Regulation of phospho-2-keto-3-deoxy-heptonate aldolase (DAHP synthase) and anthranilate synthase of Pseudomonas aureofaciens.
Phospho-2-keto-3-deoxy-heptonate aldolase (DAHP synthase) of Pseudomonas aureofaciens ATCC 15926 was inhibited by L-tyrosine. The inhibition was competitive with erythrose 4-phosphate as the varied substrate but non-competitive with respect to phosphoenolpyruvate. Anthranilate synthase was inhibited by L-tryptophan. The inhibition was competitive with respect to chorismate but non-competitive with L-glutamine or NH4+ as the varied substrate. DAHP synthase and anthranilate synthase were not repressed when aromatic amino acids were included in the growth medium. In bacteria grown in the presence of L-phenylalanine, the anthranilate synthase activity was enhanced about threefold compared with the control. Similar results were obtained with the mutant strain P. aureofaciens ACN, which produces increased amounts of pyrrolnitrin.
D010723:3-Deoxy-7-Phosphoheptulonate Synthase / Q000378:metabolism*; D000446:Aldehyde-Lyases / Q000378:metabolism*; D000878:Anthranilate Synthase / Q000378:metabolism; D000935:Antifungal Agents / Q000096:biosynthesis; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D014364:Tryptophan / Q000378:metabolism
D000935:Antifungal Agents; D014364:Tryptophan; D010723:3-Deoxy-7-Phosphoheptulonate Synthase; D000446:Aldehyde-Lyases; D000878:Anthranilate Synthase