Affinage · Plasmodium

ENR

PF3D7_0615100 · enoyl-acyl carrier reductase

Annotated
2026-09-08
46 papers in source corpus 19 papers cited in narrative 19 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0615100 (ENR) is the NADH-dependent enoyl-ACP reductase of the apicoplast-localized type II fatty acid synthesis (FAS II) pathway in Plasmodium falciparum, catalyzing the terminal reductive step of each fatty acid elongation cycle (PMID:11175846, PMID:17485508). Its role was fixed biochemically by in vitro reconstitution of the complete FAS II elongation module (ENR together with FabB/F, FabG, and FabZ), where inhibition of ENR caused accumulation of the upstream enoyl substrate intermediate, confirming ENR as the enzyme that completes each round of chain elongation (PMID:17485508). Kinetically, ENR follows an ordered mechanism, uses NADH as reductant and enoyl-CoA/ACP substrates (Km values of 165 µM for crotonyl-CoA and 33 µM for NADH), and is inhibited by triclosan through a slow-tight-binding two-step mechanism (Ki = 53 nM, Ki* ≈ 96 pM) that is competitive with NADH and facilitated by NAD+ (PMID:11735121, PMID:15086316, PMID:21603269). Crystal structures in binary (NADH) and ternary (triclosan/NAD+) states, combined with active-site mutagenesis, define the drug-binding pocket and identify residues Ala-217, Asn-218, Met-281, Phe-368 and the substrate-binding-loop residue Ala-372 as determinants of inhibitor binding and enzyme function (PMID:11792710, PMID:15139852, PMID:21280175). Genetic knockout established that ENR is dispensable for asexual blood-stage replication but stage-specifically essential: FabI-deficient parasites fail in liver-stage development and the liver-to-blood transition in rodent Plasmodium (P. berghei/P. yoelii), whereas in P. falciparum deletion abolishes sporozoite development within mosquito midgut oocysts (PMID:19064257, PMID:19068099, PMID:24297444). ENR protein localizes to the apicoplast of oocyst, sporozoite, and liver stages, colocalizing with acyl carrier protein (PMID:19068099, PMID:24297444).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 2001 High

    Establishing that Plasmodium possesses a druggable de novo FAS II pathway required demonstrating that a specific enzyme, ENR, catalyzes fatty acid synthesis and can be pharmacologically blocked.

    Evidence Enzyme purification and [14C]acetate/[14C]malonyl-CoA fatty acid labeling with triclosan inhibition in P. falciparum

    PMID:11175846

    Open questions at the time
    • Did not resolve the precise chemical step catalyzed within the elongation cycle
    • Did not define kinetic parameters or cofactor preference
  2. 2001 High

    Defining the cofactor dependence and inhibition logic clarified how triclosan engages ENR, showing NAD+ facilitates inhibitor binding and NADH competes with it.

    Evidence Recombinant expression in E. coli and steady-state kinetics of purified P. falciparum ENR

    PMID:11735121

    Open questions at the time
    • Kinetics used crotonyl-CoA rather than physiological enoyl-ACP substrate
    • Two kinetic parameters only; full mechanism not resolved
  3. 2002 High

    Solving the ENR crystal structure in ligand-bound states provided the structural basis for cofactor and inhibitor binding and its apicoplast targeting prediction.

    Evidence X-ray crystallography of binary NADH and ternary triclosan/NAD+ complexes of P. falciparum ENR

    PMID:11792710

    Open questions at the time
    • Structural prediction of apicoplast localization not yet experimentally confirmed
    • Substrate (enoyl-ACP) complex not captured
  4. 2004 High

    Characterizing triclosan as a slow-tight-binding inhibitor and mapping the residues that control its binding explained the exceptional potency and defined the drug-binding pocket.

    Evidence Steady-state kinetics, fluorescence, SPR, and active-site site-directed mutagenesis of P. falciparum ENR

    PMID:15086316 PMID:15139852

    Open questions at the time
    • Whether these residues also govern natural substrate turnover not fully separated from inhibitor binding
    • Mutant enzyme stability/catalytic effects not exhaustively profiled
  5. 2007 High

    Reconstituting the four-enzyme FAS II elongation module in vitro placed ENR mechanistically as the terminal reductive step of each elongation cycle.

