Information on EC 1.1.1.27 - L-lactate dehydrogenase

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

EC NUMBER
COMMENTARY
1.1.1.27
-
RECOMMENDED NAME
GeneOntology No.
L-lactate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(S)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
reduction of pyruvate follows an Theorell-Chance mechanism
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
mechanism
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
the NAD (H)-dependent L-LDH catalyzes the reduction of pyruvate by an ordered catalytic mechanism, catalytic cycle, overview
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
the enzyme-NADH-pyruvate ternery complex undergoes a rate-limiting conformational change, in which the substrate loop closes to form a desolvated ternary complex in order to bring the catalytic residue Arg109 into the active site, the catalytic residues Arg109, Asp168, and His195 are highly conserved, catalyic mechanism, detailed overview
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
Biosynthesis of secondary metabolites
-
Cysteine and methionine metabolism
-
glucose and xylose degradation
-
Glycolysis / Gluconeogenesis
-
heterolactic fermentation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Propanoate metabolism
-
pyruvate fermentation to lactate
-
Pyruvate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:NAD+ oxidoreductase
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A4-LDH
Q0GND8
-
anaerobic lactate dehydrogenase
Q0GND9
-
anaerobic lactate dehydrogenase
Q0GND8
-
BbLDH
Q7Z0X7
-
dehydrogenase, lactate
-
-
-
-
eLDHA
B7XH73
-
eLDHB
C6L1K8
-
Epsilon crystallin
-
-
-
-
epsilon-crystallin
-
-
-
-
H4-L-lactate dehydrogenase
-
-
heart LDH
-
-
Immunogenic protein p36
-
-
-
-
L(+)-nLDH
-
-
-
-
L-(+)-lactate dehydrogenase
-
-
-
-
L-(+)-lactate dehydrogenase
B1A4R6
-
L-(+)-lactate dehydrogenase
Thermoanaerobacter ethanolicus JW200
B1A4R6
-
-
L-lactate dehydrogenase B
-
-
L-lactic acid dehydrogenase
-
-
-
-
L-lactic dehydrogenase
-
-
-
-
L-LDH
-
-
-
-
L-LDH
Thermoanaerobacter ethanolicus JW200
B1A4R6
-
-
lactate dehydrogenase
-
-
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
Bacillus subtilis BS35
-
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
Pontonia pinnophylax
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
Rhizopus delemar RA 99-880
-
-
-
lactate dehydrogenase
Rhizopus oryzae NRRL 395
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
-
-
lactate dehydrogenase
P90613, Q27797
-
lactate dehydrogenase A
B7XH73
-
lactate dehydrogenase B
C6L1K8
-
lactate dehydrogenase NAD-dependent
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
lactic dehydrogenase
-
-
-
-
LctD
Aggregatibacter actinomycetemcomitans HK1651 and VT1169
-
-
-
LDH
-
-
-
-
LDH
Bacillus subtilis BS35
-
-
-
LDH
-
-
LDH
Mus musculus AKR
-
-
-
LDH
Pontonia pinnophylax
-
-
LDH-1
-
-
LDH-2
-
-
LDH-3
-
-
LDH-4
-
-
LDH-5
-
-
LDH-A
-
-
LDH-A
-
-
LDH-A
Mus musculus AKR
-
-
-
LDH-A4
Pontonia pinnophylax
-
-
LDH1
P90613
-
LDH2
Q27797
-
LdhA
Rhizopus oryzae NRRL 395
-
-
LDHB
Rhizopus delemar RA 99-880
-
-
-
LDHB
Rhizopus oryzae NRRL 395
-
-
muscle LDH
-
-
NAD-lactate dehydrogenase
-
-
-
-
nitric oxideinducible l-lactate dehydrogenase
-
-
proteins, specific or class, anoxic stress response, p34
-
-
-
-
TeLdhL
Thermoanaerobacter ethanolicus JW200
B1A4R6
-
-
mLDH
-
-
additional information
-
lactate dehydrogenase is a member of the 2-hydroxyacid oxidoreductase family
CAS REGISTRY NUMBER
COMMENTARY
9001-60-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Agama stellio stellio
-
-
-
Manually annotated by BRENDA team
a Gram-negative opportunistic pathogen found exclusively in the mammalian oral cavity in the space between the gums and the teeth known as the gingival crevice, gene AA02769
-
-
Manually annotated by BRENDA team
Aggregatibacter actinomycetemcomitans HK1651 and VT1169
a Gram-negative opportunistic pathogen found exclusively in the mammalian oral cavity in the space between the gums and the teeth known as the gingival crevice, gene AA02769
-
-
Manually annotated by BRENDA team
Galapagos marine iguana, gene ldh-a
UniProt
Manually annotated by BRENDA team
epsilon-crystallin
-
-
Manually annotated by BRENDA team
strain 90
SwissProt
Manually annotated by BRENDA team
Bacillus megaterium 90
strain 90
SwissProt
Manually annotated by BRENDA team
strain BS35, gene ldh
-
-
Manually annotated by BRENDA team
Bacillus subtilis BS35
strain BS35, gene ldh
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
gene ldhA encoding L-lactate dehydrogenase
-
-
Manually annotated by BRENDA team
Cyclodina aenea
-
-
-
Manually annotated by BRENDA team
genes ldh-1 and ldh-2
-
-
Manually annotated by BRENDA team
eLDHA; isozymes LDH A, encoded by gene LDHA
UniProt
Manually annotated by BRENDA team
eLDHB, fragment; isozymes LDH B, encoded by gene LDHB
UniProt
Manually annotated by BRENDA team
several isozymes, overview
-
-
Manually annotated by BRENDA team
Hoplodactylus chrysosireticus
-
-
-
Manually annotated by BRENDA team
individuals from Man Island and mainland Wellington
-
-
Manually annotated by BRENDA team
common iguana
UniProt
Manually annotated by BRENDA team
ssp. casein
-
-
Manually annotated by BRENDA team
Lactobacillus mesenteroides
-
-
-
Manually annotated by BRENDA team
strain SK007
-
-
Manually annotated by BRENDA team
strain SK007
-
-
Manually annotated by BRENDA team
strain 760
-
-
Manually annotated by BRENDA team
strain MG1363, genes ldh and ldhB
Uniprot
Manually annotated by BRENDA team
Lactococcus lactis 760
strain 760
-
-
Manually annotated by BRENDA team
Lactococcus lactis MG1363
strain MG1363, genes ldh and ldhB
Uniprot
Manually annotated by BRENDA team
Molinema dessetae
-
-
-
Manually annotated by BRENDA team
strain AKR
-
-
Manually annotated by BRENDA team
Mus musculus AKR
strain AKR
-
-
Manually annotated by BRENDA team
no activity in Rubus idaeus
leaf
-
-
Manually annotated by BRENDA team
no activity in Taraxacum officinale
leaf
-
-
Manually annotated by BRENDA team
no activity in Zea mays
leaf
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
Pontonia pinnophylax
inhabiting the mantle cavity of host Pinna nobilis
-
-
Manually annotated by BRENDA team
female Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
male adult Wistar rats
-
-
Manually annotated by BRENDA team
Rhizopus delemar RA 99-880
-
-
-
Manually annotated by BRENDA team
strains 99-880 and NRRL 395, genes ldhB and ldhA
-
-
Manually annotated by BRENDA team
Rhizopus oryzae NRRL 395
-
-
-
Manually annotated by BRENDA team
gene ldh-1
-
-
Manually annotated by BRENDA team
Streptococcus mitior
-
-
-
Manually annotated by BRENDA team
fructose 1,6-diphosphate dependent enzyme
-
-
Manually annotated by BRENDA team
gene ldhL
B1A4R6
UniProt
Manually annotated by BRENDA team
Thermoanaerobacter ethanolicus JW200
gene ldhL
B1A4R6
UniProt
Manually annotated by BRENDA team
Thermus caldophilus GK24
GK24
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
LDH plays a central role in several metabolic pathways, e.g. in energy production in glycolysis, in gluconeogenesis. Glycolytic process, overview
metabolism
-
the enzyme catalyzes the first step in L-lactate catabolism
metabolism
-
L-lactate dehydrogenase is an important enzyme involved in the last step of glycolysis that catalyzes the reversible conversion of pyruvate to L-lactate with the simultaneous oxidation of NADH to NAD+
physiological function
-
the enzyme catalyzes the stereospecific conversion of lactate to pyruvate and converts NAD+ to NADH, which is an important way of regenerating NAD+, enabling the continuation of glycolysis
physiological function
-
although Ldh-2 contributes to lactate production, Ldh-1 plays the major role in energy metabolism in Enterococcus faecalis
physiological function
-
LDH-A deficiency causes myoglobinuria
physiological function
-
the parasite's ATP production is almost completely dependent on the glucose metabolism and the glycolytic pathway, that is absent in normal human host cells, overview. PfLDH plays the essential role in NAD+ regenration needed for the continuity of the glycolytic cycle
physiological function
-
LADH-A is a key enzyme that couples L-lactate production to reoxidation of NADH formed during glycolysis
metabolism
Aggregatibacter actinomycetemcomitans HK1651 and VT1169
-
the enzyme catalyzes the first step in L-lactate catabolism
-
additional information
-
the ldh-1 mutants detoxifies excess pyruvate by converting it to acetoin
additional information
-
the enzyme is involved in development of cancer, especially of hypoxic cancer cells, since the cancer cells relay on LDH-A for the energy supply. The glycolytic phenotype is responsible for the tumorigenicity of hypoxic cells
additional information
-
ldhA expression is primarily repressed by SugR in the absence of sugar. In the presence of sugar, SugR-mediated repression of ldhA is alleviated, and ldhA expression is additionally enhanced by LldR inactivation in response to L-lactate produced by LdhA
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-lactate + 3-acetyl pyridine adenine dinucleotide
pyruvate + reduced 3-acetyl pyridine adenine dinucleotide
show the reaction diagram
-
assay is based on reduction of 3-acetyl pyridine adenine dinucleotide that is specific for PfLDH, which allows the distinction of PfLDH from that of the host erythrocyte
-
-
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
Q27743
-
-
-
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
Q6JH30
-
-
-
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
-
-
-
-
?
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
-
-, L-lactate transport and metabolism, regulation and localization of enzyme participating in the pathway, overview
-
-
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
Bacillus subtilis BS35
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
?
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
?
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
P00344
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
?
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Pontonia pinnophylax
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-, Q0GND9
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-, Q0GND8
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
the maximal velocity of lactate oxidation is about 10% of pyruvate reduction
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Molinema dessetae
-
pyruvate reduction is the favored reaction
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
inactive towards D-lactate
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
poor reaction
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
involved in glycolysis
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
P00344
wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+
-
-
?
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
P0C2T6
LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
mitochondrial metabolism of L-lactate plays a role in the response of potato to hypoxic stress
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
the astrocytic cell line CCF-STTG1 is able to consume lactate to generate ATP via oxidative phosphorylation, overview
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Pontonia pinnophylax
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, overview
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
P0C2T6
LDH posseses a catalytic His171 residue
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
mutant I12V/R81Q/M85E/G210A/V214I, residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
P00344
residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Lactococcus lactis 760
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Thermus caldophilus GK24
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Mus musculus AKR
-
-
-
-
r
(S)-lactate + NADP+
pyruvate + NADPH + H+
show the reaction diagram
P00344
wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+
-
-
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
-
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
-
r
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
-
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
-
3% of the activity with pyruvate
-
-
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
show the reaction diagram
-
107% of the activity with pyruvate
-
-
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
show the reaction diagram
-
79.6% of the activity with pyruvate
-
-
?
2-oxopentanoate + NADH
2-hydroxypentanoate + NAD+
show the reaction diagram
-
125% of the activity with pyruvate
-
-
?
2-oxovalerate + NADH
2-hydroxyvalerate + NAD+
show the reaction diagram
-
-
-
-
r
3-fluoropyruvate + NADH
?
show the reaction diagram
-
-
-
-
-
3-fluoropyruvate + NADH
?
show the reaction diagram
-
-
-
-
?
3-fluoropyruvate + NADH
?
show the reaction diagram
-
33.6% of the activity with pyruvate
-
-
?
3-methyl-2-oxobutanoate + NADH
2-hydroxy-3-methylbutanoate + NAD+
show the reaction diagram
-
28.5% of the activity with pyruvate
-
-
?
3-methyl-2-oxopentanoate + NADH
2-hydroxy-3-methylpentanoate + NAD+
show the reaction diagram
-
5.3% of the activity with pyruvate
-
-
?
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
show the reaction diagram
-
-
-
-
?
