Information on EC 1.1.2.4 - D-lactate dehydrogenase (cytochrome)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.2.4
-
RECOMMENDED NAME
GeneOntology No.
D-lactate dehydrogenase (cytochrome)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
methylglyoxal degradation VI
-
Pyruvate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:ferricytochrome-c 2-oxidoreductase
A flavoprotein (FAD).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cytochrome-dependent D-(-)-lactate dehydrogenase
-
-
-
-
D(-)-lactic cytochrome c reductase
-
-
-
-
D-lactate cytochrome c oxidoreductase
Q94AX4
-
D-lactate cytochrome c oxidoreductase
-
-
D-lactate ferricytochrome c oxidoreductase
-
-
-
-
D-lactate-cytochrome c reductase
-
-
-
-
D-LCR
-
-
-
-
D-LDH
Q94AX4
-
lactic acid dehydrogenase
-
-
-
-
NAD+-independent LDH
-
-
CAS REGISTRY NUMBER
COMMENTARY
37250-79-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Jerusalem artichoke
-
-
Manually annotated by BRENDA team
No. 7, growth photoanaerobically on lactate
-
-
Manually annotated by BRENDA team
different strains and mutants
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Q94AX4
participates in the methylglyoxal pathway
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
ir
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
required for growth on lactate as sole carbon source
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
pathway linked to respiratory chain
-
?
(R)-lactate + ferricyanide
pyruvate + ferrocyanide
show the reaction diagram
-
-
-
-
?
(R)-lactate + ferricyanide
pyruvate + ferrocyanide
show the reaction diagram
-
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
traces of activity with L-isomer
-
?
(R)-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
specific for D-isomer
-
ir
D-2-hydroxybutyrate + cytochrome c
2-oxobutanoate + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
D-2-hydroxybutyrate + cytochrome c
2-oxobutanoate + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
D-2-hydroxybutyrate + cytochrome c
2-oxobutanoate + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
D-2-hydroxybutyrate + cytochrome c
2-oxobutanoate + ferrocytochrome c
show the reaction diagram
-
reversible under anaerobic conditions
-
-
r
D-2-hydroxybutyrate + ferricytochrome c
?
show the reaction diagram
Q94AX4
135% relative activity compared to (R)lactate, highest catalytic efficiency, prefered substrate
-
-
?
D-2-hydroxyglutarate + ferricytochrome c
?
show the reaction diagram
Q94AX4
0.15% relative activity compared to (R)lactate
-
-
?
D-2-hydroxyvalerate + cytochrome c
2-oxovalerate + ferrocytochrome c
show the reaction diagram
-
very poor substrate
-
-
?
D-glycerate + ferricytochrome c
?
show the reaction diagram
Q94AX4
9.2% relative activity compared to (R)lactate
-
-
?
D-lactate + 2 ferricytochrome
pyruvate + 2 ferrocytochrome
show the reaction diagram
-
-
-
-
?
D-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c
show the reaction diagram
Q94AX4
100% relative activity, prefered substrate, with a high catalytic efficiency 200- and 2000fold higher than that for L-lactate and glycolate, respectively
-
-
?
D-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c
show the reaction diagram
-
substrate specific for D-LCR. D-LCR is efficient enough in transferring electrons from D-lactate to the next mediators
-
-
?
D-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
i.e. DCPIP, via cofactor FAD, stereospecific enzyme
-
-
?
D-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
i.e. DCPIP, via cofactors FMN or FAD
-
-
?
D-lactate + cytochrome c2ox
pyruvate + cytochrome c2red
show the reaction diagram
-
-
-
-
?
D-lactate + ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
DL-2-hydroxybutyrate + ferricytochrome c
2-oxobutanoate + ferrocytochrome c
show the reaction diagram
-
40% of the activity with (R)-lactate
-
-
?
DL-glycerate + ferricyanide
?
show the reaction diagram
-
10% of the rate of D-lactate oxidation
-
-
-
DL-glycerate + ferricytochrome c
?
show the reaction diagram
Q94AX4
10.3% relative activity compared to (R)lactate
-
-
?
glycolate + ferricytochrome c
?
show the reaction diagram
Q94AX4
0.15% relative activity compared to (R)lactate, O2 does not function as the acceptor for glycolate electrons
-
-
?
L-lactate + ferricytochrome c
?
show the reaction diagram
Q94AX4
10.8% relative activity compared to (R)lactate
-
-
?
additional information
?
-
-
study of the D-lactate transport and metabolism in Helianthus tuberosus, overview
-
-
-
additional information
?
