Information on EC 1.1.1.27 - L-lactate dehydrogenase

New: Word Map on EC 1.1.1.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.1.1.27
-
RECOMMENDED NAME
GeneOntology No.
L-lactate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-lactate + NAD+ = pyruvate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-60-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
-
SwissProt
Manually annotated by BRENDA team
strain 90
SwissProt
Manually annotated by BRENDA team
strain BS35, gene ldh
-
-
Manually annotated by BRENDA team
L. Med
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene ldhA encoding L-lactate dehydrogenase
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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
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
-
-
-
Manually annotated by BRENDA team
Molinema dessetae
-
-
-
Manually annotated by BRENDA team
strain AKR
-
-
Manually annotated by BRENDA team
-
-
-
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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Pontonia pinnophylax
inhabiting the mantle cavity of host Pinna nobilis
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Streptococcus mitior
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene ldhL
UniProt
Manually annotated by BRENDA team
GK24
-
-
Manually annotated by BRENDA team
GK24
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
(S)-lactate + NADP+
pyruvate + NADPH + H+
show the reaction diagram
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-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
show the reaction diagram
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-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
bromopyruvate + NADH
5-bromo-2-hydroxypropanoate + NAD+
show the reaction diagram
-
-
-
-
?
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
show the reaction diagram
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
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
phenyllactate + NAD+
show the reaction diagram
pyruvate + NADH
?
show the reaction diagram
-
-
-
-
?
pyruvate + NADH
L-lactate + NAD+
show the reaction diagram
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
pyruvate + NADH + H+
lactate + NAD+
show the reaction diagram
pyruvate + NADPH + H+
(S)-lactate + NADP+
show the reaction diagram
pyruvate ethyl ester + NADH
2-hydroxypropanoate ethyl ester
show the reaction diagram
-
-
-
-
?
pyruvate methyl ester + NADH
2-hydroxypropanoate methyl ester
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
show the reaction diagram
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
L-lactate + NAD+
pyruvate + NADH
show the reaction diagram
L-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
beta-NAD+
-
-
beta-NADH
-
-
FMN
-
contains non-covalently bound FMN as prosthetic group
nicotinamide hypoxanthine dinucleotide
-
alternative coenzyme
thio-NAD+
-
alternative coenzyme
additional information
-
the enzyme also utilizes both NAD(H) and NADP(H)
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
increases activity
Mg2+
-
20-30 mM, 10% increase in activity
Zn2+
-
1 mM, almost 2fold stimulation
additional information
not or poorly affected by 1 mM of EDTA, ATP, Mg2+, Co2+, Ca2+, Mn2+, and Ni2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
Alpha-NAD+
-
noncompetitive inhibitor versus beta-NAD+
amino(oxo)acetic acid
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
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
Chloroquine
citrate
-
-
citrate/phosphate buffer
-
at pH 5.4
-
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
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
19% inhibition at 1 mM
ethyl 3-(3-cyano-4-pyridyl)pyruvate
-
-
-
ethyl 3-(3-cyanopyridin-4-yl)-2-oxopropanoate
-
-
Fe2+
74% inhibition at 1 mM
Fe3+
complete inhibition at 1 mM
fructose 1,6-bisphosphate
fructose 1,6-diphosphate
glucose 6-phosphate
-
-
glutamate
Agama stellio stellio
-
both directions
gossylic nitrile 1,1'-diacetate
gossypol
gossypol lactone
HEPES buffer
-
-
iodoacetamide
iodoacetate
isocitrate
-
-
L-lactate
Lactate analogs
-
-
-
MES buffer
-
-
-
methylmalonate
Mg2+
Agama stellio stellio
-
both directions
NaCl
-
2 M, 36% loss of activity
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 enzyme‘s dissociation and partial unfolding
oxalate
oxaloacetate
Oxamate
oxo(pentadecylamino)acetic acid
oxo(phenylamino)acetic acid
oxo[(2-phenylethyl)amino]acetic acid