    Evidence In vitro multienzyme reconstitution from butyryl-ACP with MALDI-TOF detection of intermediate accumulation upon ENR inhibition, P. falciparum enzymes

    PMID:17485508

    Open questions at the time
    • Physiological chain-length products and in vivo flux not quantified
    • Interplay with acyl carrier protein handoff not structurally resolved
  6. 2007 High

    Comparative structures and expanded inhibitor complexes refined the active-site pocket and explained species-selective inhibitor affinity within apicomplexan ENRs.

    Evidence X-ray crystallography of ENR-inhibitor complexes plus enzyme and parasite growth inhibition, with comparison to T. gondii ENR

    PMID:17327670 PMID:17567585

    Open questions at the time
    • Structural insights not yet translated to whole-parasite efficacy against relevant stages
    • Selectivity over human targets not addressed here
  7. 2008 High

    Genetic knockout resolved when ENR is actually required, showing it is dispensable in blood stages but essential for liver-stage development and the liver-to-blood transition in rodent malaria.

    Evidence Targeted fabI deletion in P. falciparum and P. berghei/P. yoelii, apicoplast colocalization, and mouse liver-stage infection assays

    PMID:19064257 PMID:19068099

    Open questions at the time
    • Does not explain why blood stages tolerate loss (fatty acid scavenging vs synthesis)
    • Molecular cause of merosome/merozoite formation failure not defined
  8. 2013 High

    Stage-specific expression and knockout in P. falciparum revealed a species divergence: ENR is required for sporozoite development within mosquito oocysts, distinct from the liver-stage requirement in rodent models.

    Evidence Immunofluorescence with anti-FabI antibodies, ACP colocalization, and targeted fabI deletion with mosquito-stage development assays in P. falciparum

    PMID:24297444

    Open questions at the time
    • Mechanistic basis for the oocyst-versus-liver-stage requirement difference across species unresolved
    • Downstream lipid products required at each stage not identified
  9. 2011 High

    Full kinetic dissection established the ordered mechanism of ENR and extended slow-onset inhibition to additional chemotypes, while mutagenesis linked the substrate-binding loop and a conserved salt bridge to catalytic function.

    Evidence Steady-state/pre-steady-state kinetics, fluorescence, and A372M mutagenesis with crystallography of P. falciparum ENR

    PMID:21280175 PMID:21603269

    Open questions at the time
    • Rate-limiting step and full microscopic rate constants not comprehensively reported
    • Functional consequence of loop dynamics in vivo untested
  10. 2013 Medium

    Diverse inhibitor chemotypes and structure-activity studies mapped how the ENR active site accommodates and can be tuned toward alternative scaffolds.

    Evidence Enzyme inhibition kinetics, natural-product isolation, HTS, virtual docking, and crystallography of P. falciparum ENR-inhibitor complexes (triclosan analogs, coumarins, flavonoids, oroidin, celastrol)

    PMID:12606558 PMID:16722653 PMID:17765547 PMID:20503440 PMID:24063369 PMID:25284249

    Open questions at the time
    • Several inhibitor modes rest on single-lab enzyme assays without structural follow-up (e.g. celastrol)
    • Whole-parasite and stage-specific efficacy of most chemotypes not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved why blood-stage parasites tolerate loss of ENR while transmission and liver stages depend on it, and what specific lipid products of FAS II are required at each essential stage.
  • Fatty acid products downstream of ENR not linked to a stage-specific requirement
  • Balance between de novo synthesis and host lipid scavenging across stages not defined

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
ACYL CARRIER PROTEIN (ACP) — APICOPLAST COLOCALIZATION MARKER [#8, #9]FABB/F, FABG, FABZ — CO-FUNCTIONAL FAS II ELONGATION ENZYMES [#11]
Complex memberships
FAS II elongation module (ENR/FabI with FabB/F, FabG, FabZ) reconstituted in vitro [#11]

