Affinage · Plasmodium

PF3D7_1139700

adrenodoxin reductase, putative

Annotated
2026-09-08
2 papers in source corpus 1 papers cited in narrative 1 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1139700 is annotated as a putative adrenodoxin reductase and characterized as a ferredoxin-NADP(+) reductase (FNR) of the glutathione reductase structural type in Plasmodium falciparum, with biochemical evidence indicating novel modes of FAD- and NADP(H)-binding relative to other FNR family members (PMID:18307973). Within this family, adrenodoxin reductase homologs can catalyze oxidation of NADP(+) to its 4-oxo derivative (PMID:18307973). Beyond this single biochemical characterization (PMID:18307973), no further mechanistic, structural, or in vivo functional detail specific to PF3D7_1139700 has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2008 Low

    Establishing whether the Plasmodium falciparum FNR/adrenodoxin reductase homolog behaves like canonical FNR enzymes addressed whether this parasite protein could be a distinct, potentially druggable flavoenzyme.

    Evidence Biochemical characterization and structural comparison of P. falciparum FNR within the FNR family

    PMID:18307973

    Open questions at the time
    • No primary in vitro kinetic assay or mutagenesis data on PF3D7_1139700 itself is described
    • No structural model of the parasite protein is provided
    • Physiological electron partner (ferredoxin vs adrenodoxin) and cellular role in P. falciparum are not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unknown what the endogenous redox partners, subcellular localization, and biological pathway of PF3D7_1139700 are, and whether it is essential or validated as a drug target in P. falciparum.
  • No genetic knockout or essentiality data
  • No reconstitution of electron transfer with a defined parasite ferredoxin/adrenodoxin
  • No structural determination of the parasite enzyme

Mechanism profile

Synthesis pass · controlled-vocabulary classification

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 The ferredoxin-NADP(+) reductase (FNR) from Plasmodium falciparum (corresponding to PF3D7_1139700, a glutathione reductase-type/adrenodoxin reductase homolog) was characterized biochemically, with findings indicating novel modes of FAD- and NADP(H)-binding relative to other FNR family members, and adrenodoxin reductase homologs in this family were shown to catalyze the oxidation of NADP(+) to its 4-oxo derivative. Biochemical characterization and structural comparison (review of recent experimental findings on FNR structure-function relationships) Archives of biochemistry and biophysics Low 18307973

Source papers

Stage 0 corpus · 2 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2008 Structural and functional diversity of ferredoxin-NADP(+) reductases. Archives of biochemistry and biophysics 127 18307973
2026 Free Radical Formation in the Reactions of Redox-Active Drugs and Xenobiotics with Mitochondrial Flavoenzymes. Biomolecules 0 42352277