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Literature summary extracted from

  • Baum, B.; Lecker, L.S.; Zoltner, M.; Jaenicke, E.; Schnell, R.; Hunter, W.N.; Brenk, R.
    Structures of Pseudomonas aeruginosa beta-ketoacyl-(acyl-carrier-protein) synthase II (FabF) and a C164Q mutant provide templates for antibacterial drug discovery and identify a buried potassium ion and a ligand-binding site that is an artefact of the crysta (2015), Acta Crystallogr. Sect. F, 71, 1020-1026.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.3.1.179 drug development the enzyme is an antibiotic target in Gram-positive bacteria and might also be a target in Gram-negative bacteria Pseudomonas aeruginosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.179 gene fabF, recombinant wild-type and mutant N-terminally His6-tagged enzyme expressions from vector pNIC28-Bsa4 including a TEV cleavage site in Escherichia coli strain BL21(DE3)pLysS Pseudomonas aeruginosa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.179 purified recombinant free wild-type enzyme, and mutant C164Q enzyme, free or in complex with 3-(benzoylamino)-2-hydroxybenzoic acid, mixing of 0.001 ml of 20 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, with 0.001 ml reservoir solution containing 0.2 M MgCl2, 0.1 M Tris-HCl, pH 7.0, 10% w/v PEG 8000 for the wild-type enzyme, or 0.001 ml of 20 mg/ml protein in 50 mM Na2HPO4, pH 7.8, 150 mM NaCl, 10% v/v glycerol, and 0.5 mM DTT with 0.001 ml of reservoir consisting of 0.2 M NH4HCO2, 25% w/v PEG 3350 for the mutant enzyme, equilibration against 0.06 ml reservoir solution, at 20°C, X-ray diffraction structure determination and analysis at 1.67-2.46 A resolution, molecular replacement Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.179 C164Q site-directed mutagenesis, a mutant in which the binding site is altered to resemble the substrate-bound state Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.179 3-(benzoylamino)-2-hydroxybenzoic acid binds outside the active site of the enzyme, binding structure with wild-type and C164Q mutant enzymes, overview. Access to the depths of the active site of the PaFabF apoenzyme is restricted by the conformations of Phe230 and Phe400. 3-(benzoylamino)-2-hydroxybenzoic acid/Mg2+ ion pair selectively binds into and perhaps contributes to the formation of a stable binding site on the surface of the enzyme distant from the active site, from which it is likely to be occluded by steric hindrance Pseudomonas aeruginosa
2.3.1.179 platensimycin a natural product inhibitor Pseudomonas aeruginosa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.179 55000
-
 recombinant enzyme, gel filtration Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.179 Pseudomonas aeruginosa G3XDA2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.179 recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinit chromatography, tag cleavage through TEV, dialysis, and gel filtration Pseudomonas aeruginosa

Subunits

EC Number Subunits Comment Organism
2.3.1.179 dimer
-
 Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
2.3.1.179 3-oxoacyl-ACP synthase II
-
 Pseudomonas aeruginosa
2.3.1.179 beta-ketoacyl-(acyl-carrier-protein) synthase II
-
 Pseudomonas aeruginosa
2.3.1.179 FabF
-
 Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
2.3.1.179 metabolism the enzyme is involved in fatty-acid biosynthesis Pseudomonas aeruginosa
2.3.1.179 additional information active site structure of wild-type and mutant enzymes, ligand binding structures, overview Pseudomonas aeruginosa
2.3.1.179 physiological function the enzyme is involved in fatty-acid biosynthesis Pseudomonas aeruginosa