oxidized 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
relative activity is 46% compared to D-lactate
-
-
?
(R)-2-hydroxybutyrate + oxidized 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
97% of the activity compared to (R)-lactate
-
-
?
(R)-2-hydroxybutyrate + oxidized 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
97% of the activity compared to (R)-lactate
-
-
?
(R)-lactate + 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + ?
-
-
-
?
(R)-lactate + 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + ?
Aeropyrum pernix ATCC 700893
-
-
-
?
(R)-lactate + 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + ?
-
-
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
-
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
cytochrome c, ubiquinone and O2 are possible physiological acceptors
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
no activity with glycolate, 3-methylpentanoate, phenylglycolate, phenyllactate, 3-phosphoglycerate, 6-phosphoglycerate
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
enzyme acts on a variety of (R)-2-hydroxy acids
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
enzyme acts on a variety of (R)-2-hydroxy acids
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
cytochrome c, ubiquinone and O2 are possible physiological electron acceptors
-
?
(R)-lactate + ferricyanide
pyruvate + ferrocyanide
ferricyanide is the preferred electron acceptor
-
-
?
(R)-lactate + ferricyanide
pyruvate + ferrocyanide
ferricyanide is the preferred electron acceptor
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
Aeropyrum pernix ATCC 700893
-
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
no activity with L-lactate
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
(R)-lactate is the most preferred substrate, followed by (R)-2-hydroxybutyrate. D-Alanine, pyruvate, D-glucose, L-alanine, ethanol and L-lactate are inert as electron donors. Benzyl viologen and methylene blue are inert as electron acceptors
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
activity is 59% compared to the activity with ferricyanide
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
activity is 59% compared to the activity with ferricyanide
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
Thermoproteus tenax ATCC 35583
-
-
-
?
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
-
-
-
?
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
activity is 29% compared to the activity with ferricyanide
-
-
?
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
activity is 29% compared to the activity with ferricyanide
-
-
?
(R)-lactate + phenazine methosulfate p-iodonitrotetrazolium
pyruvate + ?
-
-
-
?
(R)-lactate + phenazine methosulfate p-iodonitrotetrazolium
pyruvate + ?
Aeropyrum pernix ATCC 700893
-
-
-
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
-
-
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
Thermoproteus tenax ATCC 35583
-
-
-
?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
-
-
-
?
D-lactate + 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
-
-
-
?
D-lactate + 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
Thermoproteus tenax ATCC 35583
-
-
-
?
D-lactate + 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
-
-
-
?
additional information
?
-
D-glycerate, D-alanine, D-leucine, 2-hydroxyisobutyrate, L-lactate, L-alanine, and L-leucine are inert as the electron donor. Ferricyanide, benzyl viologen, and methylene blue are inert as electron acceptors
-
-
-
additional information
?
-
-
D-glycerate, D-alanine, D-leucine, 2-hydroxyisobutyrate, L-lactate, L-alanine, and L-leucine are inert as the electron donor. Ferricyanide, benzyl viologen, and methylene blue are inert as electron acceptors
-
-
-
additional information
?
-
Aeropyrum pernix ATCC 700893
D-glycerate, D-alanine, D-leucine, 2-hydroxyisobutyrate, L-lactate, L-alanine, and L-leucine are inert as the electron donor. Ferricyanide, benzyl viologen, and methylene blue are inert as electron acceptors
-
-
-
additional information
?
-
the enzyme is expressed constitutively
-
-
?
additional information
?
-
methylene blue, dimethylnaphthoquinone, NAD+, and horse heart cytochrome c do not serve as electron acceptors for the purified enzyme
-
-
?
additional information
?
-
-
methylene blue, dimethylnaphthoquinone, NAD+, and horse heart cytochrome c do not serve as electron acceptors for the purified enzyme
-
-
?
additional information
?
-
no substrates: D-alanine, pyruvate, D-glucose, L-alanine, ethanol and L-lactate
-
-
-
additional information
?