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 ENR (enoyl-ACP reductase) purified from P. falciparum is inhibited by triclosan; incorporation of [14C]acetate and [14C]malonyl-CoA into fatty acids in vivo and in vitro was blocked by triclosan, establishing ENR as the target and confirming existence of a de novo type II fatty acid biosynthesis pathway in this parasite. Enzyme purification, in vitro fatty acid labeling assay with [14C]acetate and [14C]malonyl-CoA, enzyme inhibition assay Nature medicine High 11175846
2001 Triclosan shows competitive inhibition kinetics with respect to NADH but is uncompetitive with respect to NAD+, indicating that triclosan binding to ENR is facilitated in the presence of NAD+. Km values for crotonyl-CoA and NADH were determined as 165 µM and 33 µM, respectively. Recombinant expression in E. coli, steady-state enzyme kinetics Biochemical and biophysical research communications High 11735121
2002 Crystal structures of P. falciparum ENR were solved as a binary complex with NADH, a ternary complex with triclosan and NAD+, and ternary complexes with triclosan analogs and NADH. ENR was found to be a 50 kDa protein predicted to localize to the apicoplast. Novel structural features were identified in the binding loop region resembling bacterial homologs; the structural basis of triclosan binding was defined. Cloning, recombinant expression, protein purification, X-ray crystallography The Journal of biological chemistry High 11792710
2004 Triclosan is a slow-tight-binding inhibitor of P. falciparum ENR, following a two-step mechanism: rapid formation of a reversible enzyme-inhibitor complex (EI) that isomerizes to a tighter complex (EI*). Rate constants were ki(forward) = 5.49×10-2 s-1 and ki(reverse) = 1×10-4 s-1; Ki = 53 nM, Ki* = 96 pM. Steady-state kinetics, fluorescence spectroscopy, surface plasmon resonance The Biochemical journal High 15086316
2004 Mutational analysis of ENR active-site residues identified Ala-217, Asn-218, Met-281, and Phe-368 as critical for triclosan binding. The A217V mutation caused >7000-fold reduction in triclosan binding affinity, while A217G caused only 10-fold reduction, demonstrating the importance of steric constraints at this position. Site-directed mutagenesis, enzyme inhibition assays, binding affinity measurements The Biochemical journal High 15139852
2007 X-ray crystal structures of five triclosan analogs in complex with P. falciparum ENR revealed flexibility of the active site and a structure-activity relationship for the 5-substituent; replacement of the 5-chloro group with larger hydrophobic moieties improved inhibitory potency against purified ENR (IC50 < 200 nM). X-ray crystallography of ENR-inhibitor complexes, enzyme inhibition assays, in vitro parasite growth inhibition The Journal of biological chemistry High 17567585
2007 Crystal structures of P. falciparum ENR in complex with NAD+ and triclosan were solved to 2.2 Å. Structural comparison with T. gondii ENR revealed that although active sites are broadly similar to bacterial counterparts, differences in the drug-binding pocket reduce packing interactions with several inhibitors, explaining lower affinity of apicomplexan ENR for aminopyridine-based inhibitors. X-ray crystallography Acta crystallographica. Section D, Biological crystallography High 17327670
2008 Deletion of fabI in P. falciparum did not impede asexual blood-stage growth, but FabI-deficient P. berghei sporozoites were markedly less infective for mice and failed to complete liver-stage development in vitro, specifically failing to form intrahepatic merosomes. This established that ENR is essential for liver-stage but not blood-stage development. Targeted gene deletion (knockout) in P. falciparum and P. berghei, mouse infection model, in vitro liver-stage development assay Cell host & microbe High 19064257
2008 FAS II enzymes including ENR (FabI) localize to the sporozoite and liver-stage apicoplast in P. yoelii. Targeted deletion of fabI (FabI) in P. falciparum confirmed no reduction in asexual blood-stage replication. FAS II-deficient P. yoelii liver stages failed to form exo-erythrocytic merozoites, establishing that ENR function is required for the liver-to-blood transition. Targeted gene deletion, fluorescence localization (apicoplast colocalization), mouse liver-stage infection model Cellular microbiology High 19068099
