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Literature summary for 1.1.1.27 extracted from

  • Qiu, L.; Gulotta, M.; Callender, R.
    Lactate dehydrogenase undergoes a substantial structural change to bind its substrate (2007), Biophys. J., 93, 1677-1686.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
oxamate
-
Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information stopped-flow kinetics, steady-state kinetics, and thermodynamics of free and NADH-bound enzyme, overview Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Sus scrofa
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
H4-L-lactate dehydrogenase
-
Sus scrofa
LDH
-
Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Sus scrofa
NADH
-
Sus scrofa

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics Sus scrofa