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2-glycerophosphate
-
activation
3-phosphoglycerate
-
activation
5-phosphoribosyl 1-diphosphate
-
activates
D-fructose 1,6-bisphosphate
D-fructose 1,6-diphosphate
activates wild-type enzyme and mutant enzymes F16Q/I37K/D38SC81S/N85R and F16Q/C81S/N85R
D-fructose-1,6-bisphophate
-
FBP, L-nLDH activity is FBP dependent
D-fructose-1,6-bisphosphate
fructose 1,6-bisphosphate
assures that the protein forms tetrameric uniformity and serves as an allosteric activator of the enzyme
fructose 2,6-diphosphate
-
activates
phosphate
-
slight activation of not activated enzyme, inhibition of fructose 1,6-diphosphate activated enzyme
tagatose 1,6-diphosphate
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stimulates
Triton X-100
23% activation at 0.1%
Urea
9% activation at 0.1%
D-fructose 1,6-bisphosphate
-
activates wild-type 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
-
activates wild-type enzyme
D-fructose 1,6-bisphosphate
allosteric
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
D-fructose-1,6-bisphosphate
best at 4-9 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 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
-
not dependent on 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
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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
-
dependent on
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
glucose 1,6-diphosphate
-
activates
glucose 1,6-diphosphate
-
activates
additional information
thermodynamic activation parameters, overview
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additional information
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thermodynamic activation parameters, overview
-
additional information
thermodynamic activation parameters, overview
-
additional information
-
thermodynamic activation parameters, overview
-
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
-
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
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the enzyme is induced by nitric aoxide
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additional information
thermodynamic activation parameters, overview
-
additional information
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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
-
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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