-
-
no substrates: D-alanine, pyruvate, D-glucose, L-alanine, ethanol and L-lactate
-
-
-
additional information
?
-
L-lactate, glycolate, L-tartrate, citrate, glyoxylate, 2-hydroxyisobutyrate, D-glycerate and D-2-phosphoglycerate are inert as electron donors. Benzyl viologen and methylene blue are inert as electron acceptors
-
-
?
additional information
?
-
-
L-lactate, glycolate, L-tartrate, citrate, glyoxylate, 2-hydroxyisobutyrate, D-glycerate and D-2-phosphoglycerate are inert as electron donors. Benzyl viologen and methylene blue are inert as electron acceptors
-
-
?
additional information
?
-
L-lactate, glycolate, L-tartrate, citrate, glyoxylate, 2-hydroxyisobutyrate, D-glycerate and D-2-phosphoglycerate are inert as electron donors. Benzyl viologen and methylene blue are inert as electron acceptors
-
-
?
additional information
?
-
no acceptors: ferricyanide, benzyl viologen, and methylene blue
-
-
-
additional information
?
-
-
no acceptors: ferricyanide, benzyl viologen, and methylene blue
-
-
-
additional information
?
-
D-glycerate, D-alanine, D-leucine, 2-hydroxyisobutyrate, L-lactate, L-alanine, and L-leucine are inert as the electron donor. Ferricyanide, benzyl viologen, and methylene blue are inert as electron acceptors
-
-
-
additional information
?
-
-
D-glycerate, D-alanine, D-leucine, 2-hydroxyisobutyrate, L-lactate, L-alanine, and L-leucine are inert as the electron donor. Ferricyanide, benzyl viologen, and methylene blue are inert as electron acceptors
-
-
-
additional information
?
-
Thermoproteus tenax ATCC 35583
no acceptors: ferricyanide, benzyl viologen, and methylene blue
-
-
-
additional information
?
-
Thermoproteus tenax ATCC 35583
D-glycerate, D-alanine, D-leucine, 2-hydroxyisobutyrate, L-lactate, L-alanine, and L-leucine are inert as the electron donor. Ferricyanide, benzyl viologen, and methylene blue are inert as electron acceptors
-
-
-
additional information
?
-
no acceptors: ferricyanide, benzyl viologen, and methylene blue
-
-
-
additional information
?
-
D-glycerate, D-alanine, D-leucine, 2-hydroxyisobutyrate, L-lactate, L-alanine, and L-leucine are inert as the electron donor. Ferricyanide, benzyl viologen, and methylene blue are inert as electron acceptors
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
the enzyme is expressed constitutively
-
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
-
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
enzyme acts on a variety of (R)-2-hydroxy acids
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
enzyme acts on a variety of (R)-2-hydroxy acids
-
?
(R)-lactate + acceptor
pyruvate + reduced acceptor
-
cytochrome c, ubiquinone and O2 are possible physiological electron acceptors
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
molybenum-containing Fe-S-enzyme without an additional prosthetic group such as flavin or cytochrome c, enzyme contains one molybdenum, four iron and four sulfur atoms per subunit
-
FAD
-
flavoprotein, 2 molecules per molecule of enzyme, not replaceable by FMN or riboflavin
FAD
flavoprotein. FAD binds to apoprotein with a 1:1 stoichiometry and is essential for activity. Although the cofactor is tightly associated with the enzyme, it is not covalently attached
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCN
-
raises dehydrogenase activity of freshly prepared kidney extracts
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
inactivation during preincubation at 0°C; progressive inactivation, substrate decreases rate of inactivation
EDTA
-
progressive inactivation, substrate decreases rate of inactivation
oxalate
1 mM, addition of Tris buffered oxalate to a reaction mixture inhibits activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
stimulates
additional information
-
ageing of extracts increases dehydrogenase activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hyperglycemia
Dihydrolipoamide dehydrogenase suppression induces human tau phosphorylation by increasing whole body glucose levels in a C. elegans model of Alzheimer's Disease.