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
show the reaction diagram
-
39% of the activity with pyruvate
-
-
?
bromopyruvate + NADH
5-bromo-2-hydroxypropanoate + NAD+
show the reaction diagram
-
-
-
-
?
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
-
-
-
?
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH
2,3-dihydroxypropanoate + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH
2,3-dihydroxypropanoate + NAD+
show the reaction diagram
-
-
-
-
?
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
-
the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
-
-
r
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
-
LDH binds its substrate via the formation of a LDH/NADH-substrate encounter complex through a select-fit mechanism, whereby only a minority population of LDH/NADH is binding-competent, molecular dynamics calculations to explore the variations in structure accessible to the binary complex and binding-competent structures, active site interactions in the ternary complex, overview
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
B1A4R6, -
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
B7XH73, C6L1K8, -
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
an encounter complex is formed between LDH-NAD+ and lactate, collapses to form a chemically active species and loop closure/opening steps
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
no activity with D-lactate
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
the wild-type V583 strain converts glucose almost exclusively to L-lactate under anaerobic conditions
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
amino acid residues involved in substrate and cofactor binding are Arg109, Asp168, Arg171, and His195
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
no activity with D-lactate, activity of recombinant His6-tagged LctD is determined in the presence of the electron carriers 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide and phenazine methosulfate
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Aggregatibacter actinomycetemcomitans HK1651 and VT1169
-
no activity with D-lactate, no activity with D-lactate, activity of recombinant His6-tagged LctD is determined in the presence of the electron carriers 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide and phenazine methosulfate
-
-
r
oxamate + NADH
?
show the reaction diagram
-
two distinct active site LDH/NADH-oxamate complex conformations, a major populated structure wherein all significant hydrogen-bonding patterns are formed at the active site between protein and bound ligand necessary for the catalytically productive Michaelis complex and, a minor structure in a configuration of the active site that is unfavorable to carry out catalyzed chemistry. This latter structure likely simulates a dead-end complex in the reaction mixture. The evolution of the encounter complex between LDH/NADH and oxamate collapses via a branched reaction pathway to form the major and minor bound species. Once the encounter complex is formed between LDH/NADH and substrate, the ternary protein-ligand complex appears to fold to form a compact productive complex in an all or nothing like fashion with all the important molecular interactions coming together at the same time
-
-
?
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
show the reaction diagram
-
-
-
-
?
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
show the reaction diagram
-
28% of the activity with pyruvate
-
-
?
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH
?
show the reaction diagram
-
-
-
-
?
pyruvate + NADH
L-lactate + NAD+
show the reaction diagram
P56512
in the cell lysate of the host strain, L-LDH activity is hardly detectable during cultivation. As a consequence of transformation, the ratio between D- and L-isomers is changed due to the increment of L-lactate and the decrement of D-lactate, but there are no significant differences in total lactate concentration between the host and transformant cells. In the transformant harboring pLC18lld, L-LDH activity is detected during the entire cultivation period. L-LDH activity increases rapidly to the maximum level (0.18 U/mg protein) between the early- and mid-exponential growth phases (0-8 h), and decreases thereafter during the stationary phase
-
-
?
pyruvate + NADH
L-lactate + NAD+
show the reaction diagram
-
lactate yield is increased in the pyruvate decarboxylase 1/alcohol dehydrogenase 1 double mutant compared with that in the single pyruvate decarboxylase 1 mutant
-
-
?
pyruvate + NADH
L-lactate + NAD+
show the reaction diagram
Q27797, -
LDH1 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH1 enhances the parasite's ability to differentiate
-
-
?
pyruvate + NADH
L-lactate + NAD+
show the reaction diagram
Q27797, -
LDH2 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH2 enhances the parasite's ability to differentiate
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Q27743
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Streptococcus mitior
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
O13276
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
O13278, -
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
O13277, -
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Q6JH30
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
P90613
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Agama stellio stellio
-
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-, Q9GT92
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-, Q7Z0X7
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Molinema dessetae
-
pyruvate reduction is the favored reaction
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
the maximal velocity of lactate oxidation is only 10% of pyruvate reduction
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
P90613
terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase have a functional interaction that can affect NAD+/NADH metabolism and glycolysis in living cells
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
inactivation of the lshL does not abolish the production of L-lactate, but the lactate final concentration decreases about 25% compared to the wild-type, suggesting the presence of at least a second L-Ldh
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
study of the dependence of the chemical reaction mechanism of lactate dehydrogenase on the protonation state of titratable residues and on the level of the quantum mechanical description by means of hybrid quantum-mechanical methods
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Q5SJA1
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-, P50933
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
O93541
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
LdhB enzymes from type-I isolate NRRL 395 and type-II isolate 99-880 show reductive LDH activity, but no oxidative LDH activity, overview
-
-
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
the nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity, L-lactate production allows Staphylococcus aureus to maintain redox homeostasis during nitrosative stress and is essential for virulence, regulation, overview
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Q5SJA1
active site structure and substrate binding, overview
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-, P50933
active site structure and substrate binding, overview
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
O93541
active site structure and substrate binding, overview
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
LdhB
-
-
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Lactococcus lactis 760
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Thermus caldophilus GK24
-
-
-
-
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
last step in anaerobic glycolysis
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
enzyme activity increases in response to infection by black-rot fungus but decreases in response to cutting
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
key enzyme in anaerobic metabolism which converts pyruvate to lactate
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
an encounter complex is formed between LDH-NADH and pyruvate, collapses to form a chemically active species and loop closure/opening steps
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
Thermus caldophilus GK24
-
-
-
-
?
pyruvate + NADH + H+
lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
lactate + NAD+
show the reaction diagram
-
-
-
-
-
pyruvate + NADH + H+
lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
lactate + NAD+
show the reaction diagram
Rhizopus delemar, Rhizopus oryzae NRRL 395, Rhizopus delemar RA 99-880
-
-
-
-
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
show the reaction diagram
-
-
-
-
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
show the reaction diagram
-
20% of the activity with NADH
-
-
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
show the reaction diagram
-
34% of the activity with NADH
-
-
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
show the reaction diagram
-
15% of the activity with NADH
-
-
?
pyruvate ethyl ester + NADH
2-hydroxypropanoate ethyl ester
show the reaction diagram
-
-
-
-
?
pyruvate methyl ester + NADH
2-hydroxypropanoate methyl ester
show the reaction diagram
-
-
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Thermoanaerobacter ethanolicus JW200
B1A4R6
-
-
-
r
additional information
?
-
-
in addition of lactate dehydrogenase activity, the epsilon-crystallin also possesses the enzymatic activity of malate dehydrogenase
-
-
-
additional information
?
-
-
the enzyme is unlikely to catalyze lactate oxidation at an appreciable rate under physiological conditions
-
-
-
additional information
?
-
-
the enzyme is a component of the system regulating the cellular pH and/or controlling the concentration of reducing equivalents in the cytoplasm of leaf cells
-
-
-
additional information
?
-
-
Bacillus subtilis fermentation pathways, overview
-
-
-
additional information
?
-
-
exogenous L-lactate enters mitochondria by a proton-compensated process, is converted to pyruvate, which is exported to the cytoplasm via a non-energy-competent L-lactate-pyruvate shuttle, overview
-
-
-
additional information
?
-
P0C2T6
intracellular isozyme regulation in relation to pH, overview
-
-
-
additional information
?
-
-
LDH is critically implicated in tumor growth
-
-
-
additional information
?
-
-
LDH is essential for continuous glycolysis necessary for accelerated tumor growth and increased LDH activity occurs already in grade 1 EC carcinomas
-
-
-
additional information
?
-
-, Q0GND9
amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
-
-
-
additional information
?
-
-, Q0GND8
amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
-
-
-
additional information
?
-
-
Plasmodium falciparum lactate dehydrogenase has L-malate dehydrogenase activity, which plays a role in the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
the enzyme also utilizes NADP(H)
-
-
-
additional information
?
-
-
the heart-type isozyme interacts with liposomes made of acidic phospholipids, such as phosphatidylserine or cardiolipin, most effectively at low pH close to the isoelectric point of the isozyme of pH 5.5 strongly involving the enzyme's NADH-cofactor binding site, no interaction with liposomes of the muscle-type isozyme, overview
-
-
-
additional information
?
-
-
the formation of lactate in satellite gliocytes is induced by nicotinic cholinergic synapses directly involved in neuron-glial interactions and in controlling the activity of the LDH enzyme system in sympathetic neurons
-
-
-
additional information
?
-
Mus musculus AKR
-
LDH is critically implicated in tumor growth
-
-
-
additional information
?
-
Bacillus subtilis BS35
-
Bacillus subtilis fermentation pathways, overview, the enzyme also utilizes NADP(H)
-
-
-
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
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
-
L-lactate transport and metabolism, regulation and localization of enzyme participating in the pathway, overview
-
-
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
Bacillus subtilis BS35
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
P00344
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Pontonia pinnophylax
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-, Q0GND9
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-, Q0GND8
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
involved in glycolysis
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
P0C2T6
LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
mitochondrial metabolism of L-lactate plays a role in the response of potato to hypoxic stress
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
the astrocytic cell line CCF-STTG1 is able to consume lactate to generate ATP via oxidative phosphorylation, overview
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Mus musculus AKR
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
-
the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
B1A4R6, -
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
B7XH73, C6L1K8, -
-
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
no activity with D-lactate
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
the wild-type V583 strain converts glucose almost exclusively to L-lactate under anaerobic conditions
-
-
r
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Aggregatibacter actinomycetemcomitans HK1651 and VT1169
-
no activity with D-lactate
-
-
r
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
P90613
terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase have a functional interaction that can affect NAD+/NADH metabolism and glycolysis in living cells
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
inactivation of the lshL does not abolish the production of L-lactate, but the lactate final concentration decreases about 25% compared to the wild-type, suggesting the presence of at least a second L-Ldh
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
Q5SJA1
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-, P50933
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
O93541
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
-
-
r
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
LdhB enzymes from type-I isolate NRRL 395 and type-II isolate 99-880 show reductive LDH activity, but no oxidative LDH activity, overview
-
-
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
the nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity, L-lactate production allows Staphylococcus aureus to maintain redox homeostasis during nitrosative stress and is essential for virulence, regulation, overview
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
last step in anaerobic glycolysis
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
enzyme activity increases in response to infection by black-rot fungus but decreases in response to cutting
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
key enzyme in anaerobic metabolism which converts pyruvate to lactate
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
Thermus caldophilus GK24
-
-
-
-
?
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
Thermoanaerobacter ethanolicus JW200
B1A4R6
-
-
-
r
additional information
?
-
-
the enzyme is unlikely to catalyze lactate oxidation at an appreciable rate under physiological conditions
-
-
-
additional information
?
-
-
the enzyme is a component of the system regulating the cellular pH and/or controlling the concentration of reducing equivalents in the cytoplasm of leaf cells
-
-
-
additional information
?
-
-
Bacillus subtilis fermentation pathways, overview
-
-
-
additional information
?
-
-
exogenous L-lactate enters mitochondria by a proton-compensated process, is converted to pyruvate, which is exported to the cytoplasm via a non-energy-competent L-lactate-pyruvate shuttle, overview
-
-
-
additional information
?
-
P0C2T6
intracellular isozyme regulation in relation to pH, overview
-
-
-
additional information
?
-
-
LDH is critically implicated in tumor growth
-
-
-
additional information
?
-
-
LDH is essential for continuous glycolysis necessary for accelerated tumor growth and increased LDH activity occurs already in grade 1 EC carcinomas
-
-
-
additional information
?
-
Mus musculus AKR
-
LDH is critically implicated in tumor growth
-
-
-
additional information
?
