Information on EC 1.1.1.28 - D-lactate dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.28
-
RECOMMENDED NAME
GeneOntology No.
D-lactate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
heterolactic fermentation
-
-
L-alanine degradation II (to D-lactate)
-
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Microbial metabolism in diverse environments
-
-
mixed acid fermentation
-
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Pyruvate metabolism
-
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superpathway of fermentation (Chlamydomonas reinhardtii)
-
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superpathway of glucose and xylose degradation
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vancomycin resistance I
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alanine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-36-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene APE_0487; gene APE_0487
UniProt
Manually annotated by BRENDA team
Allomyces sp.
-
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
bivalve mollusc
-
-
Manually annotated by BRENDA team
black abalone
-
-
Manually annotated by BRENDA team
land snail
-
-
Manually annotated by BRENDA team
Lactobacillus jugurt-helveticus
-
-
-
Manually annotated by BRENDA team
strain NRIC 1067T, enzyme activity appears in late stage of logarithmic growth, increase of activity due to growth in presence of 50 mM sodium acetate
-
-
Manually annotated by BRENDA team
strain NRIC 1071T, enzyme activity appears in late stage of logarithmic growth, increase of activity due to growth in presence of 50 mM sodium acetate
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-
Manually annotated by BRENDA team
strain NRIC 1071T, enzyme activity appears in late stage of logarithmic growth, increase of activity due to growth in presence of 50 mM sodium acetate
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene ldhD or LEUM 1756
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-
Manually annotated by BRENDA team
horseshoe crab
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
seaworm
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
slime mold
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
No. 7, grown photoanaerobically on lactate
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-
Manually annotated by BRENDA team
strain DX12, isolated from soil
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-
Manually annotated by BRENDA team
strain DX12, isolated from soil
-
-
Manually annotated by BRENDA team
strain LDH-1, isolated as high producer of enzyme, growth under anaerobic conditions
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
two evolutionarily distinct families of LDH enzymes perform the oxidation of NADH/reduction of NAD+ to yield a product that differs only in its chirality: L-lactate or D-lactate
metabolism
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 + NAD+
pyruvate + NADH
show the reaction diagram
(R)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
2-ketocaproate + NADH
2-hydroxycaproate + NAD+
show the reaction diagram
-
-
-
-
?
2-ketoisocaproate + NADH
2-hydroxyisocaproate + NAD+
show the reaction diagram
-
-
-
-
?
2-ketoisovalerate + NADH
2-hydroxyisovalerate + NAD+
show the reaction diagram
-
-
-
-
?
2-ketovalerate + NADH
2-hydroxyvalerate + NAD+
show the reaction diagram
-
-
-
-
?
2-oxo-4-phenyl-butyric acid + NADH + H+
(R)-2-hydroxy-4-phenyl-butyric acid + NAD+
show the reaction diagram
-
-
-
-
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
-
?
2-oxobutyric acid + NADH + H+
(R)-2-hydroxybutyric acid + NAD+
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + NADH + H+
2-hydroxypentanedioate + NAD+
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenylpyruvic acid + NADH + H+
(R)-3,4-dihydroxyphenyllactic acid + NAD+
show the reaction diagram
-
-
-
-
?
alpha-ketobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
bromopyruvate + NADH
3-bromo-2-hydroxypropanoate + NAD+
show the reaction diagram
-
-
-
-
?
D-lactate + cytochrome c2ox
pyruvate + cytochrome c2red
show the reaction diagram
-
-
-
-
?
D-lactate + NAD+
pyruvate + NADH
show the reaction diagram
DL-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH
show the reaction diagram
DL-2-hydroxybutyrate + NAD+
? + NADH
show the reaction diagram
-
about 44% of activity against D-lactate
-
-
-
glyoxylate + NADH
hydroxyacetic acid + NAD+
show the reaction diagram
-
-
-
-
?
glyoxylate + NADH + H+
hydroxyacetic acid + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADH
glycerate + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADH + H+
glycerate + NAD+
show the reaction diagram
-
-
-
-
?
methylpyruvate + NADH
? + NAD+
show the reaction diagram
oxaloacetate + NADH
malate + NAD+
show the reaction diagram
oxaloacetic acid + NADH + H+
(R)-malate + NAD+
show the reaction diagram
-
-
-
-
ir
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
-
-
-
-
?
