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
-
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
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results (Activating Compound
Activating Compound on EC 1.1.1.27 - L-lactate dehydrogenase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
D-fructose 1,6-diphosphate
activates wild-type enzyme and mutant enzymes F16Q/I37K/D38SC81S/N85R and F16Q/C81S/N85R
fructose 1,6-bisphosphate
assures that the protein forms tetrameric uniformity and serves as an allosteric activator of the enzyme
phosphate
-
slight activation of not activated enzyme, inhibition of fructose 1,6-diphosphate activated enzyme
D-fructose 1,6-bisphosphate
-
activates the pyruvate reduction
D-fructose 1,6-bisphosphate
activation constants of isozymes at different pH values, overview
D-fructose-1,6-bisphosphate
enzyme binding structure, overview. The allosteric enzyme requires fructose-1,6-bisphosphate (FBP), an intermediate in the glycolysis pathway, for catalytic activities. FBP may play a role in stabilizing and maintaining the tetrameric structure
D-fructose-1,6-bisphosphate
the allosteric enzyme requires fructose-1,6-bisphosphate (FBP), an intermediate in the glycolysis pathway, for catalytic activities. FBP may play a role in stabilizing and maintaining the tetrameric structure
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
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
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 not 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 not 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
Lactobacillus mesenteroides
-
L-lactate dehydrogenase form which is not 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
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
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
-
L-lactate dehydrogenase form which is not 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 not 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 not 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 not 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 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 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
-
concentration required for 50% maximal activity is about 0.15 mM
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 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
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
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
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
-
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
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
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 not 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 not activated by fructose 1,6-diphosphate
additional information
thermodynamic activation parameters, overview
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additional information
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thermodynamic activation parameters, overview
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additional information
thermodynamic activation parameters, overview
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additional information
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thermodynamic activation parameters, overview
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additional information
direct phosphorylation of LDHA at Y10 and Y83 strongly enhances LDH-5 tetramer formation and cofactor binding, resulting in significantly increased LDH enzymatic activity
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
thermodynamic activation parameters, overview
-
additional information
-
thermodynamic activation parameters, overview
-
additional information
the enzyme also shows some activity in the absence of D-fructose-1,6-bisphosphate, with a pH optimum of pH 4.0
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additional information
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the enzyme also shows some activity in the absence of D-fructose-1,6-bisphosphate, with a pH optimum of pH 4.0
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