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Literature summary for 1.1.1.27 extracted from

  • Paventi, G.; Pizzuto, R.; Passarella, S.
    The occurrence of L-lactate dehydrogenase in the inner mitochondrial compartment of pig liver (2017), Biochem. Biophys. Res. Commun., 489, 255-261 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
oxamate 0.1 mM, inhibition of NADH oxidation rate by about 60% Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
pyruvate the enzyme shows hyperbolic dependence on the substrate concentration Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion mL-LDH is restricted in inner compartment Sus scrofa 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
the enzyme shows hyperbolic dependence on the substrate concentration Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + NADH + H+
-
Sus scrofa (S)-lactate + NAD+
-
r

Synonyms

Synonyms Comment Organism
mL-LDH
-
Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
pyruvate the enzyme shows hyperbolic dependence on the substrate concentration Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
-
Sus scrofa