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Literature summary for 6.3.1.20 extracted from

  • Allary, M.; Lu, J.Z.; Zhu, L.; Prigge, S.T.
    Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum (2007), Mol. Microbiol., 63, 1331-1344.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
8-bromooctanoate inhibition of isoform LipL1 activity, in vitro growth arrest of Plasmodium falciparum Plasmodium falciparum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion in intraerythrocytic parasites, enzyme catalyzes incorporation of lipoate to mitochondrial proteins Plasmodium falciparum 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Plasmodium falciparum lipoate scavenging by enzymes drives mitochondrial lipoylation, while apicoplast lipoylation relies on biosynthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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enzyme homologues LipL1 and LipL2
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Source Tissue

Source Tissue Comment Organism Textmining
additional information in intraerythrocytic parasites, enzyme catalyzes incorporation of lipoate to mitochondrial proteins Plasmodium falciparum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information lipoate scavenging by enzymes drives mitochondrial lipoylation, while apicoplast lipoylation relies on biosynthesis Plasmodium falciparum ?
-
?
additional information no substrate: pyruvate dehydrogenase subunit E2 Plasmodium falciparum ?
-
?