1.1.1.28: D-lactate dehydrogenase
This is an abbreviated version!
For detailed information about D-lactate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.28
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1.1.1.28
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myocardial
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creatine
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cardiac
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necrosis
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alt
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sod
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leakage
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lymphoma
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hydroxide
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ischemia
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dismutase
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reperfusion
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albumin
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infarct
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artery
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lymphocyte
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aminotransferase
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platelet
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gsh
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caspase-3
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malondialdehyde
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tnf
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pain
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lumbar
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marrow
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coronary
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cardiomyocytes
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herniation
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wistar
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univariate
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admission
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cardioprotective
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bilirubin
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admitted
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ischemia-reperfusion
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covid-19
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c-reactive
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non-hodgkin
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chest
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progression-free
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pleural
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reoxygenation
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d-dimer
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phosphokinase
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extranodal
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gsh-px
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intercalated
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dlbcl
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nanosheets
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langendorff
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synthesis
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molecular biology
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diagnostics
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biotechnology
- 1.1.1.28
- myocardial
- creatine
- cardiac
- necrosis
-
alt
- sod
- leakage
- lymphoma
-
hydroxide
- ischemia
- dismutase
-
reperfusion
- albumin
- infarct
- artery
- lymphocyte
- aminotransferase
- platelet
- gsh
- caspase-3
- malondialdehyde
- tnf
- pain
-
lumbar
- marrow
- coronary
- cardiomyocytes
- herniation
- wistar
-
univariate
-
admission
-
cardioprotective
- bilirubin
-
admitted
-
ischemia-reperfusion
- covid-19
-
c-reactive
-
non-hodgkin
- chest
-
progression-free
- pleural
-
reoxygenation
-
d-dimer
-
phosphokinase
-
extranodal
- gsh-px
-
intercalated
-
dlbcl
-
nanosheets
-
langendorff
- synthesis
- molecular biology
- diagnostics
- biotechnology
Reaction
Synonyms
D-(-)-lactate dehydrogenase, D-(-)-lactate dehydrogenase (NAD), D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein, D-lactate dehydrogenase, D-lactic acid dehydrogenase, D-lactic dehydrogenase, D-LDH, D-LDH-like enzyme, D-LDH0653, D-LDH1, D-LDH2, D-LDH3, D-LDH82319, D-nLDH, D-specific lactic dehydrogenase, dehydrogenase, D-lactate, DLD1, DLDH, DLDH744, ECBD_2243, ECLDH, FD35_GL001981, Fermentative lactate dehydrogenase, FN0511, FNLDH, lactic acid dehydrogenase, ldb0101, Ldb1010, LDH, LdhA, ldhd, LDHD1, LDHD2, LDHD3, LdhTi, Ljd-LDH, MGG_01202, NAD-dependent D-lactate dehydrogenase, PA0927, PALDH, Respiratory D-lactate dehydrogenase, SO_0968, tp0037, WP_013906894
ECTree
1.1.1.28 D-lactate dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.1.28 - D-lactate dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F299G
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mutation reduces enzyme activity with less marked change in substrate preference
F299S
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mutation reduces enzyme activity with less marked change in substrate preference
Y52A
Y52L
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site-directed mutagenesis, enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus
Y52R
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mutation severely reduces enzyme activity, preference for large aliphatic 2-ketoacids and phenylpyruvate
Y52R/F299G
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mutation abolishes activity with pyruvate, 2-ketobutyrate, 2-ketovalerate, 2-ketoisovalerate, 2-ketoisocaproate and oxaloacetate, weak activity with 2-ketocaproate, 2-ketoglutarate and phenylpyruvate
Y52T/F299S
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mutation abolishes activity with pyruvate, 2-ketobutyrate, 2-ketovalerate, 2-ketoisovalerate, 2-ketoisocaproate, 2-ketoglutarate and oxaloacetate, weak activity with hydroxypyruvate and phenylpyruvate
Y52V
Y52L
