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Literature summary for 4.1.3.27 extracted from

  • Palmer, G.C.; Jorth, P.A.; Whiteley, M.
    The role of two Pseudomonas aeruginosa anthranilate synthases in tryptophan and quorum signal production (2013), Microbiology, 159, 959-969.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.3.27

Cloned(Commentary)

Cloned (Comment) Organism
gene phnAB, phylogenetic analysis, cloning in Escherichia coli strain Dh5alpha, enzyme expression in an enzyme-deficient Pseudomonas aeruginosa strain. Overexpression of anthranilate synthase genes trpE and phnAB results in pathway crosstalk, overview Pseudomonas aeruginosa
gene trpE, phylogenetic analysis, cloning in Escherichia coli strain Dh5alpha, enzyme expression in an enzyme-deficient Pseudomonas aeruginosa strain. Overexpression of anthranilate synthase genes trpE and phnAB results in pathway crosstalk, overview Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
additional information construction of several different trpE and phnAB knockout mutants. DELTAtrpE tryptophan auxotrophy is dependent upon phnAB expression. Overexpression of either anthranilate synthase complements the loss of the other Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa P09785 and P09786 anthranilate synthase phnAB, composed of glutamine amidotransferase component phnB (P09786) and anthranilate synthase component pyocyanine-specific phnA (P09785)
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Pseudomonas aeruginosa P20576 and P20580 anthranilate synthase TrpEG, composed of glutamine amidotransferase component trpG (P20576) and anthanilate synthase component trpE (P20580); PA14, genes trpG, trpE
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Synonyms

Synonyms Comment Organism
PhnAB
-
 Pseudomonas aeruginosa
TrpE
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 Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution TrpE and PhnA sequences reveal the evolutionary relationships of each anthranilate synthase enzyme to those of other species, phylogenetic analysis and tree, overview. TrpEG are most closely related to anthranilate synthases from other members of the fluorescent pseudomonad family, while PhnAB are most closely related to anthranilate synthases from more distantly related organisms. The absence of a phnAB-like operon in other pseudomonads is evidence that PhnAB acquisition occurred after the family's diversification Pseudomonas aeruginosa
malfunction phnAB mutants are tryptophan prototrophs but do not produce Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone in minimal media Pseudomonas aeruginosa
malfunction trpEG mutants are tryptophan auxotrophs but produce Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone Pseudomonas aeruginosa
metabolism Pseudomonas aeruginosa possesses two functional anthranilate synthases, TrpEG and PhnAB, and these enzymes are not functionally redundant. They are involved in biosynthesis of Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone, which regulates density-dependent production of toxic factors involved in Pseudomonas aeruginosa virulence. TrpED catalyzes the first step in tryptophan biosynthesis Pseudomonas aeruginosa
metabolism Pseudomonas aeruginosa possesses two functional anthranilate synthases, TrpEG and PhnAB, and these enzymes are not functionally redundant. They are involved in biosynthesis of Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone, which regulates density-dependent production of toxic factors involved Pseudomonas aeruginosa virulence. TrpED catalyzes the first step in tryptophan biosynthesis Pseudomonas aeruginosa
physiological function conversion of the central metabolite chorismate to anthranilate by anthranilate synthase is required for Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone, PQS, biosynthesis. The reaction is also the first step in tryptophan biosynthesis Pseudomonas aeruginosa