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Literature summary extracted from

  • ORourke, P.E.; Eadsforth, T.C.; Fyfe, P.K.; Shepherd, S.M.; Hunter, W.N.
    Pseudomonas aeruginosa 4-amino-4-deoxychorismate lyase: spatial conservation of an active site tyrosine and classification of two types of enzyme (2011), PLoS ONE, 6, e24158.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.1.3.38 drug development the absence of the enzyme in humans and its essentiality in various microbes suggests that inhibition of PabC offers the possibility of therapeutics targeting a range of microbial infections, potential of this protein for early stage drug discovery Pseudomonas aeruginosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.38 gene pabC, expression of His6-tagged enzyme with TEV protease cleavage site in Escherichia coli strain BL21(DE3) GOLD Pseudomonas aeruginosa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.3.38 purified recombinant detagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 33 mg/mL prrotein in 100 mM HEPES, pH 7.5, 500 mM NaCl, 0.1 mM pyridoxal 5'-phosphate, and 10 mM 4-aminobenzoate, with 0001 ml of reservoir solution containing 10% w/v PEG 400, 1.8 M ammonium sulfate and 100 mM MES, pH 6.5, 20°C, 1 week, X-ray diffraction structure dtermination and analysis at 1.75 A resolution Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.38 4-amino-4-deoxychorismate Pseudomonas aeruginosa
-
 4-aminobenzoate + pyruvate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.38 Pseudomonas aeruginosa Q9HZN6 gene pabC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.38 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) GOLD by nickel affinity chromatography, cleavage of the tag by TEV protease, and gel filtration Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.38 4-amino-4-deoxychorismate
-
 Pseudomonas aeruginosa 4-aminobenzoate + pyruvate
-
 ?
4.1.3.38 4-amino-4-deoxychorismate molecular modeling of the catalytic intermediate, overview Pseudomonas aeruginosa 4-aminobenzoate + pyruvate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.3.38 dimer sequence comparisons, structure modeling of the catalytic intermediate and ligand-bound enzyme, overview Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
4.1.3.38 4-amino-4-deoxychorismate lyase
-
 Pseudomonas aeruginosa
4.1.3.38 PabC
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.3.38 pyridoxal 5'-phosphate dependent on, the PLP methyl group makes van der Waals interactions with Gln147 and is positioned 3.2 A distant from the carbonyl oxygen of Val175, Ser237 interacts with the pyridoxal 5'-phosphate phosphate Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
4.1.3.38 evolution structure comparisons with related enzymes, overview. PabC enzymes can be classified into two groups depending upon whether an active site and structurally conserved tyrosine is provided from the polypeptide that mainly forms an active site or from the partner subunit in the dimeric assembly Pseudomonas aeruginosa
4.1.3.38 additional information structure-activity relationship of PabC, ligand binding modeling and reaction mechanism, overview. No structure of PabC in complex with ligands is achieved, but a computational model of the catalytic intermediate docked into the enzyme active site is generated. A conserved tyrosine helps to create a hydrophobic wall on one side of the active site that provides important interactions to bind the catalytic intermediate, but it does not appear to participate in interactions with the C atom that undergoes an sp2 to sp3 conversion as pyruvate is produced. An active site threonine hydroxyl contributes a proton used in the reduction of the substrate methylene to pyruvate methyl in the final stage of the mechanism Pseudomonas aeruginosa
4.1.3.38 physiological function the enzyme is active in folate biosynthesis and essential for the cell growth of the pathogen Pseudomonas aeruginosa