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
LITERATURE
(S)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
mechanism
-
(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
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
Glycolysis / Gluconeogenesis
-
-
heterolactic fermentation
-
-
L-lactaldehyde degradation
-
-
lactate fermentation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Propanoate metabolism
-
-
pyruvate fermentation to lactate
-
-
Pyruvate metabolism
-
-
superpathway of glucose and xylose degradation
-
-
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
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
-
-
-
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 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
UNIPROT
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
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
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
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
Thermoanaerobacter ethanolicus JW200
gene ldhL
UniProt
Manually annotated by BRENDA team
Thermus caldophilus GK24
GK24
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
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
-
although Ldh-2 contributes to lactate production, Ldh-1 plays the major role in energy metabolism in Enterococcus faecalis
physiological function
-
LADH-A is a key enzyme that couples L-lactate production to reoxidation of NADH formed during glycolysis
physiological function
-
LDH-A deficiency causes myoglobinuria
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
-
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
metabolism
Aggregatibacter actinomycetemcomitans HK1651 and VT1169
-
the enzyme catalyzes the first step in L-lactate catabolism
-
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
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
-
the ldh-1 mutants detoxifies excess pyruvate by converting it to acetoin
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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 + H+
2,3-dihydroxypropanoate + NADP+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
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, 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
L-lactate + NAD+
show the reaction diagram
-
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
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
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
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+
-
coenzyme
NAD+
-
coenzyme
NAD+
-
coenzyme
NAD+
-
coenzyme
NAD+
-
coenzyme
NAD+
-
coenzyme
NAD+
Molinema dessetae
-
coenzyme
NAD+
-
coenzyme
NAD+
Q6JH30
-
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+
-
-
NAD+
Q0GND8
-
NAD+
P0C2T6
-
NAD+
Pontonia pinnophylax
-
-
NAD+
-
binding structure, overview
NAD+
B7XH73, C6L1K8
;
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
Molinema dessetae
-
coenzyme
NADH
-
coenzyme
NADH
O13276
coenzyme
NADH
O13277
coenzyme
NADH
O13278
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
-
coenzyme
NADH
Q6JH30
-
NADH
Agama stellio stellio
-
-
NADH
-
-
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
-
-
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
-
-
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+
NADP+
-
-
NADPH
-
coenzyme
NADPH
-
-
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
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
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+
-
partial
Cd2+
-
0.1 mM and 1.0 mM, weak inhibition
Chloroquine
-
IC50: 5.5 mM
Chloroquine
-
-
citrate
-
-
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
Q27743
-
gossypol
Q6JH30
-
gossypol
Q7Z0X7
competitive with NADH
gossypol
-
-
gossypol
-
a polyphenolic binaphthyl disesquiterpene from Gossypium sp.
gossypol lactone
Q27743
-
gossypol lactone
Q6JH30
-
HEPES buffer
-
-
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
-
-
Ni2+
-
partial
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
-
-
oxalate
Molinema dessetae
-
noncompetitive with pyruvate, competitive with lactate
oxalate
Agama stellio stellio
-
both directions
oxalate
-
0.5 mM, 28% inhibition
oxaloacetate
-
-
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
-
-
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
-
-
p-chloromercuribenzoate
Molinema dessetae
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
slight
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
-
phosphate
-
slight activation of non-activated enzyme, inhibition of fructose 1,6-diphosphate activated enzyme
phosphate
-
-
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
COMMENTARY
LITERATURE
IMAGE
2-glycerophosphate
-
activation
3-phosphoglycerate
-
activation
5-phosphoribosyl 1-diphosphate
-
activates
ADP
-
-
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]
SUBSTRATE
ORGANISM
UNIPROT
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
0.015
NAD+
-
-
0.02
NAD+
Agama stellio stellio
-
pH 7.5, 25C
0.065
NAD+
-
-
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
0.9
NAD+
-
-
0.95
NAD+
-
pH 8.2, isoenzyme II
1.1
NAD+
-
-
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
0.024
NADH
-
-
0.032
NADH
-
-
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
0.061
NADH
-
-
0.065
NADH
-
mutant enzyme S163L
0.077
NADH
P0C2T6
pH 6.0, 30C, isozyme LDHB
0.08
NADH
-
-
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
0.11
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
-
-
0.25
pyruvate
-
with 1.0 mM fructose 1,6-diphosphate
0.25
pyruvate
-
-
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
pyruvate
-
-
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]
SUBSTRATE
ORGANISM
UNIPROT
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
6.9
NAD+
-
-
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
40
NAD+
-
pH 7.5
60
NAD+
-
enzyme from heart
65
NAD+
Q27743
pH 9.2, 25C
96
NADH
-
pH 7.5
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
2330
NADH
-
-
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
643
pyruvate
-
-
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]
INHIBITOR
ORGANISM
UNIPROT
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]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
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
-
-
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
ORGANISM
UNIPROT
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
-
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
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
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
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
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
P0C2T6
isozyme LDH, sequence calculation
5.2
P0C2T6
isozyme LDHB, sequence calculation
5.5
-
heart-type isozyme
8.03
-
theoretical isoelectric point
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the level of L-lactate dehydrogenase B are specifically increased in non-small cell lung cancer
Manually annotated by BRENDA team
-
differential expressions of LDH isozymes in different types of tumors
Manually annotated by BRENDA team
-
endometrial and ovarian
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
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
Q0GND8
muscle isozyme
Manually annotated by BRENDA team
-
muscle-type isozyme, i.e. M4 isoform
Manually annotated by BRENDA team
-
isoenzyme LDH-B4 and LDH-A2B2
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
-
metabolic adaptation of Staphylococcus aureus to nitrosative stress, overview
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
P50933
structural features for structural stability, comparison to enzymes from other species in extreme environments
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
-
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
-
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
Q27797
LDH1 is absent from bradyzoites, LDH2 is absent from tachyzoites
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
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 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Cryptosporidium parvum (strain Iowa II)
Cryptosporidium parvum (strain Iowa II)
Cryptosporidium parvum (strain Iowa II)
Cryptosporidium parvum (strain Iowa II)
Cryptosporidium parvum (strain Iowa II)
Cryptosporidium parvum (strain Iowa II)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Plasmodium berghei (strain Anka)
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35200
-
sequence analysis
700558
39200
Q27797
antibodies
697818
39900
Q27797
antibodies
697818
65000 - 67000
-
gel filtration
286440
77000
Q9GT92
monomer, sedimentation velocity
656764
78000
-
gel filtration
687249
113000
Molinema dessetae
-
gel filtration
286459
125000 - 138000
-
gel filtration
286470
130000
-
sucrose density gradient centrifugation
286435
130000
-
tetramer, sucrose density gradient centrifugation in presence of fructose 1,6-diphosphate and NADH
286452
132000
-
non-denaturing gel electrophoresis
286434
134000
-
gel filtration
286468
134000
Q9GT92
dimer, sedimentation velocity
656764
135000
-
gel filtration
286434
139000
-
gel filtration
286432
140000
-
ultracentrifugal studies
286433
140000
-
tetramer, gel filtration
286457
140000
-
gel filtration
286461
144000
-
equilibrium sedimentation
286431
150000
-
disc gel electrophoresis
286445
187000
-
non-denaturing gel electrophoresis
286432
269300
-
meniscus depletion experiments
286457
280000
-
octamer, gel filtration
286457
280900
-
equilibrium sedimentation
286457
670000
-
above, gel filtration
286450