Kidney Failure, Chronic
D-lactate metabolism in patients with chronic renal failure undergoing CAPD.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.247
oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
pH 8.5, 60°C, cosubstrate: (R)-lactate
0.091
(R)-lactate
pH 8.5, 60°C, cosubstrate: 2,6-dichlorophenolindophenol
0.156
(R)-lactate
pH 8.5, 60°C, cosubstrate: 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide
0.605
(R)-lactate
pH 7.0, 60°C, electron acceptor: oxidized 2,6-dichlorophenolindophenol
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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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
pH 6.5: about 50% of maximal activity, pH 9.0: about 50% of maximal activity
7 - 9.5
pH 7.0: about 30% of maximal activit, pH 9.5: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
60
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 95
25°C: 8% of maximal activity, 95°C: about 75% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
brenda
-
ubiquitously expressed in heart, brain, placenta, lung, skeletal muscle, kidney, pancreas and colon, highest expression in liver
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
more than 85% of the enzyme is associated with the membrane, integral membrane protein, a significant portion including part of the FAD-binding pocket, is outside the membrane facing the S-layer. NADH oxidase (NoxA2) co-localized to the same sites in the membrane (NoxA2) may protect proteins involved in electron transfer by reducing O2 to H2O2 or H2O
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
mutations in the D2HGDH gene, encoding D-2-hydroxyglutarate dehydrogenase, cause D-2-hydroxyglutaric aciduria
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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). DLD_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
443
0
48487
Swiss-Prot
-
D8IY89_HERSS
Herbaspirillum seropedicae (strain SmR1)
348
0
37385
TrEMBL
-
D8IRZ7_HERSS
Herbaspirillum seropedicae (strain SmR1)
316
0
33575
TrEMBL
-
A0A811TF41_9EURY
468
0
52925
TrEMBL
-
Q6MY49_ASPFM
335
0
36534
TrEMBL
other Location (Reliability: 3)
G4RPF4_THETK
Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
448
0
48716
TrEMBL
-
Q974L0_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
440
0
49748
TrEMBL
-
Q9YEU4_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
473
0
51843
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method with polyethylene glycol 8000 as the precipitant. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 63.4, b = 119.4, c = 70.2 A, beta = 112.0°, and diffract to 2.0 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
4 - 11
the enzyme retains more than 70% activity after incubation at 50°C for 30 min
761053
4 - 11
the enzyme retains more than 70% activity after incubation at 50°C for 30 min
761053
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
80
70
retains full activity after incubation for 10 min at 70°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen-sensitive enzyme, has to be handled in the presence of detergent and absence of oxygen, if stirred under air at room temperatures 50% activity are lost within 30 min, the residual activity has a half-life of 10 h
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287841
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as part of a fusion protein with maltose-binding protein in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli, gene is localized on chromosome 9q between marker WI-3028 and WI-93330
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
D-lactate content is of great interest for clinical diagnosis. A D-lactate sensing system using a thermostable dye-linked D-lactate dehydrogenase (Dye-DLDH) is developed. The electrode for detection of D-lactate is prepared by immobilizing the thermostable Dye-DLDH and multi-walled carbon nanotube (MWCNT) within Nafion membrane. The electrocatalytic response of the electrode is clearly observed upon exposure to D-lactate. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days
analysis
construction of a D-Lactate electrochemical biosensor. The electrode for detection of D-lactate is prepared by immobilizing dye-linked D-LDH and multi-walled carbon nanotube within Nafion membrane. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days
analysis
D-lactate content is of great interest for food analysis. A D-lactate sensing system using a thermostable dye-linked D-lactate dehydrogenase (Dye-DLDH) is developed. The electrode for detection of D-lactate is prepared by immobilizing the thermostable Dye-DLDH and multi-walled carbon nanotube (MWCNT) within Nafion membrane. The electrocatalytic response of the electrode is clearly observed upon exposure to D-lactate. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tubbs, P.K.; Greville, G.D.