-
Bacillus subtilis BS35
-
Bacillus subtilis fermentation pathways, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
wild-type and S163 L mutant protein bind 3-acetylpyridine adenine dinucleotide more tightly than they bind NADH
3-acetylpyridine adenine dinucleotide
-
alternative coenzyme
3-acetylpyridine adenine dinucleotide
-
assay is based on reduction of 3-acetyl pyridine adenine dinucleotide that is specific for PfLDH, which allows the distinction of PfLDH from that of the host erythrocyte
beta-NAD+
-
-
beta-NADH
-
-
NAD+
-
coenzyme
NAD+
Molinema dessetae
-
coenzyme
NAD+
-
coenzyme
NAD+
Agama stellio stellio
-
-
NAD+
P00344
wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+
NAD+
-
the coenzyme is in an open conformation and the adenine ribose ring of it is surrounded by Asp 38, Val 39, and Gly 99. Asp 38 and Gly 99 give some specificity to the adenine orientation, overview
NAD+
Q0GND8
-
NAD+
Pontonia pinnophylax
-
-
NAD+
-
binding structure, overview
NAD+
B7XH73, C6L1K8, -
;
NADH
-
coenzyme
NADH
Molinema dessetae
-
coenzyme
NADH
-
coenzyme
NADH
O13276
coenzyme
NADH
O13277, -
coenzyme
NADH
O13278, -
coenzyme
NADH
Agama stellio stellio
-
-
NADH
Q7Z0X7
-
NADH
-
the coenzyme is in an open conformation and the adenine ribose ring of it is surrounded by Asp 38, Val 39, and Gly 99. Asp 38 and Gly 99 give some specificity to the adenine orientation, Asp 38 is an important residue in stabilizing NADH binding, overview
NADH
-
the NADH-cofactor binding site of heart LDH is involved in the interaction of the isozyme with liposomes made of acidic phospholipids, overview
NADH
Q0GND8
-
NADH
P0C2T6
NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH did not change with pH
NADH
Pontonia pinnophylax
-
-
NADH
B7XH73, C6L1K8, -
;
NADP+
P00344
wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+
NADPH
-
coenzyme
nicotinamide hypoxanthine dinucleotide
-
alternative coenzyme
thio-NAD+
-
alternative coenzyme
FMN
-
contains non-covalently bound FMN as prosthetic group
additional information
-
the enzyme also utilizes both NAD(H) and NADP(H)
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
stimulation is as effective as with Mn2+, Co2+ and Cd2+
Ca2+
-
50% of the stimulation with Mn2+, Co2+ or Cd2+, higher concentrations required
Ca2+
-
increases activity
Ca2+
-
1 mM, almost 2fold stimulation
Co2+
-
activation involves association of enzyme dimers, followed by ligand binding; stimulation
Co2+
-
increases activity
Fe2+
-
increases activity
Mg2+
-
20-30 mM, 10% increase in activity
Mn2+
-
stimulation
Mn2+
-
no effect
Zn2+
-
1 mM, almost 2fold stimulation
Mn2+
-
increases activity
additional information
B1A4R6, -
not or poorly affected by 1 mM of EDTA, ATP, Mg2+, Co2+, Ca2+, Mn2+, and Ni2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
-
-
(benzylamino)(oxo)acetic acid
-
-
(heptylamino)(oxo)acetic acid
-
-
(hexylamino)(oxo)acetic acid
-
-
(nonylamino)(oxo)acetic acid
-
-
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
-
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
1,6-dibromo-2-hydroxynaphthalene 3-carboxylic acid
-
0.31 mM
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
-
2,3-dihydroxy-4,6,7-trimethylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6,7-dimethyl-4-propylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(2-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(3-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(4-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,6-naphthalene disulfonic acid
-
IC50: 21 mM
2,6-naphthalenedicarboxalic acid
-
IC50: 5.1 mM
2-mercaptoethanol
B1A4R6, -
10% inhibition at 1 mM
3,5-dihydroxy 2-naphthoic acid
-
IC50: 1.7 mM
3,5-dihydroxynaphthalene-2-carboxylic acid
-
-
3,7-dihydroxy naphthalene-2-carboxylic acid
-
IC50: 2.4 mM
3,7-dihydroxynaphthalene-2-carboxylic acid
-
-
3-(3-nitro-4-pyridyl)pyruvate
-
-
-
3-(3-nitropyridin-4-yl)-2-oxopropanoic acid
-
-
3-acetylpyridine adenine dinucleotide
-
the enzyme exhibits characteristic reduced substrate inhibition and enhanced kcat
3-Aminopyridine adenine dinucleotide
-
competitive versus NAD+ and noncompetitive versus L-lactate
3-Fluoropyruvate
-
-
3-hydroxy-1,2-oxazole-4-carboxylic acid
-
-
3-hydroxy-1-oxaspiro[4.5]dec-3-en-2-one
-
-
3-hydroxy-2-oxo-1-oxaspiro[4,5]-dec-3-ene
-
-
-
3-nitropropionate
-
-
3-phosphoglycerate
-
-
4,7-dibromo-3-hydroxynaphthalene-2-carboxylic acid
-
-
4-(ethylcarbamoyl)benzoic acid
-
-
4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
-
trophozoites are the most susceptible stages to exposure to 4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
-
-
4-hydroxy-1,2,5-thiadiazole-3-carboxylic acid
-
-
4-hydroxy-1,2-oxazole-3-carboxylic acid
-
-
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
-
6,6'-Dithiodinicotinic acid
-
IC50: 6.6 mM
6-phosphogluconate
-
-
7-(4-chlorobenzyl)-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
-
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-(phenylamino)naphthalene-1-sulfonic acid
-
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-anilino-1-naphthalene sulfonic acid
-
IC50: 0.52 mM
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
-
ADP
-
competitive with NADH
ADP
-
isoenzyme I and II, inhibition is reduced by MgCl2
Ag+
B1A4R6, -
complete inhibition at 1 mM
Alpha-NAD+
-
noncompetitive inhibitor versus beta-NAD+
AMP
-
isoenzyme I and II, inhibition is reduced by MgCl2
ascorbate
-
at concentrations normally found in tissue. It is proposed that ascorbate facilitates the storage of glycogen in muscle at rest by inhibiting glycolysis. Aldolase and muscle G-actin protect and reverse inhibition
ATP
-
at neutral or alkaline pH ATP behaves as a weak competitive inhibitor, potent inhibitor at acid pH values
ATP
-
isoenzyme I and II, inhibition is reduced by MgCl2
ATP
-
competitive with respect to NADH at pH 7.0 and at pH 6.2
ATP
-
10 mM, 40% loss of activity
bis(acetatato-kO)(biphenyl-2,2'-diyl-k2C2,C2')copper
-
-
bis(acetatato-kO)(biphenyl-2,2'-diyl-k2C2,C2')zinc
-
-
cardiolipin
-
IC50: 0.00005 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
Cd2+
-
at high concentration
Cd2+
-
0.1 mM and 1.0 mM, weak inhibition
Chloroquine
-
IC50: 5.5 mM
citrate/phosphate buffer
-
at pH 5.4
-
Co2+
-
0.1 mM and 1.0 mM, weak inhibition
Co2+
Agama stellio stellio
-
both directions
Cu2+
-
0.1 mM and 1.0 mM, weak inhibition
Cu2+
Agama stellio stellio
-
both directions
Cu2+
B1A4R6, -
complete inhibition at 1 mM
Cu[Ac]2[2,2'-bipyridine]
-
analysis of interaction with the LDH isozymes and their modulation, significantly inhibits LDH in liver, kidney, heart, spleen, brain and skeletal muscle tissues, overview
D-fructose 1,6-bisphosphate
-
slightly inhibits activity of hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
D-fructose-1,6-diphosphate
-
5 mM, 25% loss of activity
D-lactate
-
dead-end inhibitor, competitive inhibitor versus L-lactate
dicholesteroyl diselenide
-
inhibition of different isoforms of lactate dehydrogenase by dicholesteroyl diselenide possibly involves the modification of the thiol groups at the NAD+ binding site of the enzyme. Exerts profound concentration dependent inhibitory effect on the activity of renal LDH. Inhibitory effect on hepatic LDH is markedly pronounced at 2, 4, 8 and 10 microM. Strongly inhibits cardiac LDH activity when NAD+ is omitted from the pre-incubating medium than when lactate is absent from the pre-incubating medium, significantly inhibits the enzyme activity at 1, 2, 4, and 8 microM
dihydroxyacetone phosphate
-
-
diphenyl diselenide
-
inhibition of different isoforms of lactate dehydrogenase by diphenyl diselenide possibly involves the modification of the thiol groups at the NAD+ binding site of the enzyme. Inhibitory effect on hepatic LDH is markedly different at 10 microM. Markedly inhibits cardiac LDH activity at 8 and 10 microM
DTT
B1A4R6, -
19% inhibition at 1 mM
ethyl 3-(3-cyano-4-pyridyl)pyruvate
-
-
-
ethyl 3-(3-cyanopyridin-4-yl)-2-oxopropanoate
-
-
Fe2+
B1A4R6, -
74% inhibition at 1 mM
-
Fe3+
B1A4R6, -
complete inhibition at 1 mM
-
fructose 1,6-bisphosphate
-
10 mM significantly inhibits LDHB by 23% in a non-competitive manner. Level of inhibition seems to be even more pronounced at pH 6.2, compared to the optimal pH 6.8. At the more acidic pH and in the presence of 10 mM, LDHB shows a 42% decrease in activity
fructose 1,6-bisphosphate
Rhizopus oryzae NRRL 395
-
10 mM significantly inhibits LDHA abd LDHB (by 86%) in a non-competitive manner. Level of inhibition seems to be even more pronounced at pH 6.2, compared to the optimal pH 6.8. At the more acidic pH and in the presence of 10 mM, there is almost a 97% decrease in activity for LDHB
fructose 1,6-diphosphate
-
activation at low concentrations, inhibition at high concentrations
fructose 1,6-diphosphate
-
-
glucose 6-phosphate
-
-
glutamate
Agama stellio stellio
-
both directions
gossylic nitrile 1,1'-diacetate
Q27743
-
gossylic nitrile 1,1'-diacetate
-
-
gossylic nitrile 1,1'-diacetate
Q6JH30
-
gossypol
Q6JH30
-
gossypol
Q7Z0X7
competitive with NADH
gossypol
-
a polyphenolic binaphthyl disesquiterpene from Gossypium sp.