-
Q94AX4
no activity with propionate, acetate, glutarate, DL-3-hydroxybutyrate and 4-hydroxybutyrate
-
-
-
additional information
?
-
-
no cross-reactivity with L-lactic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
-
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
ir
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
-
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
required for growth on lactate as sole carbon source
-
?
(R)-lactate + 2 ferricytochrome c
pyruvate + ferrocytochrome c
show the reaction diagram
-
pathway linked to respiratory chain
-
?
additional information
?
-
-
study of the D-lactate transport and metabolism in Helianthus tuberosus, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
can substitute for cytochrome c
2,6-dichlorophenolindophenol
-
can substitute for cytochrome c
2,6-dichlorophenolindophenol
-
can substitute for cytochrome c
cytochrome c
-
cytochome c from horse-, beef- and tuna-heart more active than yeast cytochome c
cytochrome c
-
highly specific
cytochrome c
-
only cytochrome c-553 from same organism, eucaryotic cytochromes are not reduced
FAD
-
1 FAD per subunit
FAD
-
bound to the FAD binding domain of the enzyme
phenazine methosulfate
-
can substitute for cytochrome c
phenazine methosulfate
-
can substitute for cytochrome c
additional information
-
no activity with NAD+ or NADP+
-
additional information
-
no activity with NAD+ or NADP+
-
additional information
Q94AX4
no activity with NAD+ or NADP+ as electron acceptors
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
inhibitory
Co2+
-
restores activity after inhibition with o-phenanthroline
Cu2+
-
rapid inactivation, can be restored by addition of dithiothreitol
Fe2+
-
restores activity after inhibition with o-phenanthroline
ferricyanide
-
not suitable as electron acceptor
ferricyanide
-
can substitute for cytochrome c
ferricyanide
-
can substitute for cytochrome c
Mg2+
-
inhibitory
Mn2+
-
restores activity after inhibition with o-phenanthroline
Zn2+
-
very tightly bound to enzyme
Zn2+
-
restores activity after inhibition with o-phenanthroline
Zn2+
-
required for activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-hydroxybutanoate
-
irreversible inactivation, modification of FAD
2-oxobutanoate
-
inactivation under anaerobic conditions
DL-gycerate
-
strong inhibition
-
EDTA
-
no inhibitor
High ionic strength
-
-
-
o-phenanthroline
-
very strong
o-phenanthroline
-
very strong, reactivation with Zn2+ and Co2+
o-phenanthroline
-
very strong
oxalate
-
competitive
oxaloacetate
-
competitive
p-chloromercuribenzoate
-
weak
p-Mercuriphenylsulfonate
-
-
phenylsuccinate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
carboxylic acid
-
activates, stimulation is non-competitive, hyperbolic and its dimension is directly related to the number of carboxylic groups on the activator. Stimulation does not affect the yield of oxidative phosphorylation
D-lactate
-
stimulation with D-lactate as substrate, is insensitive to malate or pyruvate addition
EDTA
-
slightly stimulating
L-Malate
-
non-competitive activation
additional information
-
growth on lactate and ethanol yields much higher activities than grows on glucose
-
additional information
-
the enzyme is induced by lacate as sole carbon source during growth
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.264
-
(R)-lactate
-
30C, pH 7.5
0.0054
-
cytochrome c
-
-
0.0054
-
cytochrome c
-
from horse heart
0.061
-
D-2-hydroxybutyrate
Q94AX4
-
1.34
-
D-2-hydroxybutyrate
-
-
1.4
-
D-2-hydroxybutyrate
-
-
2.5
-
D-2-hydroxyvalerate
-
-
8.871
-
D-glycerate
Q94AX4
-
0.0026
-
D-lactate
-
-
0.013
-
D-lactate
-
with ferricyanide
0.055
-
D-lactate
-
-
0.164
-
D-lactate
Q94AX4
-
0.8
-
D-lactate
-
-
0.8
-
D-lactate
-
pH 8.0, 30C
5
-
D-lactate
-
pH 7.0, 25C
26
-
D-lactate
-
with complete electron transport system
0.23
-
ferricyanide
-
-
0.432
-
glycolate
Q94AX4
-
4.45
-
phenazine methosulfate
-
-
4.486
-
L-lactate
Q94AX4
-
additional information
-
additional information
-
kinetics of D-lactate metabolism, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.467
-
D-2-hydroxybutyrate
Q94AX4
-
0.1
-
D-glycerate
Q94AX4
-
1.083
-
D-lactate
Q94AX4
-
250
-
D-lactate
-
per mol flavin
1500
-
D-lactate
-
per mol flavin
0.00167
-
glycolate
Q94AX4
-
0.1167
-
L-lactate
Q94AX4
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
24.17
-
D-2-hydroxybutyrate
Q94AX4
-
84693
0.0167
-
D-glycerate
Q94AX4
-
9228
6.583
-
D-lactate
Q94AX4
-
9256
