Any feedback?
Information on EC 1.1.1.28 - D-lactate dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P06149
for references in articles please use BRENDA:EC1.1.1.28Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.28 D-lactate dehydrogenaseSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
ldh, d-lactate dehydrogenase, d-ldh, paldh, fermentative lactate dehydrogenase, nad-dependent d-lactate dehydrogenase, d-nldh, ljd-ldh, d-(-)-lactate dehydrogenase, ecldh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-(-)-lactate dehydrogenase (NAD)
-
-
-
-
D-lactic acid dehydrogenase
-
-
-
-
D-lactic dehydrogenase
-
-
-
-
D-LDH
D-specific lactic dehydrogenase
-
-
-
-
dehydrogenase, D-lactate
-
-
-
-
Fermentative lactate dehydrogenase
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
LDH
-
-
-
-
Respiratory D-lactate dehydrogenase
-
-
-
-
D-LDH
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY
9028-36-8
-
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
pyruvate + NADH + H+
(R)-lactate + NAD+
-
a highly stereospecific reaction leading to 98-99%optical purity of the product
-
-
r
additional information
?
-
-
effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition
-
-
?
additional information
?
-
the enzyme ECLDH exhibits high substrate specificity toward pyruvate. No or poor activity with 2-oxovalerate, 2-oxoisovalerate, 2-oxocaproate, 2-oxoisocaproate, phenylpyruvate, and hydroxyphenylpyruvate
-
-
?
additional information
?
-
-
the enzyme ECLDH exhibits high substrate specificity toward pyruvate. No or poor activity with 2-oxovalerate, 2-oxoisovalerate, 2-oxocaproate, 2-oxoisocaproate, phenylpyruvate, and hydroxyphenylpyruvate
-
-
?
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
?
-
-
effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no activation of the enzyme by fructose 1,6-bisphosphate and Mg2+
-
additional information
-
no activation of the enzyme by fructose 1,6-bisphosphate and Mg2+
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.092
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
6.5
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
additional information
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
-
additional information
additional information
-
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
730
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
400
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8000
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
61
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity of the recombinant enzyme in Corynebacerium glutamicum compared to the wild-type enzyme in Escherichia coli, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homooctamer
8 * 38500, about, sequence calculation, the apparently octameric form of ECLDH is likely an artificial product due to the overexpression, and exhibits slightly but significantly lower specific activity than the tetrameric form
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of the apo and ternary complex structures of Fusobacterium nucleatum FnLDH and Escherichia coli EcLDH and Pseudomonas aeruginosa PaLDH. FnLDH and EcLDH exhibit positive cooperativity in substrate binding, and PaLDH shows negatively cooperative substrate binding. The three enzymes consistently form homotetrameric structures with three symmetric axes, the P-, Q-, and R-axes, which allows apo-FnLDH and EcLDH to form wide intersubunit contact surfaces between the opened catalytic domains of the two Q-axis-related subunits in coordination with their asymmetric and distorted quaternary structures. apo-PaLDH possesses a highly symmetrical quaternary structure and partially closed catalytic domains that are favorable for initial substrate binding and forms virtually no intersubunit contact surface between the catalytic domains
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
739841
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ecd_01352, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
gene ldhA, expression in an enzyme-deficient ldhA-null Corynebacterium glutamicum strain resulting in increased production of D-lactate
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garvie, E.I.
Bacterial lactate dehydrogenases
Microbiol. Rev.
44
106-139
1980
Klebsiella aerogenes, Leuconostoc mesenteroides, Eubacterium limosum, Escherichia coli, Lactobacillus acidophilus, Lactiplantibacillus plantarum, Levilactobacillus brevis, Lentilactobacillus buchneri, Lactobacillus delbrueckii subsp. bulgaricus, Lacticaseibacillus casei, Limosilactobacillus fermentum, Weissella confusa, Lactobacillus delbrueckii, Lactobacillus delbrueckii subsp. lactis, Lactobacillus jensenii, Lactobacillus jugurt-helveticus, Lactobacillus leichmannii, Lactobacillus vermiforme, Weissella viridescens, Lactococcus lactis, Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. dextranicum, Leuconostoc lactis, Oenococcus oeni, Weissella paramesenteroides, Mammalia, Staphylococcus aureus, Mycoplasma sp., Pediococcus acidilactici, Pediococcus damnosus, Pediococcus inopinatus, Pediococcus pentosaceus, Selenomonas ruminantium, Staphylococcus haemolyticus, Staphylococcus hominis, Staphylococcus sp., Staphylococcus warneri
Dym, O.; Pratt, E.A.; Ho, C.; Eisenberg, D.
The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme
Proc. Natl. Acad. Sci. USA
97
9413-9418
2000
Escherichia coli (P06149), Escherichia coli
Zhu, J.; Shimizu, K.
Effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition
Metab. Eng.
7
104-115
2005
Escherichia coli
Okino, S.; Suda, M.; Fujikura, K.; Inui, M.; Yukawa, H.
Production of D-lactic acid by Corynebacterium glutamicum under oxygen deprivation
Appl. Microbiol. Biotechnol.
78
449-454
2008
Escherichia coli, Lactobacillus delbrueckii
Furukawa, N.; Miyanaga, A.; Togawa, M.; Nakajima, M.; Taguchi, H.
Diverse allosteric and catalytic functions of tetrameric D-lactate dehydrogenases from three Gram-negative bacteria
AMB Express
4
76
2014
Escherichia coli (A0A140N893), Escherichia coli, Fusobacterium nucleatum subsp. nucleatum (Q8RG11), Pseudomonas aeruginosa (Q9I530), Pseudomonas aeruginosa, Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847 (Q8RG11)
Furukawa, N.; Miyanaga, A.; Nakajima, M.; Taguchi, H.
Structural basis of sequential allosteric transitions in tetrameric D-lactate dehydrogenases from three Gram-negative bacteria
Biochemistry
57
5388-5406
2018
Escherichia coli (A0A140N893), Escherichia coli, Fusobacterium nucleatum subsp. nucleatum (Q8RG11), Pseudomonas aeruginosa (Q9I530), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I530), Fusobacterium nucleatum subsp. nucleatum DSM 15643 (Q8RG11), Escherichia coli BL21-DE3 (A0A140N893)
EXTERNAL LINKS (specific for EC-Number 1.1.1.28)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