gossypol lactone
Q27743
-
gossypol lactone
Q6JH30
-
Hg2+
Molinema dessetae
-
-
iodoacetate
-
no effect
iodoacetate
Molinema dessetae
-
-
Isocitrate
-
-
L-lactate
-
substrate inhibition is uncompetitive
L-lactate
-
product inhibition
Lactate analogs
-
-
-
MES buffer
-
-
-
Methylmalonate
-
-
Methylmalonate
-
IC50: 4.6 mM (enzyme from brain), 4.6 mM (enzyme from liver)
Mg2+
Agama stellio stellio
-
both directions
Mn2+
-
at low pH-values
NaCl
-
2 M, 36% loss of activity
NAD+
-
product inhibition
NAD+
-
competitive with respect to NADH, reduction of pyruvate
NAD+
-
40 mM, complete loss of activity
NAD+
-
substrate inhibition due to an abortive NAD+-pyruvate complex reducing the steady state concentration of functional LDH
NAD+
-
product inhibition
NAD+
B1A4R6, -
7% inhibition at 0.5 mM
NADH
-
competitive with respect to NAD+
naphthalene-2,6-dicarboxylic acid
-
-
naphthalene-2,6-disulfonic acid
-
-
nicotinic acid adenine dinucleotide
-
competitive versus NAD+ and noncompetitive versus L-lactate
o-phthalaldehyde
-
modification not only results in inactivation of the enzyme, but also leads to the enzymes dissociation and partial unfolding
oxalate
Molinema dessetae
-
noncompetitive with pyruvate, competitive with lactate
oxalate
Agama stellio stellio
-
both directions
oxalate
-
0.5 mM, 28% inhibition
oxaloacetate
-
-
Oxamate
Molinema dessetae
-
competitive with pyruvate, noncompetitive with lactate
Oxamate
-
dead-end inhibitor, competitive inhibitor versus pyruvate
Oxamate
-
0.5 mM, 41% inhibition
Oxamate
-
specific inhibitor of L-LDH
Oxamate
-
-
oxo(pentadecylamino)acetic acid
-
-
oxo(phenylamino)acetic acid
-
-
oxo[(2-phenylethyl)amino]acetic acid
-
-
oxo[(2-phenylpropyl)amino]acetic acid
-
-
oxo[(3-phenylpropyl)amino]acetic acid
-
-
oxo[(4-phenylbutan-2-yl)amino]acetic acid
-
-
oxo[(4-phenylbutyl)amino]acetic acid
-
-
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
-
-
oxo[[1-(5,6,7,8-tetrahydronaphthalen-1-yl)ethyl]amino]acetic acid
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
Molinema dessetae
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
slight
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
phosphate
-
slight activation of non-activated enzyme, inhibition of fructose 1,6-diphosphate activated enzyme
phosphate
P0C2T6
phosphate acts as a strong activator of LDHB
phosphatidylserine
-
IC50: 0.0013 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
pyruvate
-
strong substrate inhibition at high concentrations, fructose 1,6-diphosphate activated enzyme
pyruvate
-
above 20 mM
pyruvate
-
substrate inhibition in wild type enzyme, lower substrate inhibition in mutant S163L
pyruvate
-
at high concentrations
pyruvate
-
above 0.3 mM
pyruvate
-
substrate inhibition is uncompetitive
pyruvate
-
substrate inhibition
pyruvate
-
substrate inhibition
pyruvate
-
substrate inhibition
pyruvate
-
substrate inhibition due to an abortive NAD+-pyruvate complex reducing the steady state concentration of functional LDH
pyruvate
-
the enzyme shows substrate inhibition, inhibition mechanism, overview
SDS
B1A4R6, -
complete inhibition at 0.1%
Sodium phosphate
-
-
Tartronate
-
dead-end inhibitor, competitive inhibitor versus L-lactate
Thionicotinamide adenine dinucleotide
-
competitive versus NAD+ and noncompetitive versus L-lactate
Tris/maleate buffer
-
at pH 5.4
-
Urea
Pontonia pinnophylax
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, LDH is more sensitive than MDH, overview
Zn2+
B1A4R6, -
complete inhibition at 1 mM
Zn[Ac]2[2,2'-bipyridine]
-
analysis of interaction with the LDH isozymes and their modulation, significantly inhibits LDH in liver, kidney, and heart, but not in spleen, brain and skeletal muscle tissues, overview
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
-
-
[(2-methoxyethyl)amino](oxo)acetic acid
-
-
[(3,3-diphenylpropyl)amino](oxo)acetic acid
-
-
[(3-methoxypropyl)amino](oxo)acetic acid
-
-
[(3-methylbutyl)amino](oxo)acetic acid
-
-
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
-
-
[(4-chlorobenzyl)amino](oxo)acetic acid
-
-
[(4-methylbenzyl)amino](oxo)acetic acid
-
-
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
-
-
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
-
-
[benzyl(methyl)amino](oxo)acetic acid
-
-
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
-
-
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
-
-
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
-
-
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
-
-
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
-
-
Mn2+
Agama stellio stellio
-
both directions
additional information
-
lack of substrate inhibition
-
additional information
-
loss of LDH activity with increasing pressure and time treatment due to the combined effects of denaturation and aggregation, overview
-
additional information
-
NADH, NAD+, ATP, ADP, AMP, and pyruvate inhibit the interaction of the heart-type isozyme with acidic phospholipid liposomes, potency in descending order. NADP+, GTP, CTP, UTP and lactate are ineffective, overview
-
additional information
-
inhibition mechanism, the plasmodial enzyme possesses a five-residue insertion in the substrate-specificity loop and exhibits less marked substrate inhibition than its mammalian counterparts, overview
-
additional information
-
no inhibition by nitric oxide
-
additional information
-
short-term storage in Krebs-Henseleit buffer for 24 h at 4C does not affect LDH activity, but a 42% decline occurs at 23C. After 48 h, activity declines 11% at 4C and 98% at 23C. Frozen storage results in a 40% loss at -80C and a 79% loss at -20C
-
additional information
-
blockade of nicotinic cholinoreceptors significantly decreases total LDH activity and H- and M-isoform activities in neurons. LDH activity decreases by 41.5% and 71% in conditions of partial and complete blockade, respectively. Decreases in H-isoform activity are by 25% in partial blockade and 42% in complete blockade and decreases in M-isoform activity are by 35% and 62%. In partial and complete blockade, the activity of LDH and its H- and M-isoforms decrease significantly in proportion to the number of blocked nicotinic cholinoreceptors. In satellite gliocytes, increases in the extent of blockade are associated with decreases in the activity only of the M-isoform (by 43% in partial blockade and 55.5% in complete blockade), while the activity of the H-isoform does not change. In partial blockade, the LDH isoenzyme profile of satellite gliocytes shifts towards the neuronal isoform, while in complete blockade there is no difference from the LDH isoenzyme profile of intact neurons
-
additional information
-
the Aggregatibacter actinomycetemcomitans L-lactate dehydrogenase, unlike homologous enzymes, is not feedback inhibited by pyruvate, pyruvate is a poor inhibitor of L-lactate dehydrogenase activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-glycerophosphate
-
activation
3-phosphoglycerate
-
activation
5-phosphoribosyl 1-diphosphate
-
activates
D-fructose 1,6-bisphosphate
-
activates wild-type enzyme
D-fructose 1,6-bisphosphate
-
activates the pyruvate reduction
D-fructose 1,6-bisphosphate
P0C2T6
activation constants of isozymes at different pH values, overview
D-fructose 1,6-bisphosphate
B1A4R6, -
allosteric
D-fructose 1,6-diphosphate
P00344
activates wild-type enzyme and mutant enzymes F16Q/I37K/D38SC81S/N85R and F16Q/C81S/N85R
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate; L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate; L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate; L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
Streptococcus milleri, Streptococcus mitior
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate; L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate; L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
dependent on
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
concentration required for 50% maximal activity is about 0.15 mM; L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
not dependent on fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate; maximal activation is about: 0.03 mM at pH 6.0, 0.2 mM at pH 7.1, 2 mM at pH 8.0 and 7 mM at pH 9.0
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
binding of fructose 1,6-diphosphate induces a conformational change in the enzyme which leads to increased activity, without association of enzyme subunits or dimers; L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
binding of fructose 1,6-diphosphate induces a conformational change in the enzyme, producing a form with reduced protein fluorescence and increased activity towards pyruvate reduction; L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
at pH 7.5 lactate dehydrogenase activity is absent without fructose 1,6-diphosphate, from pH 5.0 to pH 7.0 lactate dehydrogenase is present without fructose 1,6-diphosphate but is greater in the presence of the activator; L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 2,6-diphosphate
-
activates
glucose 1,6-diphosphate
-
activates
phosphate
-
slight activation of not activated enzyme, inhibition of fructose 1,6-diphosphate activated enzyme
tagatose 1,6-diphosphate
-
stimulates
Triton X-100
B1A4R6, -
23% activation at 0.1%
Urea
B1A4R6, -
9% activation at 0.1%
glucose 1,6-diphosphate
-
activates
additional information
O93541
thermodynamic activation parameters, overview
-
additional information
-, P50933
thermodynamic activation parameters, overview
-
additional information
Q5SJA1
thermodynamic activation parameters, overview
-
additional information
-
the enzyme is induced by nitric aoxide
-
additional information
Rhizopus delemar, Rhizopus oryzae NRRL 395
-
presence of an amino terminal fusion with a small ubiquitin-related modifier, SUMO, increases the oxidative activity per micromol protein by more than 100fold, while having little effect on the reductive LDH activity
-
additional information
-
hearts perfused with Krebs-Henseleit buffer, subjected to 30 min of global ischemia followed by normoxic reperfusion, which causes tissue damage and elevate LDH release
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.083
-
(S)-Lactate
-
-
0.515
-
(S)-Lactate
-
15C, pH 8
0.517
-
(S)-Lactate
-
20C, pH 8
0.537
-
(S)-Lactate
-
20C, pH 7.4
0.541
-
(S)-Lactate
-
15C, pH 8
0.567
-
(S)-Lactate
-
15C, pH 7.4
0.616
-
(S)-Lactate
-
20C, pH 8
0.62
-
(S)-Lactate
-
15C, pH 7.4
0.641
-
(S)-Lactate
-
20C, pH 7.4
0.735
-
(S)-Lactate
-
15C, pH 7
0.803
-
(S)-Lactate
-
20C, pH 7
0.822
-
(S)-Lactate
-
30C, pH 7
0.862
-
(S)-Lactate
-
15C, pH 7
0.909
-
(S)-Lactate
-
30C, pH 7
0.94
-
(S)-Lactate
-
30C, pH 7.4
0.966
-
(S)-Lactate
-
20C, pH 7
1.016
-
(S)-Lactate
-
30C, pH 7.4
1.191
-
(S)-Lactate
-
30C, pH 8
1.33
-
(S)-Lactate
-
30C, pH 7
1.79
-
(S)-Lactate
-
-
2.5
-
(S)-Lactate
Molinema dessetae
-
-
8.1
-
(S)-Lactate
Agama stellio stellio
-
pH 7.5, 25C
10.2
-
(S)-Lactate
Q6JH30
pH 9.2, 25C
11.3
-
(S)-Lactate
-
pH 9.2, 25C
12
-
(S)-Lactate
Q27743
pH 9.2, 25C
13
-
(S)-Lactate
-
-
17
-
(S)-Lactate
-
pH 8.2, isoenzyme II
22
-
(S)-Lactate
-
pH 8.8, isoenzyme I
30
-
(S)-Lactate
-
-
55
-
(S)-Lactate
-
-
67
-
(S)-Lactate
-
-
90.04
-
(S)-Lactate
-
-
93
-
(S)-Lactate
-
pH 9.2, 25C
100
-
(S)-Lactate
-
-
100
-
(S)-Lactate
-
in presence of 1 mM fructose 1,6-diphosphate
109
-
(S)-Lactate
-
-
280
-
(S)-Lactate
-
-
360
-
(S)-Lactate
-
-
420
-
(S)-Lactate
-
-
1100
-
(S)-Lactate
-
-
77
-
2-oxobutanoate
-
-
0.6
-
2-oxobutyrate
-
pH 7.5
0.116
-
2-oxovalerate
-
pH 7.5
0.123
-
3-acetylpyridine adenine dinucleotide
Q27743
pH 9.2, 25C
0.168
-
3-acetylpyridine adenine dinucleotide
-
pH 9.2, 25C
0.182
-
3-acetylpyridine adenine dinucleotide
Q6JH30
pH 9.2, 25C
0.408
-
3-acetylpyridine adenine dinucleotide
-
pH 9.2, 25C
25
-
glyoxylate
-
-
8
-
Hydroxypyruvate
-
-
0.047
-
L-lactate
-
pH 7.5
0.152