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
show the reaction diagram
phenylpyruvate + NADH + H+
D-phenyllactate + NAD+
show the reaction diagram
-
-
-
-
ir
pyruvate + NADH
(R)-lactate + NAD+
show the reaction diagram
pyruvate + NADH + H+
(R)-lactate + NAD+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-lactate + NAD+
pyruvate + NADH
show the reaction diagram
(R)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
D-lactate + NAD+
pyruvate + NADH
show the reaction diagram
O66939
-
-
-
r
phenylpyruvate + NADH + H+
(R)-3-phenyllactate + NAD+
show the reaction diagram
pyruvate + NADH
(R)-lactate + NAD+
show the reaction diagram
pyruvate + NADH + H+
(R)-lactate + NAD+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates by 15% at 1 mM
Ni2+
-
activates by 35% at 1 mM
Zn2+
-
very slightly activating
additional information
-
poor effects by 1 mM Ca2+, Zn2+, Mg2+, Ba2+, and Co2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ba2+
-
slight inhibition at 1 mM
Fe2+
-
inhibits 25% at 1 mM
iodoacetamide
iodoacetate
Mn2+
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slight inhibition at 1 mM
oxalate
oxamate
p-chloromercuribenzoate
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-
p-Chloromercuriphenyl sulfonic acid
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-
p-hydroxymercuribenzoate
phenylhydrazine
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up to 45% inhibition
pyruvate
SDS
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over 95% inhibition at 1 mM
Sodium arsenite
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-
ZnSO4
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1 mM, 80% inhibition, EDTA restores
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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strongly reducing enviroment required
fructose 1,6-diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.59 - 1250
(R)-lactate
0.38 - 20.8
2-Ketobutyrate
1.18 - 189
2-ketocaproate
15.5
2-Ketoglutarate
-
30C, pH 5.5, wild-type enzyme
0.124 - 31
2-ketoisocaproate
5.5 - 18.6
2-ketoisovalerate
0.15 - 17
2-Ketovalerate
2.3 - 58
2-oxobutyrate
4.4 - 10
alpha-Ketobutyrate
0.8
D-lactate
-
pH 8.0, 30C
19
DL-2-Hydroxybutyrate
-
pH 8.0, 25C
5.4 - 100
glyoxylate
0.28 - 53
Hydroxypyruvate
0.00044 - 2.9
NAD+
0.00021 - 2.83
NADH
0.0035
NADPH
-
-
2.2 - 43.1
oxaloacetate
0.03 - 22
phenylpyruvate
0.07 - 31
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2280
(R)-lactate
Leuconostoc mesenteroides subsp. mesenteroides
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pH 11.0, 20C, recombinant enzyme
41 - 175
2-Ketobutyrate
0.056 - 21
2-ketocaproate
0.51
2-Ketoglutarate
Lactobacillus pentosus
-
30C, pH 5.5, wild-type enzyme
11.1 - 65.7
2-ketoisocaproate
11.7 - 27
2-ketoisovalerate
5.7 - 334
2-Ketovalerate
4.5 - 120
2-oxobutyrate
50 - 270
glyoxylate
8.1 - 407
Hydroxypyruvate
0.64 - 4.42
NAD+
8.28 - 633
NADH
0.48 - 280
oxaloacetate
0.31 - 778
phenylpyruvate
22 - 29000
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.41 - 1.61
NAD+
7
182.6 - 232.6
NADH
8
100 - 105
phenylpyruvate
198
658 - 3157
pyruvate
31
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
44 - 140
formate
0.12
oxalate
-
pH 8.0, 30C
2.8 - 43
oxamate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
isozyme D-LDH1, pH 8.0, 25C, substrate D-phenylpyruvate
8.78
-
purified recombinant enzyme, D-lactate oxidation, pH 11.0, 20C
9
-
isozyme D-LDH2, pH 8.0, 25C, substrate D-phenylpyruvate
10
-
commercial preparation
13.5
-
pH 8.0, 30C
18
-
isozyme D-LDH3, pH 8.0, 25C, substrate oxaloacetic acid
28
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isozyme D-LDH3, pH 8.0, 25C, substrate D-phenylpyruvate
41
-
isozyme D-LDH2, pH 8.0, 25C, substrate 2-oxoobutyric acid
41.91
-
isozyme D-LDH3, pH 8.0, 25C, substrate D-lactate
68
-
isozyme D-LDH1, pH 8.0, 25C, substrate 2-oxoobutyric acid
88.71
-
isozyme D-LDH2, pH 8.0, 25C, substrate D-lactate
96.88
-
isozyme D-LDH1, pH 8.0, 25C, substrate D-lactate
116
-
substrate phenylpyruvate, pH 5.5, 45C
140
-
purified recombinant enzyme, substrate phenylpyruvate, pH 5.5, 30C
189
-
isozyme D-LDH3, pH 8.0, 25C, substrate 2-oxoobutyric acid
348
-
isozyme D-LDH3, pH 8.0, 25C, substrate pyruvate
