EC Number |
General Information |
Reference |
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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 | 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 |
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 | 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 |
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 |
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 | 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 | 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 |
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 |