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Literature summary for 4.1.1.65 extracted from

  • Choi, J.Y.; Kumar, V.; Pachikara, N.; Garg, A.; Lawres, L.; Toh, J.Y.; Voelker, D.R.; Ben Mamoun, C.
    Characterization of Plasmodium phosphatidylserine decarboxylase expressed in yeast and application for inhibitor screening (2016), Mol. Microbiol., 99, 999-1014 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.65

Application

Application Comment Organism
analysis use of the complementation of a Saccharomyces cerevisiae mutant for screening inhibitors Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
additional information amino acids between positions 40 and 70 are critical for proenzyme processing and decarboxylase activity. During progressive removal of 10 amino acid segments between positions 1 and 70 of PSD, deletions up to residue 50 do not reduce the ability of the enzyme to complement a Saccharomyces cerevisiae mutant. Deletions of the first 60 or 70 residues result in loss of complementation in both solid and liquid media Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
7-chloro-N-(4-ethoxyphenyl)-4-quinolinamine inhibitor with potent activity against Plasmodium falciparum, and low toxicity toward mammalian cells Plasmodium falciparum
7-chloro-N-(4-propylphenyl)-4-quinolinamine 0.01 mM, 29% inhibition, 0.1 mM, 76% inhibition of catalysis. Compound inhibits PSD activity and blocks Plasmodium falciparum blood stage development in the malaria murine model Plasmodium falciparum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane PSD is catalytically active in both soluble and membrane fractions, with a membrane/soluble distribution of 3/1 Plasmodium falciparum 16020
-
soluble PSD is catalytically active in both soluble and membrane fractions, with a membrane/soluble distribution of 3/1 Plasmodium falciparum
-
-

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q9GPP8
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification amino acids between positions 40 and 70 are critical for proenzyme processing and decarboxylase activity Plasmodium falciparum

General Information

General Information Comment Organism
physiological function enzyme is able to complement a Saccharomyces cerevisiae PSD mutant lacking PSD1 and PSD2 and DPL1 activities Plasmodium falciparum