422
-
purified recombinant enzyme, substrate pyruvate, pH 5.5, 30C
835
-
substrate pyruvate, pH 5.5, 45C
1710
-
pH 8.0, 25C
2877
-
isozyme D-LDH2, pH 8.0, 25C, substrate oxaloacetic acid
2997
-
isozyme D-LDH2, pH 8.0, 25C, substrate pyruvate
3151
-
isozyme D-LDH1, pH 8.0, 25C, substrate oxaloacetic acid
3838
-
isozyme D-LDH1, pH 8.0, 25C, substrate pyruvate
4450
-
purified recombinant enzyme, NADH oxidation, pH 8.0, 30C
4990
-
purified recombinant enzyme, pyruvate reduction, pH 8.0, 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
-
pH 3.6 or pH 8.0, changes with pyruvate concentration
5
-
substrate pyruvate
5.8 - 6.5
-
-
6.4 - 7.5
-
-
6.4
-
reduction of pyruvate
7 - 7.5
8.2 - 9.7
8.2
-
substrate D-lactate
9
-
oxidation of (R)-lactate
10
-
isozyme D-LDH3
11
-
lactate oxidation reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
activity range, profile overview
4 - 7
-
activity range, profile, overview
6 - 11
7 - 13
-
lactate oxidation reaction, activity range, profile overview
7.5 - 11
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isozymes D-LDH1 and D-LDH2, activity range, profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
lactate oxidation reaction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 55
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isozymes D-LDH1 and D-LDH2, activity range, profile, overview
10 - 60
-
isozyme D-LDH3, activity range, profile, overview
10 - 50
-
activity range, profile overview
20 - 70
-
activity range, profile, overview
25 - 60
-
activity range, profile overview
50
-
33% of activity at 40C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
cytoplasmic side
-
Manually annotated by BRENDA team
-
D-lactate dehydrogenase is inserted into the inner membrane of mitochondria through its transmembrane domain located close to the N-terminus of the polypeptide chain in such a way that the protein globule is exposed in the intermembrane space
Manually annotated by BRENDA team
-
spheroplast membrane
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Escherichia coli (strain K12)
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
2 * 32000, SDS-PAGE
34000
-
4 * 34000, SDS-PAGE
37203
-
x * 37203, sequence calculation
57000
-
x * 57000, SDS-PAGE
59000
1 * 59000, recombinant enzyme, SDS-PAGE
61000
recombinant enzyme, gel filtration
64000
-
gel filtration
68000 - 70000
-
gel filtration, analytical ultracentrifugation
70000 - 80000
-
gel filtration, equilibrium sedimentation
70000
-
SDS-PAGE
98000
-
sucrose density gradient sedimentation
115000
-
gel filtration
140000
-
gel filtration
145000
-
gel filtration
235000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 15 mg/ml protein in 10 mM potassium phosphate, pH 7.0, with 0.002 ml of reservoir solution containing 14.4% PEG 8000, 80 mM cacodylate pH 6.5, 160 mM calcium acetate and 20% glycerol, and equilibration against 0.1 ml of reservoir solution, 25C, 2 weeks, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified recombinant enzyme in fully closed formation with lactate or pyruvate bound to the active site of each subunit of the functional dimer, 0.001 ml of protein solution containing 20.3 mg/ml protein in 20 mM Tris-HCl buffer pH 8.0 containing 150 mM NaCl, is mixed with 0.001 ml of reservoir solution containing 0.1 M MES buffer, pH 6.0, and 25% w/v PEG 200, 10 days, method optimization, X-ray diffraction structure determination and analysis at 2.12 A resolution, molecular replacement and structure modelling
hexagonal and tetragonal crystal forms, tetragonal form diffracted to 3.0 A resolution
-
1.9 A resolution
crystals belong to the orthorhombic space group, diffract beyond 3.0 A resolution
-
hanging drop vapour diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
-
656314
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 55
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thermal stability of the D-LDH isozymes, pH 7.0, with sodium pyruvate as a substrate, profiles, overview
30 - 40
-
the enzyme is significantly stable below 30C, but the activity decreases significantly above 40C
30 - 45
-
87% activity remaining after 4 h at 30C, higher loss of activity above 45C
35
-
stable below, Tris-HCl, pH 8.5