-
L-lactate
-
pH not specified in the publication, temperature not specified in the publication
60
-
L-lactate
B1A4R6, -
pH 7.0, 70C, recombinant enzyme
3.3
-
Lactate
-
-
10.26
-
Lactate
-
-
47.4
-
Lactate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 3.75 mM NAD+
0.0081
-
NAD+
P00344
25C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate
0.02
-
NAD+
Agama stellio stellio
-
pH 7.5, 25C
0.074
-
NAD+
-
-
0.086
-
NAD+
Q27743
pH 9.2, 25C
0.105
-
NAD+
P00344
25C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate
0.143
-
NAD+
-
pH 9.2, 25C
0.155
-
NAD+
Q6JH30
pH 9.2, 25C
0.18
-
NAD+
Molinema dessetae
-
-
0.18
-
NAD+
-
pH 7.5
0.311
-
NAD+
-
pH 9.2, 25C
0.95
-
NAD+
-
pH 8.2, isoenzyme II
2.4
-
NAD+
-
in presence of 1.0 mM fructose 1,6-diphosphate
2.4
-
NAD+
-
in presence of 1 mM fructose 1,6-diphosphate
0.007
-
NADH
Q27743
pH 7.5, 25C
0.007
-
NADH
Q6JH30
pH 7.5, 25C
0.0081
-
NADH
Q7Z0X7
-
0.009
-
NADH
-
pH 7.5, 25C
0.01
-
NADH
-
fructose 1,6-diphosphate has no effect
0.011
-
NADH
-
pH 7.5
0.0125
-
NADH
-
pH 7.3, isoenzyme I and isoenzyme II
0.014
-
NADH
-
pH 7.5, 25C
0.0142
-
NADH
-
-
0.0143
-
NADH
-
-
0.016
-
NADH
-
pH 7.5
0.018
-
NADH
-
wild-type enzyme
0.0186
-
NADH
O13278, -
-
0.0189
-
NADH
O13277, -
-
0.0196
-
NADH
O13276
-
0.02
-
NADH
-
pH 5.4
0.021
-
NADH
-
pH 7.5
0.04
-
NADH
-
pH 7.4
0.04
-
NADH
Agama stellio stellio
-
pH 7.5, 25C
0.05
-
NADH
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
0.054
-
NADH
P0C2T6
pH 6.0, 30C, isozyme LDH
0.058
-
NADH
P0C2T6
pH 7.0, 30C, isozyme LDH
0.065
-
NADH
-
mutant enzyme S163L
0.077
-
NADH
P0C2T6
pH 6.0, 30C, isozyme LDHB
0.08
-
NADH
-
pH 6.9, 90 mM Tris-maleate buffer, pH 6.9, 0.5 mM fructose 1,6-diphosphate
0.08
-
NADH
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.15
-
NADH
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
0.18
-
NADH
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.19
-
NADH
-
measured with D-fructose 1,6-bisphosphate; measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
0.25
-
NADH
Molinema dessetae
-
-
0.32
-
NADH
-
-
0.364
-
NADH
P0C2T6
pH 7.0, 30C, isozyme LDHB
0.4
-
NADH
-
in presence of fructose 1,6-diphosphate
0.5
-
NADH
-, Q9GT92
pH 8.0, 25C
8
-
NADH
-
without fructose 1,6-diphosphate
44
-
NADH
-
in absence of fructose 1,6-diphosphate
4.7
-
NADP+
P00344
25C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate
1.76
-
phenylpyruvate
-
pH 6.5, 30C, purified enzyme
0.016
-
pyruvate
-
20C, pH 7
0.016
-
pyruvate
-
-
0.016
-
pyruvate
-
-
0.017
-
pyruvate
Q6JH30
pH 7.5, 25C
0.018
-
pyruvate
-
octameric enzyme form
0.018
-
pyruvate
-
15C, pH 7
0.019
-
pyruvate
-
tetrameric enzyme form
0.02
-
pyruvate
Agama stellio stellio
-
pH 7.5, 25C
0.02
-
pyruvate
-, Q9GT92
pH 8.0, 25C
0.025
-
pyruvate
-
15C, pH 7.4
0.027
-
pyruvate
-
15C, pH 7
0.03
-
pyruvate
-
-
0.03
-
pyruvate
Q27743
pH 7.5, 25C
0.033
-
pyruvate
-
20C, pH 7
0.039
-
pyruvate
-
20C, pH 7.4
0.044
-
pyruvate
-
15C, pH 7.4
0.049
-
pyruvate
-
pH 7.5
0.054
-
pyruvate
-
20C, pH 7.4
0.055
-
pyruvate
-
pH 7.5
0.057
-
pyruvate
-
15C, pH 8
0.057
-
pyruvate
-
pH 7.5
0.06
-
pyruvate
P00344
pH 6.0, 25C, recombinant wild-type enzyme
0.061
-
pyruvate
-
30C, pH 7
0.07
-
pyruvate
-
pH 7.2, 25C, isoenzyme LDH-A2B2
0.071
-
pyruvate
-
pH 7.5, 25C
0.078
-
pyruvate
-
20C, pH 8
0.08
-
pyruvate
-
at 0C and at 5C
0.086
-
pyruvate
-
30C, pH 7.4
0.09
-
pyruvate
-
pH 7.6, 25C, isoenzyme LDH-B4
0.09
-
pyruvate
-
25C
0.11
-
pyruvate
-
15C, pH 8
0.113
-
pyruvate
-
pH 7.0, 4C
0.117
-
pyruvate
-
30C, pH 7.4
0.12
-
pyruvate
-
10C
0.13
-
pyruvate
-
15C
0.13
-
pyruvate
-
25C
0.14
-
pyruvate
-
20C
0.14
-
pyruvate
-
pH 7.5, 25C
0.14
-
pyruvate
-
25C
0.145
-
pyruvate
-
30C, pH 8
0.15
-
pyruvate
-
25C
0.15
-
pyruvate
-
-
0.16
-
pyruvate
O93541
pH 7.0, 0C, recombinant enzyme
0.16
-
pyruvate
Q5SJA1
pH 7.0, 0C, recombinant enzyme
0.171
-
pyruvate
-
20C, pH 8
0.18
-
pyruvate
-
30C
0.18
-
pyruvate
B1A4R6, -
pH 5.8, 60C, recombinant enzyme
0.19
-
pyruvate
-
-
0.2
-
pyruvate
-
-
0.2
-
pyruvate
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.21
-
pyruvate
-, P50933
pH 7.0, 0C, recombinant enzyme
0.22
-
pyruvate
-
-
0.22
-
pyruvate
-
pH 7.1, 25C, isoenzyme LDH-A4
0.24
-
pyruvate
-
-
0.24
-
pyruvate
-
-
0.25
-
pyruvate
-
with 1.0 mM fructose 1,6-diphosphate
0.26
-
pyruvate
O13278, -
-
0.312
-
pyruvate
-
30C, pH 7.4
0.32
-
pyruvate
-
pH 6.5, 30C, purified enzyme
0.33
-
pyruvate
O13277, -
-
0.34
-
pyruvate
-
pH 7.3, isoenzyme I
0.34
-
pyruvate
Molinema dessetae
-
-
0.34
-
pyruvate
O13276
-
0.35
-
pyruvate
-
pH 6.2
0.398
-
pyruvate
-
-
0.42
-
pyruvate
-
pH 7.3, isoenzyme II
0.5
-
pyruvate
-
pH 6.5, isoenzyme II
0.67
-
pyruvate
-
pH 8.0, 25C, in absence of aldolase
0.8
-
pyruvate
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
1
-
pyruvate
-
in presence of 0.02 mM fructose 1,6-diphosphate
1.15
-
pyruvate
-
in absence of fructose 1,6-diphosphate
1.3
-
pyruvate
P0C2T6
pH 6.0, 30C, isozyme LDHB
1.3
-
pyruvate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 0.25 mM NADH
1.5
-
pyruvate
-
pH 6.5
1.5
-
pyruvate
-
pH 6.9, 90 mM Tris-maleate buffer, pH 6.9, 0.5 mM fructose 1,6-diphosphate
1.5
-
pyruvate
P0C2T6
pH 6.0, 30C, isozyme LDH
1.7
-
pyruvate
P0C2T6
pH 7.0, 30C, isozyme LDH
1.75
-
pyruvate
-
-
1.88
-
pyruvate
-
-
1.9
-
pyruvate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 0.2 mM NADH
2.2
-
pyruvate
-
in absence of fructose 1,6-diphosphate
2.76
-
pyruvate
-
pH 6.0, 25C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate
2.8
-
pyruvate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 0.15 mM NADH
2.9
-
pyruvate
P0C2T6
pH 7.0, 30C, isozyme LDHB
3.7
-
pyruvate
-
pH 6.0, 25C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate
4.8
-
pyruvate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 0.125 mM NADH
5
-
pyruvate
-
LDHB, in the presence of 0.25 mM NADH
6.8
-
pyruvate
-
measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
7
-
pyruvate
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
7.7
-
pyruvate
-
in presence of fructose 1,6-diphosphate
7.7
-
pyruvate
-
LDHB, in the presence of 0.2 mM NADH
8.4
-
pyruvate
-
LDHB, in the presence of 0.15 mM NADH
13
-
pyruvate
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
13.3
-
pyruvate
-
pH 7.5, 25C, recombinant mutant I12V/R81Q/M85E/G210A/V214I
15
-
pyruvate
-
-
15
-
pyruvate
-
LDHB, in the presence of 0.125 mM NADH
19.3
-
pyruvate
-
pH 6.0, 25C, recombinant mutant D38R in absence of fructose 1,6-bisphosphate
32
-
pyruvate
-
pH 6.0, 25C, recombinant wild-type enzyme in absence of fructose 1,6-bisphosphate
34
-
pyruvate
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
105.1
-
Lactate
-
LDHB, in the presence of 3.75 mM NAD+
additional information
-
additional information
-
influence of pH
-
additional information
-
additional information
-
KM-values for mutant enzymes with enlarged loop
-
additional information
-
additional information
-
KM-values at position of temperatur minimum
-
additional information
-
additional information
-
stopped-flow kinetics, steady-state kinetics, and thermodynamics of free and NADH-bound enzyme, overview
-
additional information
-
additional information
-
kinetics analysis
-
additional information
-
additional information
-
steady-state and transient kinetics, rapid kinetics of the multiple-turnover reaction, overview
-
additional information
-
additional information
P0C2T6
isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH
-
additional information
-
additional information
-, P50933
an allosteric enzyme
-
additional information
-
additional information
B1A4R6, -
kinetics, the enzyme is allosteric in presence of D-fructose 1,6-bisphosphate, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
12.33
-
(S)-Lactate
Q6JH30
pH 9.2, 25C
25
-
(S)-Lactate
-
pH 9.2, 25C
38.33
-
(S)-Lactate
-
pH 9.2, 25C
65
-
(S)-Lactate
Q27743
pH 9.2, 25C
80
-
2-oxobutyrate
-
pH 7.5
0.64
-
2-oxovalerate
-
pH 7.5
1.4
-
3-acetylpyridine adenine dinucleotide
-
-
16
-
3-acetylpyridine adenine dinucleotide
-
enzyme form heart and muscle
153.3
-
3-acetylpyridine adenine dinucleotide
-
pH 9.2, 25C
233.3
-
3-acetylpyridine adenine dinucleotide
-
pH 9.2, 25C
250
-
3-acetylpyridine adenine dinucleotide
Q27743
pH 9.2, 25C
333.3
-
3-acetylpyridine adenine dinucleotide
Q6JH30
pH 9.2, 25C
0.33
-
4-methyl-2-oxopentanoate
-
wild-type enzyme
269
-
Bromopyruvate
-
-
0.7
-
epsilon-NAD+
-
-
5.3
-
epsilon-NAD+
-
-
6.2
-
epsilon-NAD+
-
enzyme from heart
98
-
Fluoropyruvate
-
-
3.3
-
NAD+
-
enzyme from muscle
12.33
-
NAD+
Q6JH30
pH 9.2, 25C
23
-
NAD+
P00344
25C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate; 25C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate
25
-
NAD+
-
pH 9.2, 25C
32
-
NAD+
P00344
25C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate
38.33
-
NAD+
-
pH 9.2, 25C
60
-
NAD+
-
enzyme from heart
65
-
NAD+
Q27743
pH 9.2, 25C
125
-
NADH
-
pH 7.5, 25C
126.7
-
NADH
Q6JH30
pH 7.5, 25C
148.3
-
NADH
Q27743
pH 7.5, 25C
216.7
-
NADH
Q7Z0X7
-
266.7
-
NADH
-
pH 7.5, 25C
1.1
-
nicotinamide hypoxanthine dinucleotide
-
-
1.1
-
nicotinamide hypoxanthine dinucleotide
-
enzyme from muscle
5.5
-
nicotinamide hypoxanthine dinucleotide
-
-
18.8
-
nicotinamide hypoxanthine dinucleotide
-
enzyme from heart
39.5
-
phenylpyruvate
-
wild-type enzyme
21.1
-
pyruvate
-
pH 6.0, 25C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate
46.5
-
pyruvate
-
pH 7.5, 25C, recombinant mutant I12V/R81Q/M85E/G210A/V214I
94
-
pyruvate
-
pH 7.5
96
-
pyruvate
-
pH 7.5
106
-
pyruvate
-
pH 7.5
125
-
pyruvate
-
pH 7.5, 25C
126.7
-
pyruvate
Q6JH30
pH 7.5, 25C
142
-
pyruvate
-
LDHB, in the presence of 0.125 mM NADH
148.3
-
pyruvate
Q27743
pH 7.5, 25C
154
-
pyruvate
-
LDHB, in the presence of 0.15 mM NADH
178.4
-
pyruvate
-
pH 6.0, 25C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate
180
-
pyruvate
-
wild-type enzyme
194.9
-
pyruvate
-
pH 6.0, 25C, recombinant mutant D38R in absence of fructose 1,6-bisphosphate
197
-
pyruvate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 0.125 mM NADH
204
-
pyruvate
-
-
230
-
pyruvate
O93541
pH 7.0, 0C, recombinant enzyme
244
-
pyruvate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 0.15 mM NADH
250
-
pyruvate
P00344
pH 6.0, 25C, recombinant wild-type enzyme
266.7
-
pyruvate
-
pH 7.5, 25C
298
-
pyruvate
-
LDHB, in the presence of 0.2 mM NADH
318
-
pyruvate
Rhizopus oryzae NRRL 395
-
LDHB, in the presence of 0.2 mM NADH
320
-
pyruvate
Rhizopus oryzae NRRL 395
-
RLDHB, in the presence of 0.25 mM NADH
327.2
-
pyruvate
-
pH 6.0, 25C, recombinant wild-type enzyme in absence of fructose 1,6-bisphosphate
350
-
pyruvate
-
LDHB, in the presence of 0.25 mM NADH
676
-
pyruvate
Q5SJA1
pH 7.0, 0C, recombinant enzyme
884
-
pyruvate
-, P50933
pH 7.0, 0C, recombinant enzyme
176
-
pyruvate ethyl ester
-
-
227
-
pyruvate methyl ester
-
-
40
-
L-lactate
-
pH 7.5
additional information
-
additional information
-
turnover-numbers for mutant enzymes with enlarged loop
-
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
(benzylamino)(oxo)acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0025
-
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.016
-
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
pH not specified in the publication, temperature not specified in the publication
0.004
-
2,3-dihydroxy-4,6,7-trimethylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.013
-
2,3-dihydroxy-4,6,7-trimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.022
-
2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.034
-
2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.001
-
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.002
-
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0001
-
2,3-dihydroxy-6,7-dimethyl-4-propylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0001
-
2,3-dihydroxy-6,7-dimethyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0002
