[Regulation of 3-desoxy-D-arabino-heptulosonate-7-phosphate synthetase in the bacteria Pseudomonas aurantiaca B-162].
The regulation of activity and synthesis of DAHP-synthase in Pseudomonas aurantiaca B-162 was studied. Analysis of partially purified preparations of the enzyme revealed two isoenzymes: DAHP-synthase [tyr] and DAHP-synthase [phe], each of them being regulated by a corresponding amino acid. DAHP-synthase [tyr] is a dominant isoenzyme presenting 78 % of the enzyme activity, 50 % inhibition of which is possible by 1,3 x 10(-5) M of tyrosine. DAHP-synthase [phe] is minor isoenzyme (sharing 22 % of enzyme activity) and is controlled by phenylalanine. In this case, 50% of inhibition of activity is possible by adding 5,5 10(-6) M of corresponding amino acid. Synthesis of DAHP-synthase is constitutive.
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D010723:3-Deoxy-7-Phosphoheptulonate Synthase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007527:Isoenzymes / Q000378:metabolism; D009154:Mutation; D010649:Phenylalanine / Q000494:pharmacology; D011549:Pseudomonas / Q000201:enzymology*; D014443:Tyrosine / Q000494:pharmacology
D004791:Enzyme Inhibitors; D007527:Isoenzymes; D014443:Tyrosine; D010649:Phenylalanine; D010723:3-Deoxy-7-Phosphoheptulonate Synthase