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Literature summary for 1.1.1.27 extracted from

  • Talaiezadeh, A.; Shahriari, A.; Tabandeh, M.R.; Fathizadeh, P.; Mansouri, S.
    Kinetic characterization of lactate dehydrogenase in normal and malignant human breast tissues (2015), Cancer Cell Int., 15, 19.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
diagnostics low LDH affinity kinetics can be a diagnostic parameter for human breast cancer Homo sapiens

KM Value [mM]

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactate + NAD+ Homo sapiens
-
pyruvate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens P07864
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from malignant and healthy breast tissue 14.3fold by anion exchange and affinity chromatography Homo sapiens

Source Tissue

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 [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
LDH
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
activation energy is measured at 5-42°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
NADH
-
Homo sapiens

General Information

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