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.013
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.002
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.003
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.001
-
2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.006
-
2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.003
-
2,3-dihydroxy-6-methyl-7-(2-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0002
-
2,3-dihydroxy-6-methyl-7-(3-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.00003
-
2,3-dihydroxy-6-methyl-7-(4-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.001
-
7-(4-chlorobenzyl)-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0005
-
7-benzyl-2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.008
-
7-benzyl-2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0002
-
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0007
-
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00005
-
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0003
-
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0012
-
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0013
-
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0008
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
pH not specified in the publication, temperature not specified in the publication
0.0006
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0003
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0011
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0004
-
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
pH not specified in the publication, temperature not specified in the publication
0.0006
-
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
1.2
-
fructose 1,6-bisphosphate
Rhizopus oryzae NRRL 395
-
LDHA
3.2
-
fructose 1,6-bisphosphate
Rhizopus oryzae NRRL 395
-
LDHB
28.8
-
fructose 1,6-bisphosphate
-
LDHB
0.00024
-
gossylic nitrile 1,1'-diacetate
Q6JH30
pH 7.5, 25C
0.0007
-
gossylic nitrile 1,1'-diacetate
Q27743
pH 7.5, 25C
0.0007
-
gossylic nitrile 1,1'-diacetate
-
pH 7.5, 25C
0.0018
-
gossylic nitrile 1,1'-diacetate
-
pH 7.5, 25C
0.0007
-
gossypol
Q27743
pH 7.5, 25C
0.0007
-
gossypol
-
pH not specified in the publication, temperature not specified in the publication
0.0014
-
gossypol
Q6JH30
pH 7.5, 25C
0.0014
-
gossypol
-
LDH-B, pH not specified in the publication, temperature not specified in the publication
0.0019
-
gossypol
-
pH 7.5, 25C
0.0019
-
gossypol
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0042
-
gossypol
-
LDH-C, pH not specified in the publication, temperature not specified in the publication
0.0126
-
gossypol
-
pH 7.5, 25C
0.00007
-
gossypol lactone
Q6JH30
pH 7.5, 25C
0.0004
-
gossypol lactone
Q27743
pH 7.5, 25C
0.0005
-
gossypol lactone
-
pH 7.5, 25C
0.0015
-
gossypol lactone
-
pH 7.5, 25C
10
-
oxo(phenylamino)acetic acid
-
above, LDH-A, pH not specified in the publication, temperature not specified in the publication
7
-
oxo[(2-phenylethyl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
10
-
oxo[(2-phenylpropyl)amino]acetic acid
-
above, LDH-A, pH not specified in the publication, temperature not specified in the publication
0.9
-
oxo[(3-phenylpropyl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.8
-
oxo[(4-phenylbutan-2-yl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
2
-
oxo[(4-phenylbutyl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.14
-
pyruvate
-
pH 7.5
1.64
-
pyruvate
-
pH 7.0, 4C
10.9
-
pyruvate
-
pH 6.0, 25C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate
31.1
-
pyruvate
-
pH 6.0, 25C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate
57
-
pyruvate
-
pH 7.5
66
-
pyruvate
-
pH 7.5
1
-
[(4-chlorobenzyl)amino](oxo)acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
2
-
[(4-methylbenzyl)amino](oxo)acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
3.02
-
Methylmalonate
-
enzyme from brain
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
substrate and product inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.059
-
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00008
-
(benzylamino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.16
-
(heptylamino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
(heptylamino)(oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.047
-
(hexylamino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.133
-
(hexylamino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.088
-
(nonylamino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
(nonylamino)(oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.0083
-
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.179
-
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.00175
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.0114
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.0031
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.187
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
21
-
2,6-naphthalene disulfonic acid
-
IC50: 21 mM
5.1
-
2,6-naphthalenedicarboxalic acid
-
IC50: 5.1 mM
1.7
-
3,5-dihydroxy 2-naphthoic acid
-
IC50: 1.7 mM
1.7
-
3,5-dihydroxynaphthalene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
150
-
3,5-dihydroxynaphthalene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
2.4
-
3,7-dihydroxy naphthalene-2-carboxylic acid
-
IC50: 2.4 mM
2.4
-
3,7-dihydroxynaphthalene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
5
-
3,7-dihydroxynaphthalene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0011
-
3-hydroxy-1,2-oxazole-4-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.31
-
4,7-dibromo-3-hydroxynaphthalene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
5.9
-
4,7-dibromo-3-hydroxynaphthalene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00065
-
4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00014
-
4-hydroxy-1,2,5-thiadiazole-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.016
-
4-hydroxy-1,2-oxazole-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
4.6
-
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
6.6
-
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
6.6
-
6,6'-Dithiodinicotinic acid
-
IC50: 6.6 mM
0.191
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.225
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.52
-
8-(phenylamino)naphthalene-1-sulfonic acid
-
pH not specified in the publication, temperature not specified in the publication
1.1
-
8-(phenylamino)naphthalene-1-sulfonic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0873
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.232
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.52
-
8-anilino-1-naphthalene sulfonic acid
-
IC50: 0.52 mM
0.0944
-
amino(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.116
-
amino(oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00005
-
cardiolipin
-
IC50: 0.00005 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
5.5
-
Chloroquine
-
IC50: 5.5 mM
4.6
-
Methylmalonate
-
IC50: 4.6 mM (enzyme from brain), 4.6 mM (enzyme from liver)
1.4
-
naphthalene-2,6-dicarboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
5.11
-
naphthalene-2,6-dicarboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
9.8
-
naphthalene-2,6-disulfonic acid
-
pH not specified in the publication, temperature not specified in the publication
21
-
naphthalene-2,6-disulfonic acid
-
pH not specified in the publication, temperature not specified in the publication
0.15
-
oxo(pentadecylamino)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
oxo(pentadecylamino)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.0001
-
oxo[(2-phenylethyl)amino]acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.000035
-
oxo[(3-phenylpropyl)amino]acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.041
-
oxo[(4-phenylbutyl)amino]acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.088
-
oxo[(4-phenylbutyl)amino]acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0188
-
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.146
-
oxo[[1-(5,6,7,8-tetrahydronaphthalen-1-yl)ethyl]amino]acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
oxo[[1-(5,6,7,8-tetrahydronaphthalen-1-yl)ethyl]amino]acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.0013
-
phosphatidylserine
-
IC50: 0.0013 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
0.158
-
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.014
-
[(2-methoxyethyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.025
-
[(2-methoxyethyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.035
-
[(3,3-diphenylpropyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.09
-
[(3,3-diphenylpropyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.031
-
[(3-methoxypropyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.043
-
[(3-methoxypropyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.157
-
[(3-methylbutyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[(3-methylbutyl)amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.0979
-
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.107
-
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00007
-
[(4-chlorobenzyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00009
-
[(4-methylbenzyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.186
-
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.043
-
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.168
-
[benzyl(methyl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[benzyl(methyl)amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.043
-
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.046
-
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.169
-
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.059
-
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.101
-
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.032
-
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
0.051
-
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
-
pH not specified in the publication, temperature not specified in the publication
0.2
-
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
-
above, pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.714
-
-
isoenzyme I
1.87
-
-
isoenzyme II
5.1
-
-
single pyruvate decarboxylase 1 mutant strain T157
11.5
-
-
pyruvate decarboxylase 1/alcohol dehydrogenase 1 mutant strain AF297C
30
-
-
commercial preparation
53
-
Agama stellio stellio
-
-
80
-
-
isoenzyme X
80.27
-
Molinema dessetae
-
-
106
-
-
-
203.3
-
-
purified native enzyme, substrate pyruvate
215
-
-
reduction of pyruvate
216
-
-
reduction of pyruvate
253
-
Q27743
reduction of pyruvate
450
-
Q6JH30
reduction of pyruvate
456
-
-
purified protein with pyruvate as substrate
458.5
-
-
-
2119
-
-
recombinant enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
cofactor specificity in different strains
additional information
-
-
-
additional information
-
Pontonia pinnophylax
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, overview
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
6
-
reduction of pyruvate
4.5
-
-
reduction of pyruvate, with addition of fructose 1,6-diphosphate and Mn2+
4.5
-
-
reduction of pyruvate
5
6.2
-
reduction of pyruvate
5
7
-
reduction of pyruvate, in presence of fructose 1,6-diphosphate
5.3
-
-
reduction of pyruvate
5.4
-
-
sodium acetate buffer
5.5
6
P0C2T6
isozyme LDHB
5.5
7
-
reduction of pyruvate
5.5
-
-
reduction of pyruvate
5.6
-
-
reduction of pyruvate
5.8
-
B1A4R6, -
pyruvate reduction, recombinant enzyme
6
-
-
reduction of pyruvate
6
-
-
assay at, reduction reaction
6
-
-
with substrate phenylpyruvate
6.5
-
-
reduction of pyruvate, without fructose 1,6-diphosphate
6.5
-
-
reduction of oxo acids with NADH or NADPH
6.5
-
-
reduction of pyruvate
6.8
-
Molinema dessetae
-
reduction of pyruvate
6.8
-
Rhizopus delemar, Rhizopus oryzae NRRL 395
-
-
6.9
-
-
