EC Number |
General Information |
Reference |
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4.1.3.27 | 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 |
728263 |
4.1.3.27 | malfunction |
mutation in strain trpD9923 (mutant in the tryptophan operon) results in the synthesis of a truncated anthranilate synthase component II protein, retaining the full glutamine amidotransferase domain and only seven of the 333 amino acid residues of the anthranilate phosphoribosyl transferase domain. Mutation in the trpD gene causes the loss of anthranilate phosphoribosyl transferase activity, but maintains anthranilate synthase activity, thus causing anthranilate accumulation |
-, 705533 |
4.1.3.27 | malfunction |
phnAB mutants are tryptophan prototrophs but do not produce Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone in minimal media |
728263 |
4.1.3.27 | malfunction |
trpEG mutants are tryptophan auxotrophs but produce Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone |
728263 |
4.1.3.27 | malfunction |
Virus-induced gene silencing of HvCS, HvASa2, and HvCM1 increase formation of Blumeria graminis f. sp. hordei secondary hyphae but not conidiation in Mla6-mediated resistant plants |
705812 |
4.1.3.27 | metabolism |
anthranilate synthase functions as rate-limiting factor for the biosynthesis of pyrroloquinazoline alkaloids |
749037 |
4.1.3.27 | 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 |
728263 |
4.1.3.27 | 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 |
728263 |
4.1.3.27 | metabolism |
the enzyme catalyzes the initial step in the pathway for both tryptophan-dependent and tryptophan-independent pathways in the biosynthesis of indole-3-acetic acid, the transfer of the alpha-amino group of glutamine to chorismate producing anthranilate |
728052 |
4.1.3.27 | more |
the enzyme shows a mechanism of this tight activity regulation, catalytic Cys-His-Glu triad, molecular dynamics simulations, overview |
718925 |