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mutant used for synthesis of (R)-2-hydroxy-4-phenylbutyric acid in Pichia pastoris
D259N
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56fold reduction in kcat, 5fold lowering of Km, shifting of the enzymatic activity profile towards the acidic range by two units
E264G
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shift of 2 units in optimal pH toward the acidic range
H296K
Y52L/F299Y
V152R
catalytic efficiency with NAD analogue nicotinamide cytosine dinucleotide is 2.4fold higher than that with NAD
V152R/I177K
mutant shows good activity with NAD analogue nicotinamide cytosine dinucleotide and reduced activity with NAD
V152R/I177K/N213I
triple mutant shows high preference or activity with NAD analogue nicotinamide cytosine dinucleotide
V152R/N213E
mutant shows good activity with NAD analogue nicotinamide cytosine dinucleotide and reduced activity with NAD
V152R/V210N/N213E
triple mutant shows high preference or activity with NAD analogue nicotinamide cytosine dinucleotide
Y51A
mutant with improved catalytic efficiency on phenylpyruvate
Y51F
mutant with improved catalytic efficiency on 2-oxobutanoate and 3-methyl-2-oxobutanoate of 37.2 and 23.2 per s and mM, respectively
Y51L
mutant with improved catalytic efficiency on phenylpyruvate of 2200 per s and mM
Y51M
mutant with improved catalytic efficiency on phenylpyruvate
Y51S
mutant with improved catalytic efficiency on phenylpyruvate
Y51A
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mutant with improved catalytic efficiency on phenylpyruvate
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Y51F
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mutant with improved catalytic efficiency on 2-oxobutanoate and 3-methyl-2-oxobutanoate of 37.2 and 23.2 per s and mM, respectively
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E263A
site-directed mutagenesis, the mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
F298A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
G79A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
H295A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
M307A
site-directed mutagenesisthe mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
R234A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
Y101A
site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
G79A
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site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
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H295A
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site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
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R234A
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site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
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Y101A
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site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
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A234G
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mutation enhances catalytic activity toward pyruvate
A234S
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mutation enhances catalytic activity toward pyruvate
A234G
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mutation enhances catalytic activity toward pyruvate
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A234S
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mutation enhances catalytic activity toward pyruvate
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additional information
Y52A
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mutation induces high activity and preference for large aliphatic 2-ketoacids and phenylpyruvate
Y52A
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site-directed mutagenesis, enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus
Y52V
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mutation induces high activity and preference for large aliphatic 2-ketoacids and phenylpyruvate
Y52V
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site-directed mutagenesis, enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus. Escherichia coli pET-28a-d-ldh produces 12.2 g phenyllactate/l in 3 h with a molar conversion rate of 61%, while Escherichia coli pET-28a-d-ldhY52V produces 15.6 g phenyllactate/l with a molar conversion rate of 77%. Site-directed mutagenesis of d-ldh markedly improves D-phenyllactate yield and substrate conversion rate. Phenyllactate yield does not show a significant increase when higher glucose amounts are added. Method optimization, overview
H296K
no significant changes in kcat or Km value, shift of optimum pH value from 7.0-7.5 to 6
Y52L/F299Y
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the mutant shows a specific activity that is 233.2-312.3fold higher than that of the wild type recombinant enzyme
Y52L/F299Y
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the mutant shows a specific activity that is 233.2-312.3fold higher than that of the wild type recombinant enzyme
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additional information
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at media D-lactate concentrations greater than 5-10 mM the development of wild-type plants is arrested shortly after germination whereas plants overexpressing the endogenous D-lactate dehydrogenase detoxify D-lactate to pyruvate and survive, phenotypes, overview
additional information
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at media D-lactate concentrations greater than 5-10 mM the development of wild-type plants is arrested shortly after germination whereas plants overexpressing the endogenous D-lactate dehydrogenase detoxify D-lactate to pyruvate and survive, phenotypes, overview
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additional information
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due to the presence of the pentose phosphate pathway, wild-type strain IO-1 produces only L-lactic acid, disruption of the phosphoketolase pathway by deletion of the phosphoketolase 1 gene xpk1 in the L-lactate dehydrogenase gene ldhL1-deficient DELTAxpk1,DELTAldhL1 NCIMB 8826 strain results in strain DELTAldhL1 NCIMB 8826, which produces optically pure D-lactic acid, introduction of the pentose phosphate pathway by introduction of the transketolase gene from Lactococcus lactis IL 1403 into this strain. Xylose fermentation by the mutant strains, overview