0.0033
-
glycolate
Q94AX4
-
11117
0.033
-
L-lactate
Q94AX4
-
12273
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.12
-
oxalate
-
pH 8.0, 30C
0.01
-
oxaloacetate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.203
-
-
after purification by 4-hydroxy-alpha-cyanocinnamic acid-AH-Sepharose column chromatography, pH and temperature not specified in the publication
0.342
-
-
after purification by hydroxylapatite column chromatography and 4-hydroxy-alpha-cyanocinnamic acid-AH-Sepharose column chromatography, pH and temperature not specified in the publication
3.38
-
-
enzyme purified on H-Sepharose with covalently bound 4-hydroxy-alpha cyanocinnamic acid
5.71
-
-
combination of chromatography on hydroxylapatite and H-Sepharose with covalently bound 4-hydroxy-alpha cyanocinnamic acid
20.3
-
-
purified enzyme
87
-
-
purified enzyme
1670
-
-
purified enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
with ferricyanide
7
-
-
phosphate buffer
7
-
-
assay at
7.5
-
-
imidazole and Tris buffer
7.5
-
-
with cytochrome c
7.5
-
-
assay at
8
9
Q94AX4
pH optimum for D-lactate, L-lactate and glycolate oxidation
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
no activity at pH 5, almost maximum activity at pH 9
5.5
7.5
-
very low activity with ferricyanide
5.5
8.5
-
low activity with cytochrome c at pH 5.5, almost maximum activity at pH 8.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
cells cultured in a medium containing DL-lactate as the sole carbon source
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
either on the inner side of the inner mitochondrial membrane or in the matrix
Manually annotated by BRENDA team
additional information
-
equally distributed between soluble and membrane fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
100000
-
-
sedimentation equilibrium centrifugation
105000
-
-
sedimentation equilibrium centrifugation
135000
-
Q94AX4
gel filtration
235000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 55000, sedimentation equilibrium centrifugation and SDS-PAGE
homodimer
Q94AX4
2 * 59000, sequence analysis
tetramer
-
4 * 57000, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
stable for short term exposure (30 s)
6.5
-
-
very stable
7.25
-
Q94AX4
retains at least 25% activity down to pH 7.25, whereas it rapidly loses activity at lower pH values
7.5
-
-
complete inactivation above pH 7.5
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
-
30 min, about 10% loss of activity
55
-
-
10 min, about 90% loss of activity
60
-
-
rapid inactivation above
75
-
-
2 min,about 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dithiothreitol and bovine serum albumin required for stability
-
very stable in cold
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 0.1 M Tris-buffer, pH 7.3, 20% loss of activity
-
4C, in presence of dithiothreitol, stable
-
-20C, as ammonium sulfate precipitate
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by centrifugation, sonication and on Ni2+-NTA column, to near homogeneity
Q94AX4
by affinity chromatography
-
by fast protein liquid chromatography on hydroxylapatite and on AH-Sepharose with covalently bound 4-hydroxy-a cyanocinnamic acid; hydroxylapatite column chromatography and 4-hydroxy-alpha-cyanocinnamic acid-AH-Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into vector pET16 and expressed in Escherichia coli BLR DE3 pLysS
Q94AX4
gene amplification in Escherichia coli
-
in Saccharomyces cerevisiae, gene amplification in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Q94AX4
mRNAs are present in both d2hgdh mutant lines, but not in dldh1-1 and dldh1-2 mutant lines
additional information
-
mutation in fog1, fog 2 and Klhap2 gene loci for regulation studies
additional information
-
mutation in Hap1p/2/3/4/5 gene loci for regulation studies
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
Pseudomonas stutzeri containing D-lactate dehydrogenase can act as a novel biocatalyst for pyruvate production from DL-lactate
additional information
-
carbon paste electrode-based biosensor with immobilized D-LCR seems to be optimal for analysis, representing significant advantage due to simplification of the whole device, i.e., the sensor exerts lower limit of detection under supposed concentration of D-lactate in real samples, low material demands, simplicity of D-LCR biosensor and short total time of analysis of about 2 min, pointing at the sensor possibilities in commercial applications