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	additional information	the enzyme shows a mechanism of this tight activity regulation, catalytic Cys-His-Glu triad, molecular dynamics simulations, overview	718925	
4.1.3.27	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	728263	
4.1.3.27	physiological function	enhanced cellular glutamine may account for the enhanced growth in glutamine synthase-expressing transgenic poplar plants through the regulation of auxin biosynthesis	728052	
4.1.3.27	physiological function	enzyme activity is required for indole-3-butyric acid-induced adventitious root formation	747430	
4.1.3.27	physiological function	plastid transformed lines exhibit a higher level of anthranilate synthase activity that is less sensitive to tryptophan-feedback inhibition and, consequently, increases free tryptophan levels in leaves about 7fold. Overexpression of ASA2 gene does not result in any negative effects for the plants	704881	
4.1.3.27	physiological function	role of HvCS, HvASa2, and HvCM1 in penetration resistance to Blumeria graminis f. sp.hordei. HvCS, HvCM1, and HvASa2 contribute to mlo-mediated broad-spectrum resistance	705812