Application | Comment | Organism |
---|---|---|
diagnostics | low LDH affinity kinetics can be a diagnostic parameter for human breast cancer | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | LDH has different kinetic characteristics in breast tumors compared to normal breast tissues. Tumor LDH affinity in the pyruvate reduction reaction is the same as for normal LDH but Vmax of cancerous LDH is higher relative to normal LDH. In the lactate oxidation reaction, affinity of tumor LDH for lactate and NAD+ is lower than for normal LDH, also the enzyme efficiency for lactate and NAD+ is higher in normal samples. The activation energy for the pyruvate reduction reaction is higher in cancerous tissues. The enzyme in forward reaction in both tissues displays sigmoidal kinetics with respect to pyruvate and NADH | Homo sapiens | |
0.5 | - |
NAD+ | pH 8.0, temperature not specified in the publication, healthy breast tissue enzyme | Homo sapiens | |
0.99 | - |
NAD+ | pH 8.0, temperature not specified in the publication, breast cancer tissue enzyme | Homo sapiens | |
10.73 | - |
(S)-lactate | pH 8.0, temperature not specified in the publication, healthy breast tissue enzyme | Homo sapiens | |
21.78 | - |
(S)-lactate | pH 8.0, temperature not specified in the publication, breast cancer tissue enzyme | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | Homo sapiens | - |
pyruvate + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P07864 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from malignant and healthy breast tissue 14.3fold by anion exchange and affinity chromatography | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
breast | normal and malignant human breast tissues | Homo sapiens | - |
breast cancer cell | normal and malignant human breast tissues. The enzyme is highly expressed in breast | Homo sapiens | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.6 | - |
lactate oxidation, pH 8.0, 25°C, healthy breast tissue | Homo sapiens |
0.63 | - |
lactate oxidation, pH 8.0, 25°C, breast cancer tissue | Homo sapiens |
1.237 | - |
NAD+ reduction, pH 8.0, 25°C, healthy breast tissue | Homo sapiens |
1.282 | - |
NAD+ reduction, pH 8.0, 25°C, breast cancer tissue | Homo sapiens |
1.37 | - |
NADH oxidation, pH 8.0, 25°C, healthy breast tissue | Homo sapiens |
1.747 | - |
pyruvate reduction, pH 8.0, 25°C, healthy breast tissue | Homo sapiens |
2.788 | - |
NADH oxidation, pH 8.0, 25°C, breast cancer tissue | Homo sapiens |
4.034 | - |
pyruvate reduction, pH 8.0, 25°C, breast cancer tissue | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | - |
Homo sapiens | pyruvate + NADH + H+ | - |
r | |
pyruvate + NADH + H+ | - |
Homo sapiens | (S)-lactate + NAD+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
LDH | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
activation energy is measured at 5-42°C | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Homo sapiens | |
NADH | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | lactate dehydrogenase (LDH) is a critical enzyme during aerobic glycolysis as it is typically responsible for the production of lactate and regeneration of NAD+, which allows for the continued functioning of glycolysis even in the absence of oxygen. LDH is the final enzyme in glycolysis pathway that catalyzes interconversion of pyruvate and lactate and it also regenerates NAD+, which is necessary for continued high glycolysis rate in cancer cells | Homo sapiens |