Dehydrogenation of D-lactate by a soluble enzyme from kidney mitochondria
Biochim. Biophys. Acta
34
290-291
1959
Oryctolagus cuniculus
brenda
Cammack, R.
D-2-hydroxy acid dehydrogenase from animal tissue
Methods Enzymol.
41
323-329
1975
Oryctolagus cuniculus
brenda
Trautwein, T.; Krauss, F.; Lottspeich, F.; Simon, H.
The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein
Eur. J. Biochem.
222
1025-1032
1994
Proteus vulgaris
brenda
Hekmat, D.; Danninger, J.; Simon, H.; Vortmeyer, D.
Production of pyruvate from (R)-lactate in an enzyme-membrane reactor with coupled electrochemical regeneration of the artificial mediator anthraquinone-2,6-disulfonate
Enzyme Microb. Technol.
24
471-479
1999
Proteus vulgaris
-
brenda
Huang, T.; Yang, W.; Pereira, A.C.; Craigen, W.J.; Shih, V.E.
Cloning and characterization of a putative human D-2-hydroxyacid dehydrogenase in chromosome 9q
Biochem. Biophys. Res. Commun.
268
298-301
2000
Homo sapiens
brenda
Satomura, T.; Kawakami, R.; Sakuraba, H.; Ohshima, T.
A novel flavin adenine dinucleotide (FAD) containing D-lactate dehydrogenase from the thermoacidophilic crenarchaeota Sulfolobus tokodaii strain 7: purification, characterization and expression in Escherichia coli
J. Biosci. Bioeng.
106
16-21
2008
Sulfurisphaera tokodaii (Q974L0), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q974L0)
brenda
Shibahara, T.; Satomura, T.; Kawakami, R.; Ohshima, T.; Sakuraba, H.
Crystallization and preliminary X-ray analysis of a dye-linked D-lactate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix
Acta Crystallogr. Sect. F
67
1425-1427
2011
Aeropyrum pernix (Q9YEU4), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9YEU4)
brenda
Pagala, V.R.; Park, J.; Reed, D.W.; Hartzell, P.L.
Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus
Archaea
1
95-104
2002
Archaeoglobus fulgidus (O29853)
brenda
Reed, D.W.; Hartzell, P.L.
The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn2+ flavoprotein
J. Bacteriol.
181
7580-7587
1999
Archaeoglobus fulgidus (O29853), Archaeoglobus fulgidus
brenda
Satomura, T.; Hayashi, J.; Ohshida, T.; Sakuraba, H.; Ohshima, T.; Suye, S.I.
Enzymological characteristics of a novel archaeal dye-linked D-lactate dehydrogenase showing loose binding of FAD
Extremophiles
22
975-981
2018
Thermoproteus tenax (G4RPF4), Thermoproteus tenax, Aeropyrum pernix (Q9YEU4), Aeropyrum pernix, Aeropyrum pernix ATCC 700893 (Q9YEU4), Thermoproteus tenax DSM 2078 (G4RPF4), Thermoproteus tenax ATCC 35583 (G4RPF4)
brenda
Satomura, T.; Hayashi, J.; Sakamoto, H.; Nunoura, T.; Takaki, Y.; Takai, K.; Takami, H.; Ohshima, T.; Sakuraba, H.; Suye, S.I.
D-Lactate electrochemical biosensor prepared by immobilization of thermostabledye-linked D-lactate dehydrogenase from Candidatus Caldiarchaeum subterraneum
J. Biosci. Bioeng.
126
425-430
2018
Candidatus Caldarchaeum subterraneum (E6N788), Candidatus Caldarchaeum subterraneum
brenda
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