1.1.1.27: L-lactate dehydrogenase
This is an abbreviated version!
For detailed information about L-lactate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.27
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1.1.1.27
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creatine
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aminotransferase
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myocardial
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isoenzymes
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cardiac
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dismutase
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necrosis
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malondialdehyde
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ischemia
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albumin
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catalase
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lymphoma
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infarct
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transaminase
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reperfusion
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lymphocyte
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platelet
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sod
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artery
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alt
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pulmonary
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hemoglobin
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c-reactive
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hepatocytes
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coronary
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wistar
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bilirubin
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gsh
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hypoxia
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caspase-3
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cardioprotective
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ventricular
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fever
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admission
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covid-19
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admitted
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cardiomyocytes
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ischemia-reperfusion
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phosphokinase
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hepatotoxicity
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troponin
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progression-free
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bronchoalveolar
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chest
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hemolysis
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trypan
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uric
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non-hodgkin
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coronavirus
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d-dimer
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medicine
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degradation
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diagnostics
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biotechnology
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analysis
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drug development
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synthesis
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agriculture
- 1.1.1.27
- creatine
- aminotransferase
- myocardial
- isoenzymes
- cardiac
- dismutase
- necrosis
- malondialdehyde
- ischemia
- albumin
- catalase
- lymphoma
- infarct
- transaminase
-
reperfusion
- lymphocyte
- platelet
- sod
- artery
-
alt
- pulmonary
- hemoglobin
-
c-reactive
- hepatocytes
- coronary
- wistar
- bilirubin
- gsh
- hypoxia
- caspase-3
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cardioprotective
- ventricular
- fever
-
admission
- covid-19
-
admitted
-
cardiomyocytes
-
ischemia-reperfusion
-
phosphokinase
-
hepatotoxicity
- troponin
-
progression-free
-
bronchoalveolar
- chest
-
hemolysis
-
trypan
-
uric
-
non-hodgkin
- coronavirus
-
d-dimer
- medicine
- degradation
- diagnostics
- biotechnology
- analysis
- drug development
- synthesis
- agriculture
Reaction
Synonyms
A4-LDH, AdhE, alpha-HBDH, alpha-hydroxybutyrate dehydrogenase, anaerobic lactate dehydrogenase, BbLDH, dehydrogenase, lactate, eLDHA, eLDHB, Epsilon crystallin, epsilon-crystallin, H4-L-lactate dehydrogenase, HBDH, heart LDH, Immunogenic protein p36, L(+)-nLDH, L-(+)-lactate dehydrogenase, L-lactate dehydrogenase, L-lactate dehydrogenase B, L-lactic acid dehydrogenase, L-lactic dehydrogenase, L-LDH, L-Ldh0845, L-nLDH, lactate dehydrogenase, lactate dehydrogenase 5, lactate dehydrogenase A, lactate dehydrogenase B, lactate dehydrogenase NAD-dependent, lactic acid dehydrogenase, lactic dehydrogenase, LctD, LDH, LDH-1, LDH-2, LDH-3, LDH-4, LDH-5, LDH-A, LDH-A4, LDH-m4, LDH1, LDH2, LdhA, LDHB, ldhL, LDHL1, LDHL2, LOX, LutACB, mL-LDH, mLDH, More, muscle LDH, NAD-dependent lactate dehydrogenase, NAD-lactate dehydrogenase, NGO0904, NGO0905, NGO0906, nitric oxideinducible l-lactate dehydrogenase, PfLDH, proteins, specific or class, anoxic stress response, p34, Sa-LDH-1, SMU.1115, SMU_1115, TeLdhL, Tsac_0416
ECTree
1.1.1.27 L-lactate dehydrogenaseAdvanced search results
results (
results (Subunits
Subunits on EC 1.1.1.27 - L-lactate dehydrogenase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
heterotetramer
the heterotetrameric LDH (H2M2) from swine brain is formed by two subunit of LDHA and two subunits of LDHB
homotetramer
octamer
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8 * 35000, enzyme also exists in an tetrameric enzyme form, SDS-PAGE, meniscus depletion experiments in 4 M guanidinium chloride
tetramer
additional information
?
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x * 42000, recombinant His6-tagged LctD, SDS-PAGE
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?
