Information on EC 1.1.5.12 - D-lactate dehydrogenase (quinone)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.5.12
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RECOMMENDED NAME
GeneOntology No.
D-lactate dehydrogenase (quinone)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-lactate + a quinone = pyruvate + a quinol
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-chloroacrylate degradation I
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D-lactate to cytochrome bo oxidase electron transfer
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methylglyoxal degradation I
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Pyruvate metabolism
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
(R)-lactate + a quinone
pyruvate + a quinol
show the reaction diagram
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?
(R)-lactate + oxidized phenazine methosulfate
pyruvate + reduced phenazine methosulfate
show the reaction diagram
(R)-lactate + phenazine methosulfate
pyruvate + reduced phenazine methosulfate
show the reaction diagram
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-
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?
(R,S)-2-hydroxybutanoate + a quinone
2-oxobutanoate + a quinol
show the reaction diagram
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12% of the activity with (R)-lactate
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?
(S)-lactate + oxidized dichlorophenolindophenol
pyruvate + reduced dichlorophenolindophenol
show the reaction diagram
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14% of the activity with (R)-lactate
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?
D-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
show the reaction diagram
D-lactate + ferricyanide
pyruvate + ferrocyanide
show the reaction diagram
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
show the reaction diagram
D-lactate + ubiquinone 1
pyruvate + reduced ubiquinone 1
show the reaction diagram
DL-2-hydroxybutanoate + 2,6-dichloroindophenol
2-oxobutanoate + reduced 2,6-dichloroindophenol
show the reaction diagram
L-lactate + 2,6-dichloroindophenol
pyruvate + reduced 2,6-dichloroindophenol
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxy-3-butynoic acid
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inactivation
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cyanide
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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
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not inhibited by 4-chloromercuribenzoate, N-ethylmaleimide, or 5,5'-dithiobis(2-nitrobenzoic acid)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
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stimulates D-lactate dehydrogenase activity at neutral pH, though it inhibits the activity at alkaline pH
Triton X-100
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5fold increase in activtiy of purified detergent-free enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 2.3
(R)-lactate
1.2
(R,S)-2-hydroxybutanoate
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pH 8.0, 23C
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18
(S)-lactate
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pH 8.0, 23C
0.5 - 1.4
D-lactate
21 - 30
L-lactate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
230
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pH 8.0, 23C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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8 - 9.5
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presence of Triton X-100
9 - 9.5
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
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sucrose density gradient centrifugation
72000
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1 * 72000, SDS-PAGE
75000
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x * 75000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 72000, SDS-PAGE
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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1 h, 35% loss of activity, more readily inactivated in presence of Triton X-100
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, detergent-free enzyme is destroyed by freezing and thawing
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-90C, 20% ethylene glycol, stable for at least 2 weeks
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0C, 5 days, 80% residual activity
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4C, stable up to 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from sonicated cell extracts, purifiaction in the presence of 1% Triton X-100 and 0.1% sodium dodecyl sulfate
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F12W
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increase in activtiy
F176W
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about 25% of wild-type vmax
F263W
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loss of activity
F279W
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loss of activity
F326W
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loss of activity
F340W
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about 35% of wild-type vmax
F361W
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activity similar to wild-type
F39W
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about 50% of wild-type vmax
F412W
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loss of activity
F435W
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about 25% of wild-type vmax
F490W
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loss of activity
F544W
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loss of activity
I152W
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loss of activity
I193W
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loss of activity
I99W
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loss of activity
L110W
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loss of activity
L203W
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loss of activity
L456W
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loss of activity
L517W
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about 50% of wild-type vmax
Y243W
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activity similar to wild-type
Y309W
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loss of activity
Y388W
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about 75% of wild-type vmax
Show AA Sequence (2334 entries)
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