in presence of fructose 1,6-diphosphate
7
-
-
reduction of pyruvate, addition of fructose 1,6-diphosphate
7
-
-
reduction of pyruvate
7
-
-
reduction of pyruvate
7
-
-
assay at
7
-
Q0GND9
assay at
7
-
Q0GND8
assay at
7
-
-, P50933
the enzyme shows a narrow pH optimum
7
-
B1A4R6, -
lactate oxidation, recombinant enzyme
7.1
-
-
reduction of pyruvate, isoenzyme LDH-A4
7.1
-
Pontonia pinnophylax
-
assay at, pyruvate reduction
7.2
-
-
oxidation of lactate
7.25
-
-
reduction of pyruvate, isoenzyme LDH-A2B2
7.3
-
-
reduction of pyruvate, isoenzyme I and II
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
oxidation of lactate
7.5
-
-
reduction of pyruvate and oxidation of lactate
7.5
-
Agama stellio stellio
-
with pyruvate as substrate
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
oxidation of lactate
7.6
-
-
reduction of pyruvate, isoenzyme LDH-B4
7.6
-
-
assay at
7.8
8.8
-
oxidation of lactate, isoenzyme I and II
7.8
-
-
oxidation of lactate
8
-
-
reduction of pyruvate, in absence of fructose 1,6-diphosphate
8.2
-
-
oxidation of lactate
8.2
-
-
in absence of fructose 1,6-diphosphate
8.5
-
-
oxidation of lactate
8.6
-
Molinema dessetae
-
oxidation of lactate
9
-
-
oxidation of lactate
9.1
-
-
oxidation of lactate
9.2
-
Agama stellio stellio
-
with lactate as substrate
9.5
-
-
glycine-NaOH buffer
9.8
-
-
oxidation of lactate
9.8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
9
-
activity range, the enzyme is inactive below pH 3.0 and above pH 9.0
4.3
8
-
no activity below pH 4.3 and above pH 8.0
5
7
-
about 55% of maximal activity at pH 5.0 and at pH 7.0
5.2
7.2
-
pH 5.2: about 35% of maximal activity, pH 7.2: about 50% of maximal activity
5.2
7.2
P0C2T6
LDH activity shows a broad plateau between pH 5.2 and pH 7.2, and no activity at pH 4.8
5.3
8
-
pH 5.3: about 50% of maximal activity, pH 8.0: about 60% of maximal activity, reduction of pyruvate
5.4
10.8
Agama stellio stellio
-
pH 5.4: about 60% of maximal activity, pH 10.8: about 55% of maximal activity, reaction with pyruvate
5.5
8
-
pH 5.5: 40% of maximal activity of isoenzyme LDH-B4 and 60% of maximal activity of isoenzyme LDH-A2B2 and LDH-A4, pH 8.0: about 60% of maximal activity of isoenzyme LDH-A4, LDH-B4 and LDH-A4B4, reduction of pyruvate
6
8
Molinema dessetae
-
pH 6.0: 85% of maximal activity, pH 8.0: 45% of maximal activity, reduction of pyruvate
6.4
6.9
Rhizopus delemar, Rhizopus oryzae NRRL 395
-
LDHB, in Bis-Tris-propane buffer
6.5
10
-
optimal pH range for pyruvate reduction and lactate oxidation is 6.5-7.0 and 9.0-10.0, respectively
6.6
10.8
Agama stellio stellio
-
pH 5.4: about 55% of maximal activity, pH 10.8: about 55% of maximal activity, reaction with lactate
7.7
9.5
-
pH 7.7: about 60% of maximal activity, pH 9.5: about 30% of maximal activity, reduction of pyruvate
8
9.6
Molinema dessetae
-
pH 8.0: 60% of maximal activity, pH 9.6: 45% of maximal activity, oxidation of lactate
8.5
10.7
-
pH 8.5: about 60% of maximal activity, pH 10.7: about 70% of maximal activity, oxidation of lactate
additional information
-
P0C2T6
the two isozymes LDH and LDHB exhibited different pH profiles for maximal activity
additional information
-
O93541
pH profile
additional information
-
-, P50933
pH profile
additional information
-
Q5SJA1
pH profile
additional information
-
Q27797
under alkaline conditions the presence of the recombinant LDH protein increases the differentiation; under alkaline conditions the presence of the recombinant LDH proteins increases the differentiation
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at, reduction reaction
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
in vivo assay at
25
-
Pontonia pinnophylax
-
assay at, pyruvate reduction
25
-
P00344
assay at
30
-
Q0GND9
assay at
30
-
Q0GND8
assay at
30
-
P0C2T6
assay at
30
-
-
assay at
37
-
-
assay at
40
-
-
with substrate phenylpyruvate
45
-
-
highest relative activity for both the reduction and oxidation reactions
60
-
B1A4R6, -
pyruvate reduction, recombinant enzyme
70
-
B1A4R6, -
lactate oxidation, recombinant enzyme
90
-
Q5SJA1
about
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
14
46
Q0GND9
in vivo temperature
14
46
Q0GND8
in vivo temperature
20
70
-
90% of maximal activity at 50C and 50% at 60C
37
60
-
37C: about 85% of maximal activity, 60C: about 90% of maximal activity
37
65
-
optimal temperatures for the reduction and oxidation reactions are 37-65C and 40-50C, respectively
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
P0C2T6
isozyme LDH, sequence calculation
5.2
-
P0C2T6
isozyme LDHB, sequence calculation
5.5
-
-
heart-type isozyme
6
-
Q6JH30
-
6.5
-
Q27743
-
8.03
-
-
theoretical isoelectric point
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the level of L-lactate dehydrogenase B are specifically increased in non-small cell lung cancer
Manually annotated by BRENDA team
B7XH73, C6L1K8, -
;
Manually annotated by BRENDA team
-
endometrial and ovarian
Manually annotated by BRENDA team
-
differential expressions of LDH isozymes in different types of tumors
Manually annotated by BRENDA team
Mus musculus AKR
-
differential expressions of LDH isozymes in different types of tumors
-
Manually annotated by BRENDA team
P07195
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
Manually annotated by BRENDA team
-
embryonic membrane of oncosphere
Manually annotated by BRENDA team
-
H-type isozyme
Manually annotated by BRENDA team
-
heart-type isozyme
Manually annotated by BRENDA team
-
in patients with tubercular pyothorax, decrease in heart specific aerobic LDH-1 (6fold), LDH-2 (2fold) and LDH-3 (1.5fold)
Manually annotated by BRENDA team
B7XH73, C6L1K8, -
;
Manually annotated by BRENDA team
Mus musculus AKR
-
H-type isozyme
-
Manually annotated by BRENDA team
Mus musculus AKR
-
-
-
Manually annotated by BRENDA team
Mus musculus AKR
-
-
-
Manually annotated by BRENDA team
P07195
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
Manually annotated by BRENDA team
-
M-type isozyme
Manually annotated by BRENDA team
-
significant rise in the level of muscle specific anaerobic LDH-5 and LDH-4 in patients with tubercular pyothorax
Manually annotated by BRENDA team
Mus musculus AKR
-
M-type isozyme
-
Manually annotated by BRENDA team
-
primary non-small cell lung cancer cell line
Manually annotated by BRENDA team
-
brain metastatic subline of NCI-H226. L-lactate dehydrogenase B is significantly up-regulated in the conditional medium of NCI-H226Br cells
Manually annotated by BRENDA team
-
activities of both H- and M-isoforms of LDH are high but neurons show a dominance of H-isoform activity
Manually annotated by BRENDA team
P07195
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
Manually annotated by BRENDA team
-
patients with tubercular pyothorax show highest levels in LDH-5 followed by LDH-4, LDH-3, LDH-2 and LDH-1
Manually annotated by BRENDA team
P07195
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
Manually annotated by BRENDA team
-
patients with tubercular pyothorax show highest levels in LDH-5 followed by LDH-4, LDH-2, LDH-3 and LDH-1. In LDH-5 and LDH-4 nearly 4- and 5folds increase in patients
Manually annotated by BRENDA team
Agama stellio stellio
-
-
Manually annotated by BRENDA team
-
muscle-type isozyme, i.e. M4 isoform
Manually annotated by BRENDA team
Q0GND8
muscle isozyme
Manually annotated by BRENDA team
-
isoenzyme LDH-B4 and LDH-A2B2
Manually annotated by BRENDA team
B7XH73, C6L1K8, -
muscle; muscle
Manually annotated by BRENDA team
-
fat-free milk, or 2% fat milk
Manually annotated by BRENDA team
additional information
Q8I8U5
LDH is stage specifically transcribed in Eimeria, but its presence at the protein level remains constant during different life-cycle stages
Manually annotated by BRENDA team
additional information
-
tissue-specific expression analysis, overview
Manually annotated by BRENDA team
additional information
-
type-I isolate, e.g. strain NRRL 395, accumulating primarily lactic acid when grown in the presence of a fermentable carbon source and containing two LDH genes, ldhA and ldhB, and type-II isolates, e.g. strain 99-880, synthesizing predominantly fumaric acid and having only an ldhB gene
Manually annotated by BRENDA team
additional information
O93541
structural features for structural stability, comparison to enzymes from other species in extreme environments
Manually annotated by BRENDA team
additional information
-, P50933
structural features for structural stability, comparison to enzymes from other species in extreme environments
Manually annotated by BRENDA team
additional information
Q5SJA1
structural features for structural stability, comparison to enzymes from other species in extreme environments
Manually annotated by BRENDA team
additional information
-
metabolic adaptation of Staphylococcus aureus to nitrosative stress, overview
Manually annotated by BRENDA team
additional information
Q27797
LDH1 is absent from bradyzoites; LDH2 is absent from tachyzoites
Manually annotated by BRENDA team
additional information
-
in satellite gliocytes, activities of both H- and M-isoforms of LDH are high, dominance of M-isoform activity
Manually annotated by BRENDA team
additional information
-
surface of the tegument in adults. Is absent from internal tissues
Manually annotated by BRENDA team
additional information
-
homo- and heterotetrameric isozymes with tissue-specific expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q7Z0X7
of intra- and extraerythrocytic parasites
Manually annotated by BRENDA team
Pontonia pinnophylax
-
-
Manually annotated by BRENDA team
Q7Z0X7
of infected erythrocytes
Manually annotated by BRENDA team
-
embryonic membrane of oncosphere
Manually annotated by BRENDA team
-
inner compartment, transport and metabolism of L-lactate, overview
Manually annotated by BRENDA team
-
LDH is present in the inner mitochondrial compartments
Manually annotated by BRENDA team
Mus musculus AKR
-
LDH-A
-
Manually annotated by BRENDA team
additional information
-
immunohistochemic analysis of subcellular localization
-
Manually annotated by BRENDA team
additional information
-
the recombinant protein is exclusively associated with inclusion bodies
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus cereus (strain ATCC 14579 / DSM 31)
Bacillus cereus (strain ATCC 14579 / DSM 31)
Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Plasmodium berghei (strain Anka)
Plasmodium falciparum (isolate 3D7)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Plasmodium falciparum (isolate CDC / Honduras)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35200
-
-
sequence analysis
39200
-
Q27797
antibodies
39900
-
Q27797
antibodies
65000
67000
-
gel filtration
77000
-
-, Q9GT92
monomer, sedimentation velocity
78000
-
-
gel filtration
113000
-
Molinema dessetae
-
gel filtration
125000
138000
-
gel filtration
130000
-
-
sucrose density gradient centrifugation
130000
-
-
tetramer, sucrose density gradient centrifugation in presence of fructose 1,6-diphosphate and NADH
132000
-
-
non-denaturing gel electrophoresis
134000
-
-
gel filtration
134000
-
-, Q9GT92
dimer, sedimentation velocity
135000
-
-
gel filtration
139000
-
-
gel filtration
140000
-
-
ultracentrifugal studies
140000
-
-
tetramer, gel filtration
140000
-
-
gel filtration
144000
-
-
equilibrium sedimentation
150000
-
-
disc gel electrophoresis
187000
-
-
non-denaturing gel electrophoresis
269300
-
-
meniscus depletion experiments
280000
-
-
octamer, gel filtration
280900
-
-
equilibrium sedimentation
670000
-
-
above, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 33700, SDS-PAGE
?
-
x * 40000, oligomer, SDS-PAGE
?
Agama stellio stellio
-
x * 36000, SDS-PAGE
?
-
x * 39000, recombinant His6-tagged LDH-1, SDS-PAGE, x * 34600, about, sequence calculation
?
-
x * 42000, recombinant His6-tagged LctD, SDS-PAGE
?
