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Information on EC 1.1.1.27 - L-lactate dehydrogenase and Organism(s) Bos taurus
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1.1.1.27 L-lactate dehydrogenaseIUBMB Comments
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
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- 1.1.1.27
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lactate dehydrogenase, lactic dehydrogenase, ldh-a, lactate dehydrogenase a, l-lactate dehydrogenase, ldh-5, lactic acid dehydrogenase, ldh-1, pfldh, alpha-hydroxybutyrate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, lactate
-
-
-
-
Epsilon crystallin
-
-
-
-
epsilon-crystallin
-
-
-
-
Immunogenic protein p36
-
-
-
-
L(+)-nLDH
-
-
-
-
L-(+)-lactate dehydrogenase
-
-
-
-
L-lactic acid dehydrogenase
-
-
-
-
L-lactic dehydrogenase
-
-
-
-
L-LDH
lactate dehydrogenase
lactate dehydrogenase NAD-dependent
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
lactic dehydrogenase
-
-
-
-
LDH
NAD-lactate dehydrogenase
-
-
-
-
proteins, specific or class, anoxic stress response, p34
-
-
-
-
L-LDH
-
-
-
-
lactate dehydrogenase
-
-
-
-
LDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
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
9001-60-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + NADH
L-lactate + NAD+
-
lactate yield is increased in the pyruvate decarboxylase 1/alcohol dehydrogenase 1 double mutant compared with that in the single pyruvate decarboxylase 1 mutant
-
-
?
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
L-lactate transport and metabolism, regulation and localization of enzyme participating in the pathway, overview
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
L-lactate transport and metabolism, regulation and localization of enzyme participating in the pathway, overview
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
([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
-
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
additional information
-
loss of LDH activity with increasing pressure and time treatment due to the combined effects of denaturation and aggregation, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
(heptylamino)(oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.133
(hexylamino)(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
(nonylamino)(oxo)acetic acid
Bos taurus
-
above, 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
Bos taurus
-
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
Bos taurus
-
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
Bos taurus
-
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
Bos taurus
-
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
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.116
amino(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.15
oxo(pentadecylamino)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.088
oxo[(4-phenylbutyl)amino]acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
Bos taurus
-
above, 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
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.158
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.025
[(2-methoxyethyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.09
[(3,3-diphenylpropyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.031
[(3-methoxypropyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(3-methylbutyl)amino](oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.107
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.186
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.168
[benzyl(methyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.043
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.046
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.059
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.032
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
inner compartment, transport and metabolism of L-lactate, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LDHB_BOVIN
334
0
36724
Swiss-Prot
other Location (Reliability: 2)
LDH6B_BOVIN
381
0
41592
Swiss-Prot
Mitochondrion (Reliability: 2)
LDHA_BOVIN
332
0
36598
Swiss-Prot
other Location (Reliability: 2)
F1MK19_BOVIN
241
0
26005
TrEMBL
other Location (Reliability: 2)
E1BNS9_BOVIN
332
0
36015
TrEMBL
other Location (Reliability: 2)
A0A3Q1M4R3_BOVIN
334
0
36769
TrEMBL
other Location (Reliability: 1)
A0A3Q1LY19_BOVIN
332
0
36583
TrEMBL
other Location (Reliability: 2)
A0A3Q1M5R4_BOVIN
341
0
37470
TrEMBL
other Location (Reliability: 2)
B0JYN3_BOVIN
334
0
36725
TrEMBL
other Location (Reliability: 2)
Q862D4_BOVIN
124
0
13699
TrEMBL
other Location (Reliability: 2)
Q2KJG0_BOVIN
241
0
26074
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
analysis of enzyme structure under high pressure conditions: even the lowest high pressure processing treatment of 206 MPa induces a reduction in LDH activity, and the course of reduction increases with high pressure processing treatment until complete inactivation at 482, 515, and 620 MPa. The structure of LDH shows gradual denaturation after exposure at 206 MPa for 6 min, leading to a random coil structure at both 515 and 620 MPa. The loss of LDH activity with increasing pressure and time treatment was due to the combined effects of denaturation and aggregation, structure analysis by far-ultraviolet circular dichroism spectroscopy and dynamic light scattetering
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
development of a recombinant yeast exhibiting efficient lactate production by substituting the coding region of PDC1 on chromosome XII for that of LDH through homologous recombination
-
expressed in Saccharomyces cerevisiae replacing disrupted pyruvate decarboxylase 1 and alcohol dehydrogenase 1
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
L-leucine depletion decreases the proteins synthesis, and also decreases L-lactate dehydrogenase B chain mRNA expression in bovine mammary alveolar cells cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
L-leucine depletion decreases the proteins synthesis, and also decreases L-lactate dehydrogenase B chain mRNA expression in bovine mammary alveolar cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishida, N.; Saitoh, S.; Tokuhiro, K.; Nagamori, E.; Matsuyama, T.; Kitamoto, K.; Takahashi, H.
Efficient production of L-Lactic acid by metabolically engineered Saccharomyces cerevisiae with a genome-integrated L-lactate dehydrogenase gene
Appl. Environ. Microbiol.
71
1964-1970
2005
Bos taurus, Bifidobacterium longum (P0CW93), Bifidobacterium longum
Saad, L.O.; Mirandola, S.R.; Maciel, E.N.; Castilho, R.F.
Lactate dehydrogenase activity is inhibited by methylmalonate in vitro
Neurochem. Res.
31
541-548
2006
Bos taurus, Rattus norvegicus
Kouassi, G.K.; Anantheswaran, R.C.; Knabel, S.J.; Floros, J.D.
Effect of high-pressure processing on activity and structure of alkaline phosphatase and lactate dehydrogenase in buffer and milk
J. Agric. Food Chem.
55
9520-9529
2007
Bos taurus
Atlante, A.; de Bari, L.; Bobba, A.; Marra, E.; Passarella, S.
Transport and metabolism of L-lactate occur in mitochondria from cerebellar granule cells and are modified in cells undergoing low potassium dependent apoptosis
Biochim. Biophys. Acta
1767
1285-1299
2007
Bos taurus
Tokuhiro, K.; Ishida, N.; Nagamori, E.; Saitoh, S.; Onishi, T.; Kondo, A.; Takahashi, H.
Double mutation of the PDC1 and ADH1 genes improves lactate production in the yeast Saccharomyces cerevisiae expressing the bovine lactate dehydrogenase gene
Appl. Microbiol. Biotechnol.
82
883-890
2009
Bos taurus
Granchi, C.; Bertini, S.; Macchia, M.; Minutolo, F.
Inhibitors of lactate dehydrogenase isoforms and their therapeutic potentials
Curr. Med. Chem.
17
672-697
2010
Bos taurus, Homo sapiens, Plasmodium falciparum, Plasmodium vivax, Plasmodium malariae, Plasmodium ovale
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