2013 In P. falciparum, ENR (FabI) protein is expressed in mosquito midgut oocysts and sporozoites and in liver-stage parasites but not during blood stages. FabI colocalizes with apicoplast-targeted acyl carrier protein in these stages. Targeted deletion of fabI abolished sporozoite development within the midgut oocyst, revealing that FAS II is essential for P. falciparum sporozoite development — an important distinction from rodent malaria models where FAS II is required in liver stage but not oocyst stage. Immunofluorescence with anti-FabI antibodies, colocalization with ACP (apicoplast marker), targeted gene deletion, mosquito stage development assay Eukaryotic cell High 24297444
2007 Flavonoids including luteolin and (-)-catechin gallate act as tight-binding noncompetitive inhibitors of P. falciparum ENR (FabI), as established by kinetic analysis. FabG was inhibited noncompetitively and FabZ competitively by the same compounds, demonstrating distinct inhibition modes for each FAS II enzyme. Enzyme inhibition kinetics with purified recombinant enzymes, in vitro parasite growth assay Journal of medicinal chemistry Medium 16722653
2007 In vitro reconstitution of the complete FAS II elongation module of P. falciparum — including ENR (FabI) together with FabB/F, FabG, and FabZ — demonstrated that these four enzymes are sufficient to reconstitute fatty acid chain elongation from butyryl-ACP. Inhibition of ENR by triclosan or NAS-21/91 caused accumulation of the substrate intermediate detectable by MALDI-TOF MS, confirming ENR's role as the terminal reductive step in each elongation cycle. In vitro reconstitution of multienzyme pathway, MALDI-TOF mass spectrometry Antimicrobial agents and chemotherapy High 17485508
2003 Novel inhibitor classes (identified by high-throughput screening) inhibit P. falciparum ENR enzyme activity without requiring metabolic activation, and are effective against wild-type and drug-resistant P. falciparum strains. Crystal structure of the M. tuberculosis ENR homolog (InhA) with one inhibitor revealed a unique stoichiometry where either one or two triclosan molecules could bind the active site. High-throughput enzyme inhibition screen, X-ray crystallography (InhA), in vitro parasite growth assay The Journal of biological chemistry Medium 12606558
2008 (E)-Oroidin from the marine sponge Agelas oroides is an uncompetitive inhibitor of P. falciparum ENR with Ki values of 0.4 ± 0.2 µM (with respect to substrate) and 0.8 ± 0.2 µM (with respect to cofactor). Delta5,9 fatty acid mixtures also inhibit PfENR with IC50 ≈ 0.35 µg/ml. Activity-guided isolation, enzyme kinetic inhibition studies with purified PfENR Bioorganic & medicinal chemistry Medium 17765547
2011 Mutation of Ala372 in the substrate-binding loop of P. falciparum ENR to Met (A372M) increased affinity for triclosan approximately twofold and introduced a more hydrophobic environment resembling E. coli ENR. Crystal structure of the A372M mutant confirmed altered active-site contacts. Mutations disrupting a conserved salt bridge that stabilizes the substrate-binding loop caused loss of function, except when an alternative water-bridge network was formed. Site-directed mutagenesis, X-ray crystallography, enzyme kinetics IUBMB life High 21280175
2011 Steady-state kinetics, pre-steady-state kinetics, and equilibrium fluorescence spectroscopy established the ordered kinetic mechanism of P. falciparum ENR, and showed that a pentacyano(isoniazid)ferrateII inorganic complex inhibits ENR with slow-onset kinetics. Steady-state kinetics, pre-steady-state kinetics, equilibrium fluorescence spectroscopy Enzyme research Medium 21603269
2010 X-ray crystal structures of P. falciparum ENR complexed with multiple triclosan variants revealed that substitutions at 4' and 2' positions increase interactions with the protein, cofactor, and solvent. Substitution at the 2' position relocates a conserved water molecule, creating an additional hydrogen bond. Unsubstituted 2'/4' compounds shift position within the hydrophobic pocket to compensate for lost halogen interactions. X-ray crystallography, in vitro parasite culture inhibition assay IUBMB life Medium 20503440
2013 Crystal structures of two coumarin-based triclosan analogs (compounds 7 and 11) in complex with P. falciparum ENR confirmed their binding mode within the active site and validated docking predictions, establishing structure-activity relationships for this inhibitor class. X-ray crystallography of ENR-inhibitor complexes, enzyme inhibition assays Journal of medicinal chemistry Medium 24063369
2014 Celastrol was identified as a noncompetitive, low-micromolar inhibitor of P. falciparum ENR in an in vitro activity assay, demonstrating a mode of inhibition distinct from triclosan. Structure-based virtual docking, in vitro enzyme activity assay Bioorganic & medicinal chemistry Low 25284249

