GPI

PF3D7_1436000 (GPI) encodes a functional glucose-6-phosphate isomerase of Plasmodium falciparum, isolated by genetic complementation of an E. coli double mutant lacking glucose phosphate isomerase, demonstrating that the encoded protein is catalytically active (PMID:2197273). The gene comprises a 1773-bp intronless open reading frame on chromosome 14, with its translation initiation site defined by deletional and site-directed mutagenesis, and shares ~34% amino acid identity with the human enzyme, the conservation being highest in regions corresponding to the proposed active sites (PMID:2197273). Beyond this initial identification and functional confirmation (PMID:2197273), no further mechanistic detail on PF3D7_1436000 has been characterized in the available corpus.

1. 1990 Medium

   Whether P. falciparum encodes a functional glucose-6-phosphate isomerase was unknown; complementation of a glucose phosphate isomerase-deficient E. coli mutant established that this gene produces a catalytically active enzyme.

   Evidence Genetic complementation in E. coli, gene cloning and sequencing, with deletional and oligonucleotide-mediated site-specific mutagenesis to define the initiation site

   PMID:2197273

   Open questions at the time

   • No structural model or biochemical kinetic characterization of the P. falciparum enzyme
   • The enzyme's role in parasite glycolysis or its essentiality in vivo was not tested
   • No inhibitor or drug-target validation reported

• How PF3D7_1436000 functions within P. falciparum metabolism, its localization, regulation, and essentiality during the parasite life cycle remain uncharacterized in the available corpus.
• No subcellular localization determined
• No genetic knockout or essentiality data in the parasite
• No interaction partners or pathway context established beyond inferred glycolytic activity