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Literature summary for 1.1.1.27 extracted from

  • Wiwanitkit, V.
    Plasmodium and host lactate dehydrogenase molecular function and biological pathways: implication for antimalarial drug discovery (2007), Chem. Biol. Drug Des., 69, 280-283.
    View publication on PubMed

Application

Application Comment Organism
drug development a selective lactate dehydrogenase inhibitor targeting the L-malate dehydrogenase function of Plasmodium falciparum and its corresponding tricarboxylic acid cycle provides an attractive therapeutic opportunity, in contrast to LDH targeting due to the functional similarity between human and parasite LDHs Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
Chloroquine
-
Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactate + NAD+ Plasmodium falciparum involved in glycolysis pyruvate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + NAD+
-
Plasmodium falciparum pyruvate + NADH + H+
-
r
(S)-lactate + NAD+ involved in glycolysis Plasmodium falciparum pyruvate + NADH + H+
-
r
additional information Plasmodium falciparum lactate dehydrogenase has L-malate dehydrogenase activity, which plays a role in the tricarboxylic acid cycle Plasmodium falciparum ?
-
?

Synonyms

Synonyms Comment Organism
LDH
-
Plasmodium falciparum