Source papers

Stage 0 corpus · 46 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nature medicine 356 11175846
2008 Type II fatty acid synthesis is essential only for malaria parasite late liver stage development. Cellular microbiology 316 19068099
2008 The fatty acid biosynthesis enzyme FabI plays a key role in the development of liver-stage malarial parasites. Cell host & microbe 236 19064257
2003 Targeting tuberculosis and malaria through inhibition of Enoyl reductase: compound activity and structural data. The Journal of biological chemistry 209 12606558
2002 Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. The Journal of biological chemistry 177 11792710
2001 Triclosan inhibits the growth of Plasmodium falciparum and Toxoplasma gondii by inhibition of apicomplexan Fab I. International journal for parasitology 163 11239932
2006 Inhibition of Plasmodium falciparum fatty acid biosynthesis: evaluation of FabG, FabZ, and FabI as drug targets for flavonoids. Journal of medicinal chemistry 152 16722653
2007 New advances in fatty acids as antimalarial, antimycobacterial and antifungal agents. Progress in lipid research 129 18023422
2013 Type II fatty acid biosynthesis is essential for Plasmodium falciparum sporozoite development in the midgut of Anopheles mosquitoes. Eukaryotic cell 121 24297444
2007 Marine natural products from the Turkish sponge Agelas oroides that inhibit the enoyl reductases from Plasmodium falciparum, Mycobacterium tuberculosis and Escherichia coli. Bioorganic & medicinal chemistry 94 17765547
2004 Inhibiting activities of the secondary metabolites of Phlomis brunneogaleata against parasitic protozoa and plasmodial enoyl-ACP Reductase, a crucial enzyme in fatty acid biosynthesis. Planta medica 90 15326547
2001 Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors. Biochemical and biophysical research communications 65 11735121
2004 Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan. The Biochemical journal 60 15086316
2007 X-ray structural analysis of Plasmodium falciparum enoyl acyl carrier protein reductase as a pathway toward the optimization of triclosan antimalarial efficacy. The Journal of biological chemistry 56 17567585
2006 Novel diphenyl ethers: design, docking studies, synthesis and inhibition of enoyl ACP reductase of Plasmodium falciparum and Escherichia coli. Bioorganic & medicinal chemistry 55 16893651
2005 Anti-protozoal and plasmodial FabI enzyme inhibiting metabolites of Scrophularia lepidota roots. Phytochemistry 54 15680992
2007 Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents. Acta crystallographica. Section D, Biological crystallography 42 17327670
2004 Mutational analysis of the triclosan-binding region of enoyl-ACP (acyl-carrier protein) reductase from Plasmodium falciparum. The Biochemical journal 41 15139852
2006 Turkish freshwater and marine macrophyte extracts show in vitro antiprotozoal activity and inhibit FabI, a key enzyme of Plasmodium falciparum fatty acid biosynthesis. Phytomedicine : international journal of phytotherapy and phytopharmacology 37 16697632
2007 Discovery of novel inhibitors targeting enoyl-acyl carrier protein reductase in Plasmodium falciparum by structure-based virtual screening. Biochemical and biophysical research communications 32 17509532
2003 Expression, purification and crystallization of the Plasmodium falciparum enoyl reductase. Acta crystallographica. Section D, Biological crystallography 30 12832774
2013 Potential of lichen secondary metabolites against Plasmodium liver stage parasites with FAS-II as the potential target. Journal of natural products 25 23806111
2013 Design, synthesis, and biological and crystallographic evaluation of novel inhibitors of Plasmodium falciparum enoyl-ACP-reductase (PfFabI). Journal of medicinal chemistry 24 24063369