additional information
Lactiplantibacillus plantarum NCIMB 8826
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due to the presence of the pentose phosphate pathway, wild-type strain IO-1 produces only L-lactic acid, disruption of the phosphoketolase pathway by deletion of the phosphoketolase 1 gene xpk1 in the L-lactate dehydrogenase gene ldhL1-deficient DELTAxpk1,DELTAldhL1 NCIMB 8826 strain results in strain DELTAldhL1 NCIMB 8826, which produces optically pure D-lactic acid, introduction of the pentose phosphate pathway by introduction of the transketolase gene from Lactococcus lactis IL 1403 into this strain. Xylose fermentation by the mutant strains, overview
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additional information
Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
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due to the presence of the pentose phosphate pathway, wild-type strain IO-1 produces only L-lactic acid, disruption of the phosphoketolase pathway by deletion of the phosphoketolase 1 gene xpk1 in the L-lactate dehydrogenase gene ldhL1-deficient DELTAxpk1,DELTAldhL1 NCIMB 8826 strain results in strain DELTAldhL1 NCIMB 8826, which produces optically pure D-lactic acid, introduction of the pentose phosphate pathway by introduction of the transketolase gene from Lactococcus lactis IL 1403 into this strain. Xylose fermentation by the mutant strains, overview
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additional information
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highly stereoselective biosynthesis of (R)-alpha-hydroxy carboxylic acids through rationally re-designed mutation of D-lactate dehydrogenase, asymmetric reduction of a homologous series of alpha-keto carboxylic acids such as phenylpyruvic acid, 2-oxobutyric acid, 2-oxovaleric acid, beta-hydroxypyruvate, overview. Compared with wild-type D-nLDH, the Y52L mutant D-nLDH shows elevated activities toward unnatural substrates especially with large substitutes at C-3. By the biocatalysis combined with a formate dehydrogenase for in situ generation of NADH, the corresponding (R)-alpha-hydroxy carboxylic acids can be produced at high yields and highly optical purity. Production of chiral (R)-phenyllactic acid. 50 mM PPA is completely reduced to (R)-phenyllactate in 90 min with a high yield of 99.0% and a highly optical purity (99.9% e.e.) by the engineered coupled production system. Activties of the F299Y mutant are similar to the wild-type enzyme
additional information
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highly stereoselective biosynthesis of (R)-alpha-hydroxy carboxylic acids through rationally re-designed mutation of D-lactate dehydrogenase, asymmetric reduction of a homologous series of alpha-keto carboxylic acids such as phenylpyruvic acid, 2-oxobutyric acid, 2-oxovaleric acid, beta-hydroxypyruvate, overview. Compared with wild-type D-nLDH, the Y52L mutant D-nLDH shows elevated activities toward unnatural substrates especially with large substitutes at C-3. By the biocatalysis combined with a formate dehydrogenase for in situ generation of NADH, the corresponding (R)-alpha-hydroxy carboxylic acids can be produced at high yields and highly optical purity. Production of chiral (R)-phenyllactic acid. 50 mM PPA is completely reduced to (R)-phenyllactate in 90 min with a high yield of 99.0% and a highly optical purity (99.9% e.e.) by the engineered coupled production system. Activties of the F299Y mutant are similar to the wild-type enzyme
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additional information
enzymatic production of D-3-phenyllactic acid by recombinant Pediococcus pentosaceus D-lactate dehydrogenase with NADH regeneration by recombinant Ogataea parapolymorpha formate dehydrogenase, EC 1.2.1.2, at pH 6.0, 50°C
additional information
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enzymatic production of D-3-phenyllactic acid by recombinant Pediococcus pentosaceus D-lactate dehydrogenase with NADH regeneration by recombinant Ogataea parapolymorpha formate dehydrogenase, EC 1.2.1.2, at pH 6.0, 50°C
additional information
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enzyme deletion mutant, sensitive to osmotic conditions indicating an aktin disfunction
additional information
glutamate dehydrogenase activities of enzyme mutants, overview
additional information
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glutamate dehydrogenase activities of enzyme mutants, overview
additional information
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glutamate dehydrogenase activities of enzyme mutants, overview
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additional information
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random mutagensis, and screening for gain-of-function mutants, mutant Y2-8 shows improved D(-)-lactate synthesis, which is 2fold increased compared to the wild-type strain DX12
additional information
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random mutagensis, and screening for gain-of-function mutants, mutant Y2-8 shows improved D(-)-lactate synthesis, which is 2fold increased compared to the wild-type strain DX12
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additional information
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construction of peroxidase-based biosensors for the selective determination of D,L-lactic acid and L-malic acid in wines, enzyme immobilization, method optimization, overview
additional information
fermentation conditions are critical for microbial growth and lactic acid secretion, optimization of enzyme and D-lactic acid production by the enzyme from Thermodesulfatator indicus in Bacillus licheniformis strains B11 and BA11, overview. Disruption of the lactate permease LctP in host strains BN11 and BA11 results in reductions in D-lactic acid (28.6 and 35.2%, respectively). Replacement of LctP inhost strain BN11 with the mesophilic permease LldP of Escherichia coli also leads to a 12.1% decrease in D-lactic acid accumulation