Aggregatibacter actinomycetemcomitans HK1651 and VT1169
-
x * 42000, recombinant His6-tagged LctD, SDS-PAGE
-
dimer
-
2 * 37000, SDS-PAGE
dimer
Molinema dessetae
-
2 * 58000, isoenzyme LDH1 and LDH2, SDS-PAGE
dimer
-, Q9GT92
2 * 77000, monomer-dimer equilibrium in solution
dimer
-
2 * 39000, SDS-PAGE
dimer
-
2 * 39000, SDS-PAGE
-
octamer
-
8 * 35000, enzyme also exists in an tetrameric enzyme form, SDS-PAGE, meniscus depletion experiments in 4 M guanidinium chloride
tetramer
-
4 * 35900, SDS-PAGE
tetramer
-
4 * 34000, SDS-PAGE
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 33500, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
wild-type enzyme and N-terminal deletion mutants lacking the first 5 or the first 10 amino acids
tetramer
Q8I8U5
-
tetramer
-
heart-type isozyme
tetramer
-
homo- and heterotetrameric isozymes with tissue-specific expression
monomer
-, Q9GT92
1 * 77000, monomer-dimer equilibrium in solution
additional information
-
three bands detected after SDS-PAGE with MW of 60000 Da, 66000 Da and 74000 Da
additional information
-
analysis of enzyme structure under high pressure conditions: even the lowest high pressure processing treatment of 206 MPa induces a reduction in LDH activity, and the course of reduction increases with high pressure processing treatment until complete inactivation at 482, 515, and 620 MPa. The structure of LDH shows gradual denaturation after exposure at 206 MPa for 6 min, leading to a random coil structure at both 515 and 620 MPa. The loss of LDH activity with increasing pressure and time treatment was due to the combined effects of denaturation and aggregation, structure analysis by far-ultraviolet circular dichroism spectroscopy and dynamic light scattetering
additional information
-
binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview
additional information
-
three-dimensional structures of the L-LDH-NADH complex of enzyme from muscle and heart, molecular analysis, overview
additional information
Q0GND9
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Iguana iguana, overview
additional information
Q0GND8
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Amblyrhynchus cristatus, overview
additional information
P0C2T6
LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers
additional information
Pontonia pinnophylax
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, overview
additional information
O93541
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
-, P50933
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview
additional information
Q5SJA1
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
B1A4R6, -
TeLdhL contains a GXGXXG motif common to most NAD-linked dehydrogenases close to the N-terminus, and a putative signal peptide with cleavage site between residue 26 and 27, deletion of the putative signal peptide sequence leads to nonexpression of TeLdhL
additional information
-
structure comparison of LDH-M and LDH-H subunit isoforms, the homotetramers have essentially the same tertiary structure, while the hybrid tetramers show different structures, overview. Rossmann fold topology, structure comparison to the enzyme from Plasmodium falciparum, PDB IDs 1i10 and 1ldg, Ser163 is a highly conserved residue amongst human hLDH isozymes, corresponds to Leu163 in PfLDH, differences occur mainly in the N-terminus, overview
additional information
-
Rossmann fold topology, structure comparison to the enzyme from Homo sapiens, PDB IDs 1i10 and 1ldg, differences occur mainly in the N-terminus, overview
additional information
B7XH73, C6L1K8, -
three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview; three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview
additional information
Thermoanaerobacter ethanolicus JW200
-
TeLdhL contains a GXGXXG motif common to most NAD-linked dehydrogenases close to the N-terminus, and a putative signal peptide with cleavage site between residue 26 and 27, deletion of the putative signal peptide sequence leads to nonexpression of TeLdhL
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified His-tagged wild-type and mutant H171C enzymes, hanging drop vapor diffusion method, 0.002 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.5, with 1 mM fructose 1,6-bisphosphate and NAD+, is mixed with 0.002 ml of reservoir solution containing 16% w/v PEG MME 2000, 0.06 M sodium/potassium phosphate, 1.8% v/v glycerol pH 5.5, or 14% w/v PEG 4000, 0.1 M sodium/potassium phosphate, 2% v/v glycerol, pH 7.0, equilibration against 1 ml reservoir solution, X-ray diffraction structure determinaation and analysis at 2.2-2.5 A resolution
-
apo enzyme form, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement
O93541
purified enzyme, hanging drop vapor diffusion technique, 8 mg/ml protein in 20% PEG 5000 MME, 0.1M bicine, pH 9.0, at room temperature, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
-, P50933
crystal structure of a mutant into which an additional loop has been engineered in order to prevent tetramerization
-
binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview
-
overexpression in Escherichia coli
-
hanging drop method of vapour diffusion, ternary complex with NADH and oxamate
-
crystals the apo-form of PfLDH are ontained by hanging-drop method with 2-methyl-2,4-pentanediol as precipitant, crystallization of enzyme:naphthoic acid complexes with 2,6-naphthalenedicarboxalic acid, 2,6-naphthalene disulfonic acid or 3,7-dihydroxy naphthalene-2-carboxylic acid and 3,7-dihydroxy naphthalene-2-carboxylic acid plus NAD+
-
purified recombinant His-tagged Sa-LDH-1, sitting drop vapour diffusion method, 0.001 ml protein solution, containing 5 mg/ml protein in 20 mM Tris-HCl, 200 mM NaCl, pH 7.5, is mixed with mixed with an equal volume of reservoir solution, containing ,0.2 M calcium chloride dihydrate, 0.1 M Na HEPES, pH 7.5, 28%(v/v) PEG 400, and equilibrated against 0.1 ml reservoir solution, 3 days, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
2.1 A resolution as a quarternary complex with the cofactor NADH, the allosteric activator fructose-1,6-bisphosphate and the substrate analog oxamate
-
apo enzyme form and enzyme in ternary complex, X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution, molecular replacement
Q5SJA1
in apo-form and in ternary complexes containing NAD+ or NAD+-analogue 3-acetylpyridine adenine dinucleotide and sulfate or the inhibitor oxalate
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
7
-
1 h, 25C, pH 3.8: 50% loss of activity, pH 7.0: stable, mutant enzyme with a deletion of 10 N-terminal amino acids
4
8
-
rather stable from pH 4.0 to pH 8.0, but rapid decline in activity below pH 4.0 and above pH 8.0
5
7.5
-
rapid loss of activity below pH 5.0 and above pH 7.5
5.5
7
-
1 h, 25C, pH 5.5: 50% loss of activity, pH 7.0: stable, wilde-type enzyme
5.7
7
-
1 h, 25C, pH 5.7: 50% loss of activity, pH 7.0: stable, mutant enzyme with a deletion of 5 N-terminal amino acids
5.8
8.2
B1A4R6, -
purified recombinant enzyme, 1-5 h, 70C, completely stable
6.5
-
-
highest stability at
additional information
-
B1A4R6, -
incubation of TeLdhL at lower pH results in a rapid inactivation of the enzyme
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
35
-
the mean Q10 value for all species is 1.8
45
-
-
20 min, about 10% loss of activity, isoenzyme A4
45
-
O93541
inactivation above, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
46
-
-
1 h, 25C, 50% loss of activity, mutant enzyme with a deletion of 10 N-terminal amino acids
48
-
-
30 min, stable up to
50
-
-
2 min, 6% loss of activity in presence of fructose 1,6-diphosphate, NADH and pyruvate, complete loss of activity without protectant
50
-
Molinema dessetae
-
15 min, 2% loss of activity
50
-
-
900 min, stable
50
-
-
10 min, 90% loss of activity
50
-
-
1 h, 25C, 50% loss of activity, mutant enzyme with a deletion of 5 N-terminal amino acids
50
-
-
20 min, about 40% loss of activity of isoenzyme A4, about 10% loss of activity of isoenzyme B4, about 25% loss of activity of isoenzyme A2B2
51
-
-
20 min, about 75% loss of activity, isoenzyme A4
53
-
-
20 min, complete loss of activity of isoenzyme A4, about 40% loss of activity of isoenzyme A2B2
55
-
Molinema dessetae
-
stable below
55
-
-
stable up to
55
-
-
20 min, about 90% loss of activity of isoenzyme A2B2, about 15% loss of activity of isoenzyme B4
58
-
-
20 min, 50% loss of activity, allozyme LDH-Ba4
58
-
-
30 min, stable up to A hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH is named S100M
60
-
-
relatively stable
60
-
-
5 min, complete inactivation without stabilizer, Mn2+ in combination with fructose 1,6-diphosphate stabilizes the enzyme completely
60
-
-, P50933
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
61
-
-
20 min, 50% loss of activity, allozyme LDH-Ba/Bb
63
-
-
20 min, 50% loss of activity, allozyme LDH-Bb4
65
-
-
20 min, stable up to
65
-
-
stable for 10 min, 30% loss of activity after 1 h
65
-
Pontonia pinnophylax
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, MDH is more sensitive than LDH, overview
66
-
-
20 min, about 35% loss of activity of isoenzyme B4
68
-
-
1 h, 25C, 50% loss of activity, wilde-type enzyme
68
-
-
20 min, about 68% loss of activity of isoenzyme B4
69
-
-
30 min, 50% loss of activity
70
-
-
3 min, complete inactivation
70
-
Agama stellio stellio
-
30 min, stable
70
-
B1A4R6, -
purified recombinant enzyme, 1-5 h, pH 5.8-8.2, completely stable
71
-
-
30 min, 50% loss of activity
71
-
-
20 min, complete loss of activity of isoenzyme B4
71.5
-
-
20 min, 50% loss of activity
73.5
-
-
30 min, 50% loss of activity
74
-
-
30 min, stable up to
75
-
-
30 min, 50% loss of activity
80
-
B1A4R6, -
purified recombinant enzyme, half-life is 1.5 h
90
-
Agama stellio stellio
-
rapid inactivation
90
-
Q5SJA1
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
additional information
-
-
protection against heat inactivation by 1 mM fructose 1,6-diphosphate, 1 mM ATP, 1 mM glucose 6-phosphate and increased levels of phosphate
additional information
-
-
very stable at room temperature, 4C and 50C
additional information
-
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
addition of cofactor stabilizes all allozymes to urea inactivation
-
inactivation by pronase, trypsin and chymotrypsin
-
stable to dilution in the range 0.2-0.01 mg protein per ml
-
very stable during 70 h dialysis in acetate buffer pH 5.5, in imidazol buffer, pH 6.5, in phosphate buffer pH 6.5 with dithioerythritol and in Tris-HCl buffer pH 7.5 with Mn2+ and fructose 1,6-diphosphate
-
irreversible loss of activity after several hours when the concentration is below 0.1 mg protein per ml
-
Mn2+ and fructose 1,6-diphosphate are required during dialysis at pH 5.5, very unstable during dialysis at pH 7.5 although Mn2+ and fructose 1,6-diphosphate are added
-
NADH and fructose 1,6-diphosphate partially stabilize the 140000 Da molecular weight form against dissociation in triethanolamine-hydrochloride buffer at pH 8.0
-
N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are more sensitive to denaturing environment than wild-type enzyme. They are easily inactivated and unfolded. Their instability increases and their ability to refold decreases with the increased number of amino acid residues removed from the N-terminus of LDH
-
the transition midpoints, 50% activity after 1 h incubation in guanidine HCl, are 0.77 M for the mutant enzyme with a deletion of 10 N-terminal amino acids, 0.92 M for the mutant with a deletion of 5 N-terminal amino acids and 1.7 M for the wild-type enzyme
-
fructose-1,6-diphosphate is necessary to stabilize the tetrameric enzyme form
-
modification by o-phthalaldehyde not only results in inactivation of the enzyme, but also leads to the enzymes dissociation and partial unfolding
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for months
-
stabilized for storage at 4C by addition of 0.2-1 M potassium chloride or 3.2 M ammonium sulfate
-
4C, as ammonium sulfate suspension, stable for more than 8 months
-
-20C, 50 mM sodium phosphate buffer, pH 7.0, stable for several months
-
4C, Krebs-Henseleit buffer, 24 h
-
4C, glycerol and DDT containing buffer
Rhizopus delemar, Rhizopus oryzae NRRL 395
-
-5C, precipitated from phosphate buffer with (NH4)2SO4 and storage in the supernatant solution, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isoenzyme LDH-5
Agama stellio stellio
-
native enzyme, and recombinant His6-tagged enzyme by nickel affinity chromatography from Escherichia coli BL21(DE3)
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity and anion exchange chromatography
-
native enzyme by ultracentrifugation, hydrophobic interaction chromatography, gel filtration, and ultrafiltration
O93541
isoenzyme LDH-A4 from muscle
-
recombinant enzyme from Escherichia coli strain DH5alpha by heat treatment at 55C for 90 s, hydrophobic interaction chromatography, hydroxyapatite chromatography, gel filtration, and ultrafiltration
-, P50933
allozymes: LDH-Ba4, LDH-Ba/Bb and LDH-Bb4
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 by ion-exchange chromatography and affinity chromatography, respectively
-
isoenzyme I and II
-
isoenzyme I and II; partial
-
fructose 1,6-diphosphate-activated enzyme form
-
native enzyme 34.3fold to about 98% purity by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
isozymes LDHB and LDH 400fold and 30fold, from cell extracts of strains FI9078 and MG1363, respectively
P0C2T6
two major isoenzymes LDH1 and LDH2
Molinema dessetae
-
isoenzyme A4, B4 and X
-
optimization of a molecular analysis method based on the three-dimensional structure of protein and protein-ligand interactions using dye-ligand density for target protein separation, 3.7fold purification with expanded bed affinity adsorption, overview
-
to homogeneity yielding 18 mg of protein/litre culture
-
wild-type and enlarged loop mutants ELM1 and ELM2
-
partially purified renal LDH
-
on cobalt affinity resin
-
recombinant His6-tagged LdhB from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography and cleavage of the tag
-
on cobalt affinity resin
Rhizopus oryzae NRRL 395
-
recombinant N-termially His6-tagged LDH-1 from Escherichia coli BL21 by nickel affinity chromatography and gel filtration to homogeneity
-
by His bind purification
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
B1A4R6, -
recombinant enzyme from Escherichia coli strain DH5alpha by heat treatment at 70C for 90 s, anion exchange chromatography, gel filtration, and ultrafiltration
Q5SJA1
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene AA02769 or lctD, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli DH5alpha, expression as His6-tagged protein in Escherichia coli BL21(DE3)
-
gene ldh-a, DNA and amino acid sequence determination and analysis
Q0GND9
expression in Escherichia coli HB101 using a pEMBL vector. The gene is strongly expressed in the vector used if the orientation of the insert allows the LDH promoter and the vector's lac promoter to direct transcription in the same direction
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
-
development of a recombinant yeast exhibiting efficient lactate production by substituting the coding region of PDC1 on chromosome XII for that of LDH through homologous recombination
P0CW93
development of a recombinant yeast exhibiting efficient lactate production by substituting the coding region of PDC1 on chromosome XII for that of LDH through homologous recombination
-
expressed in Saccharomyces cerevisiae replacing disrupted pyruvate decarboxylase 1 and alcohol dehydrogenase 1
-
expression in Escherichia coli
-
expression in Escherichia coli as maltose-binding protein fusion protein. CpLDH1 is probably evolved from the same ancestor of CpMalDH1 by a very recent gene duplication that occurs after Cryptosporidium parvum diverges from other apocomplexans
-, Q9GT92
expression in Escherichia coli strain DH5alpha
-, P50933
-
-, Q8I8U3
LDHA, DNA and amino acid sequence determination and analysis, genetic structure, and sequence comparisons, phylogenetic analysis, overview; LDHB, DNA and amino acid sequence determination and analysis, genetic structure, and sequence comparisons, phylogenetic analysis, overview
B7XH73, C6L1K8, -
a chimeric bifunctional enzyme composing of galactose dehydrogenase from Pseudomonas fluorescens and lactate dehydrogenase from Bacillus stearothermophilus is successfully constructed and expressed in Escherichia coli
-
expression in Escherichia coli HB101 using a pEMBL vector. The gene is strongly expressed in the vector used if the orientation of the insert allows the LDH promoter and the vector's lac promoter to direct transcription in the same direction
-
expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
expression in Escherichia coli
-
gene ldh-a, DNA and amino acid sequence determination and analysis
Q0GND8