2008 Inhibiting enoyl-ACP reductase (FabI) across pathogenic microorganisms by linear sesquiterpene lactones from Anthemis auriculata. Phytomedicine : international journal of phytotherapy and phytopharmacology 24 18424102
2007 Mass spectrometry-based systems approach for identification of inhibitors of Plasmodium falciparum fatty acid synthase. Antimicrobial agents and chemotherapy 21 17485508
2013 Novel type II fatty acid biosynthesis (FAS II) inhibitors as multistage antimalarial agents. ChemMedChem 20 23341167
2010 X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition. IUBMB life 20 20503440
2008 New method for the assessment of all drug-like pockets across a structural genome. Journal of computational biology : a journal of computational molecular cell biology 17 18333758
2015 In silico identification of genetically attenuated vaccine candidate genes for Plasmodium liver stage. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases 16 26348884
2010 SAR and pharmacophore models for the rhodanine inhibitors of Plasmodium falciparum enoyl-acyl carrier protein reductase. IUBMB life 16 20131353
2014 Celastrol inhibits Plasmodium falciparum enoyl-acyl carrier protein reductase. Bioorganic & medicinal chemistry 15 25284249
2009 Molecular modeling studies, synthesis, and biological evaluation of Plasmodium falciparum enoyl-acyl carrier protein reductase (PfENR) inhibitors. Molecular diversity 15 19347595
2005 Evaluation of antiprotozoal and plasmodial enoyl-ACP reductase inhibition potential of turkish medicinal plants. Phytotherapy research : PTR 14 15852483
2014 Compound prioritization from inverse docking experiment using receptor-centric and ligand-centric methods: a case study on Plasmodium falciparum Fab enzymes. Journal of molecular recognition : JMR 13 24591179
2012 Dynamics of Plasmodium falciparum enoyl-ACP reductase and implications on drug discovery. Protein science : a publication of the Protein Society 11 22969045
2008 Malaria pulls a FASt one. Cell host & microbe 11 19064250
2013 Development of a triclosan scaffold which allows for adaptations on both the A- and B-ring for transport peptides. Bioorganic & medicinal chemistry letters 9 23664871
2023 Structure-Based Design and Pharmacophore-Based Virtual Screening of Combinatorial Library of Triclosan Analogues Active against Enoyl-Acyl Carrier Protein Reductase of Plasmodium falciparum with Favourable ADME Profiles. International journal of molecular sciences 8 37108083
2020 Identification of novel antiplasmodial compound by hierarquical virtual screening and in vitro assays. Journal of biomolecular structure & dynamics 8 32364060
2009 Design, development, synthesis, and docking analysis of 2'-substituted triclosan analogs as inhibitors for Plasmodium falciparum enoyl-ACP reductase. IUBMB life 8 19859979
2013 Design, synthesis, structural characterization by IR, (1) H, (13) C, (15) N, 2D-NMR, X-ray diffraction and evaluation of a new class of phenylaminoacetic acid benzylidene hydrazines as pfENR inhibitors. Chemical biology & drug design 7 23398677
2011 Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from Plasmodium falciparum. IUBMB life 6 21280175
2015 Combined 3D-QSAR and Molecular Docking Study for Identification of Diverse Natural Products as Potent Pf ENR Inhibitors. Current computer-aided drug design 5 26517356
2011 Enzyme Mechanism and Slow-Onset Inhibition of Plasmodium falciparum Enoyl-Acyl Carrier Protein Reductase by an Inorganic Complex. Enzyme research 4 21603269
2026 Integrated molecular docking, toxicity prediction, and molecular dynamics simulations studies to identify potential antimalarial candidates targeting enoyl-acyl carrier protein reductase enzyme. In silico pharmacology 0 42614364
2022 Identification of natural products against enoyl-acyl-carrier-protein reductase in malaria via combined pharmacophore modeling, molecular docking and simulations studies. Journal of biomolecular structure & dynamics 0 35043754