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x * 34400, isoform LDHL2, calculated from sequence and SDS-PAGE
?
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x * 35500, isoform LDHL1, calculated from sequence and SDS-PAGE
?
Sporolactobacillus inulinus YBS1-5
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x * 34400, isoform LDHL2, calculated from sequence and SDS-PAGE
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?
Sporolactobacillus inulinus YBS1-5
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x * 35500, isoform LDHL1, calculated from sequence and SDS-PAGE
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?
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x * 39000, recombinant His6-tagged LDH-1, SDS-PAGE, x * 34600, about, sequence calculation
homotetramer
each monomer has one active site, and the tetramer has two allosteric sites, each of which is situated at the Y-axis interface between two monomers
homotetramer
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each monomer has one active site, and the tetramer has two allosteric sites, each of which is situated at the Y-axis interface between two monomers
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homotetramer
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dimer of dimers, differential chemical crosstalk between the monomers
tetramer
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wild-type enzyme and N-terminal deletion mutants lacking the first 5 or the first 10 amino acids
additional information
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Iguana iguana, overview
additional information
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molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Iguana iguana, overview
additional information
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analysis of enzyme structure under high pressure conditions: even the lowest high pressure processing treatment of 206 MPa induces a reduction in LDH activity, and the course of reduction increases with high pressure processing treatment until complete inactivation at 482, 515, and 620 MPa. The structure of LDH shows gradual denaturation after exposure at 206 MPa for 6 min, leading to a random coil structure at both 515 and 620 MPa. The loss of LDH activity with increasing pressure and time treatment was due to the combined effects of denaturation and aggregation, structure analysis by far-ultraviolet circular dichroism spectroscopy and dynamic light scattetering
additional information
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
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primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
the ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate
additional information
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the ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate
additional information
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview
additional information
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primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview
additional information
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secondary, tertiary, and quaternary structure analysis, and structure comparisons, overview.The subunit structure of L-LDH can be divided into N-terminal NADH-binding domain and C-terminal catalytic domain
additional information
secondary, tertiary, and quaternary structure analysis, and structure comparisons, overview.The subunit structure of L-LDH can be divided into N-terminal NADH-binding domain and C-terminal catalytic domain
additional information
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secondary, tertiary, and quaternary structure analysis, and structure comparisons, overview.The subunit structure of L-LDH can be divided into N-terminal NADH-binding domain and C-terminal catalytic domain
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additional information
three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview
additional information
three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview
additional information
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three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview
additional information
three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview
additional information
three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview
additional information
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three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview
additional information
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binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview
additional information
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structure comparison of LDH-M and LDH-H subunit isoforms, the homotetramers have essentially the same tertiary structure, while the hybrid tetramers show different structures, overview. Rossmann fold topology, structure comparison to the enzyme from Plasmodium falciparum, PDB IDs 1i10 and 1ldg, Ser163 is a highly conserved residue amongst human hLDH isozymes, corresponds to Leu163 in PfLDH, differences occur mainly in the N-terminus, overview
additional information
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Amblyrhynchus cristatus, overview
additional information
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molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Amblyrhynchus cristatus, overview
additional information
LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers
additional information
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LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers
additional information
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LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers
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additional information
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three bands detected after SDS-PAGE with MW of 60000 Da, 66000 Da and 74000 Da
additional information
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three-dimensional structures of the L-LDH-NADH complex of enzyme from muscle and heart, molecular analysis, overview
additional information
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Rossmann fold topology, structure comparison to the enzyme from Homo sapiens, PDB IDs 1i10 and 1ldg, differences occur mainly in the N-terminus, overview
additional information
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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
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
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in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
TeLdhL contains a GXGXXG motif common to most NAD-linked dehydrogenases close to the N-terminus, and a putative signal peptide with cleavage site between residue 26 and 27, deletion of the putative signal peptide sequence leads to nonexpression of TeLdhL
additional information
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TeLdhL contains a GXGXXG motif common to most NAD-linked dehydrogenases close to the N-terminus, and a putative signal peptide with cleavage site between residue 26 and 27, deletion of the putative signal peptide sequence leads to nonexpression of TeLdhL
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additional information
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
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primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
